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23 results on '"Truman, Andrew"'

1. Editorial: A new chapter for Cell Stress and Chaperones

Author

Bourboulia, Dimitra, Blair, Laura J., Clark, Melody S., Edkins, Adrienne L., Hightower, Lawrence E., Mollapour, Mehdi, Prahlad, Veena, Repasky, Elizabeth A., Truebano, Manuela, Truman, Andrew W., Truttmann, Matthias C., van Oosten-Hawle, Patricija, Woodford, Mark R., Bourboulia, Dimitra, Blair, Laura J., Clark, Melody S., Edkins, Adrienne L., Hightower, Lawrence E., Mollapour, Mehdi, Prahlad, Veena, Repasky, Elizabeth A., Truebano, Manuela, Truman, Andrew W., Truttmann, Matthias C., van Oosten-Hawle, Patricija, and Woodford, Mark R.

Published
2024

2. Complete biosynthesis of the potent vaccine adjuvant QS-21

Author

Martin, Laetitia BB, Martin, Laetitia BB, Kikuchi, Shingo, Rejzek, Martin, Owen, Charlotte, Reed, James, Orme, Anastasia, Misra, Rajesh C, El-Demerdash, Amr, Hill, Lionel, Hodgson, Hannah, Liu, Yuzhong, Keasling, Jay D, Field, Robert A, Truman, Andrew W, Osbourn, Anne, Martin, Laetitia BB, Martin, Laetitia BB, Kikuchi, Shingo, Rejzek, Martin, Owen, Charlotte, Reed, James, Orme, Anastasia, Misra, Rajesh C, El-Demerdash, Amr, Hill, Lionel, Hodgson, Hannah, Liu, Yuzhong, Keasling, Jay D, Field, Robert A, Truman, Andrew W, and Osbourn, Anne

Abstract

QS-21 is a potent vaccine adjuvant currently sourced by extraction from the Chilean soapbark tree. It is a key component of human vaccines for shingles, malaria, coronavirus disease 2019 and others under development. The structure of QS-21 consists of a glycosylated triterpene scaffold coupled to a complex glycosylated 18-carbon acyl chain that is critical for immunostimulant activity. We previously identified the early pathway steps needed to make the triterpene glycoside scaffold; however, the biosynthetic route to the acyl chain, which is needed for stimulation of T cell proliferation, was unknown. Here, we report the biogenic origin of the acyl chain, characterize the series of enzymes required for its synthesis and addition and reconstitute the entire 20-step pathway in tobacco, thereby demonstrating the production of QS-21 in a heterologous expression system. This advance opens up unprecedented opportunities for bioengineering of vaccine adjuvants, investigating structure-activity relationships and understanding the mechanisms by which these compounds promote the human immune response.

Published
2024

3. Complete biosynthesis of the potent vaccine adjuvant QS-21

Author

Martin, Laetitia B.B., Kikuchi, Shingo, Rejzek, Martin, Owen, Charlotte, Reed, James, Orme, Anastasia, Misra, Rajesh C., El-Demerdash, Amr, Hill, Lionel, Hodgson, Hannah, Liu, Yuzhong, Keasling, Jay D., Field, Robert A., Truman, Andrew W., Osbourn, Anne, Martin, Laetitia B.B., Kikuchi, Shingo, Rejzek, Martin, Owen, Charlotte, Reed, James, Orme, Anastasia, Misra, Rajesh C., El-Demerdash, Amr, Hill, Lionel, Hodgson, Hannah, Liu, Yuzhong, Keasling, Jay D., Field, Robert A., Truman, Andrew W., and Osbourn, Anne

Abstract

QS-21 is a potent vaccine adjuvant currently sourced by extraction from the Chilean soapbark tree. It is a key component of human vaccines for shingles, malaria, coronavirus disease 2019 and others under development. The structure of QS-21 consists of a glycosylated triterpene scaffold coupled to a complex glycosylated 18-carbon acyl chain that is critical for immunostimulant activity. We previously identified the early pathway steps needed to make the triterpene glycoside scaffold; however, the biosynthetic route to the acyl chain, which is needed for stimulation of T cell proliferation, was unknown. Here, we report the biogenic origin of the acyl chain, characterize the series of enzymes required for its synthesis and addition and reconstitute the entire 20-step pathway in tobacco, thereby demonstrating the production of QS-21 in a heterologous expression system. This advance opens up unprecedented opportunities for bioengineering of vaccine adjuvants, investigating structure–activity relationships and understanding the mechanisms by which these compounds promote the human immune response. (Figure presented.)

Published
2024

5. The Hsp90 requirement in the Slt2p stress-activated MAP kinase activity of yeast

Author

Truman, Andrew William

Subjects
572.633
Abstract

The Hsp90 molecular chaperone function is essential and extremely well conserved in eukaryotic organisms, yet much of the mechanism of Hsp90 action remains a mystery. This investigation set out to identify a model client protein of Hsp90 in the yeast Saccharomyces cerevisiae that would be amenable to structural and genetic analysis. Initial studies were conducted on HSF (1-583) strain, which has a C-terminally truncated heat shock transcription factor resulting in low Hsp90 expression. This mutant displayed a swollen cell phenotype that could be suppressed with osmotic stabilisation, indicating that the mutant had defective maintenance of cell wall integrity under stress conditions. This was shown to be a result of an inability to activate Rim 1p, the transcription factor regulated by the cell integrity MAP kinase pathway. Expression of the T22I mutant form of the Hsp82 isoform of Hsp90 expressed as the sole Hsp90 of the cell was also shown to generate a cell integrity defect. Unlike with HSF (1-583), this is apparent at low as well as high temperatures of growth. An interaction between Hsp82 and the MAP kinase Slt2p, the activator of RIm 1p, was demonstrated by both protein binding and two hybrid studies. This interaction was shown to be reinforced under cell wall stressing conditions and dependent on the phosphorylation status of S1t2p. The final part of this investigation revealed that mammalian BMK1 (ERK5) MAP kinase can substantially provide Slt2p MAP kinase function in yeast. We demonstrated that this BMKl protein could associate with both isoforms of Hsp90 in yeast, Hsp82 and Hsc82. Overall, the data indicated the Slt2p MAP kinase is a client protein of Hsp82, providing the first evidence for an Hsp90 involvement in activity of a member of the MAP kinase family proteins.

Published
2005

6. Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022

Author

van Oosten-Hawle, Patricija, Backe, Sarah J., Ben-Zvi, Anat, Bourboulia, Dimitra, Brancaccio, Mara, Brodsky, Jeff, Clark, Melody, Colombo, Giorgio, Cox, Marc B., de los Rios, Paolo, Echtenkamp, Frank, Edkins, Adrienne, Freeman, Brian, Goloubinoff, Pierre, Houry, Walid, Johnson, Jill, LaPointe, Paul, Li, Wei, Mezger, Valerie, Neckers, Len, Nillegoda, Nadinath B., Prahlad, Veena, Reitzel, Adam, Scherz-Shouval, Ruth, Sistonen, Lea, Tsai, Francis T. F., Woodford, Mark R., Mollapour, Mehdi, Truman, Andrew W., van Oosten-Hawle, Patricija, Backe, Sarah J., Ben-Zvi, Anat, Bourboulia, Dimitra, Brancaccio, Mara, Brodsky, Jeff, Clark, Melody, Colombo, Giorgio, Cox, Marc B., de los Rios, Paolo, Echtenkamp, Frank, Edkins, Adrienne, Freeman, Brian, Goloubinoff, Pierre, Houry, Walid, Johnson, Jill, LaPointe, Paul, Li, Wei, Mezger, Valerie, Neckers, Len, Nillegoda, Nadinath B., Prahlad, Veena, Reitzel, Adam, Scherz-Shouval, Ruth, Sistonen, Lea, Tsai, Francis T. F., Woodford, Mark R., Mollapour, Mehdi, and Truman, Andrew W.

Abstract

The Second International Symposium on Cellular and Organismal Stress Responses took place virtually on September 8-9, 2022. This meeting was supported by the Cell Stress Society International (CSSI) and organized by Patricija Van OostenHawle and Andrew Truman (University of North Carolina at Charlotte, USA) and Mehdi Mollapour (SUNY Upstate Medical University, USA). The goal of this symposium was to continue the theme from the initial meeting in 2020 by providing a platform for established researchers, new investigators, postdoctoral fellows, and students to present and exchange ideas on various topics on cellular stress and chaperones. We will summarize the highlights of the meeting here and recognize those that received recognition from the CSSI.

Published
2023
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7. Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8–9, 2022 [Meeting Review]

Author

van Oosten-Hawle, Patricija, Backe, Sarah J., Ben-Zvi, Anat, Bourboulia, Dimitra, Brancaccio, Mara, Brodsky, Jeff, Clark, Melody, Colombo, Giorgio, Cox, Marc B., De Los Rios, Paolo, Echtenkamp, Frank, Edkins, Adrienne, Freeman, Brian, Goloubinoff, Pierre, Houry, Walid, Johnson, Jill, LaPointe, Paul, Li, Wei, Mezger, Valerie, Neckers, Len, Nillegoda, Nadinath B., Prahlad, Veena, Reitzel, Adam, Scherz-Shouval, Ruth, Sistonen, Lea, Tsai, Francis T. F., Woodford, Mark R., Mollapour, Mehdi, Truman, Andrew W., van Oosten-Hawle, Patricija, Backe, Sarah J., Ben-Zvi, Anat, Bourboulia, Dimitra, Brancaccio, Mara, Brodsky, Jeff, Clark, Melody, Colombo, Giorgio, Cox, Marc B., De Los Rios, Paolo, Echtenkamp, Frank, Edkins, Adrienne, Freeman, Brian, Goloubinoff, Pierre, Houry, Walid, Johnson, Jill, LaPointe, Paul, Li, Wei, Mezger, Valerie, Neckers, Len, Nillegoda, Nadinath B., Prahlad, Veena, Reitzel, Adam, Scherz-Shouval, Ruth, Sistonen, Lea, Tsai, Francis T. F., Woodford, Mark R., Mollapour, Mehdi, and Truman, Andrew W.

Abstract

The Second International Symposium on Cellular and Organismal Stress Responses took place virtually on September 8–9, 2022. This meeting was supported by the Cell Stress Society International (CSSI) and organized by Patricija Van Oosten-Hawle and Andrew Truman (University of North Carolina at Charlotte, USA) and Mehdi Mollapour (SUNY Upstate Medical University, USA). The goal of this symposium was to continue the theme from the initial meeting in 2020 by providing a platform for established researchers, new investigators, postdoctoral fellows, and students to present and exchange ideas on various topics on cellular stress and chaperones. We will summarize the highlights of the meeting here and recognize those that received recognition from the CSSI.

Published
2023

9. Towards the sustainable discovery and development of new antibiotics

Author

Miethke, Marcus, Pieroni, Marco, Weber, Tilmann, Brönstrup, Mark, Hammann, Peter, Halby, Ludovic, Arimondo, Paola B., Glaser, Philippe, Aigle, Bertrand, Bode, Helge B., Moreira, Rui, Li, Yanyan, Luzhetskyy, Andriy, Medema, Marnix H., Pernodet, Jean-Luc, Stadler, Marc, Tormo, Jose Ruben, Genilloud, Olga, Truman, Andrew W., Weissman, Kira J., Takano, Eriko, Sabatini, Stefano, Stegmann, Evi, Brötz-Oesterhelt, Heike, Wohlleben, Wolfgang, Seemann, Myriam, Empting, Martin, Hirsch, Anna K. H., Loretz, Brigitta, Lehr, Claus-Michael, Titz, Alexander, Herrmann, Jennifer, Jaeger, Timo, Alt, Silke, Hesterkamp, Thomas, Winterhalter, Mathias, Schiefer, Andrea, Pfarr, Kenneth, Hoerauf, Achim, Graz, Heather, Graz, Michael, Lindvall, Mika, Ramurthy, Savithri, Karlén, Anders, van Dongen, Maarten, Petkovic, Hrvoje, Keller, Andreas, Peyrane, Frederic, Donadio, Stefano, Fraisse, Laurent, Piddock, Laura J. V., Gilbert, Ian H., Moser, Heinz E., Müller, Rolf, Miethke, Marcus, Pieroni, Marco, Weber, Tilmann, Brönstrup, Mark, Hammann, Peter, Halby, Ludovic, Arimondo, Paola B., Glaser, Philippe, Aigle, Bertrand, Bode, Helge B., Moreira, Rui, Li, Yanyan, Luzhetskyy, Andriy, Medema, Marnix H., Pernodet, Jean-Luc, Stadler, Marc, Tormo, Jose Ruben, Genilloud, Olga, Truman, Andrew W., Weissman, Kira J., Takano, Eriko, Sabatini, Stefano, Stegmann, Evi, Brötz-Oesterhelt, Heike, Wohlleben, Wolfgang, Seemann, Myriam, Empting, Martin, Hirsch, Anna K. H., Loretz, Brigitta, Lehr, Claus-Michael, Titz, Alexander, Herrmann, Jennifer, Jaeger, Timo, Alt, Silke, Hesterkamp, Thomas, Winterhalter, Mathias, Schiefer, Andrea, Pfarr, Kenneth, Hoerauf, Achim, Graz, Heather, Graz, Michael, Lindvall, Mika, Ramurthy, Savithri, Karlén, Anders, van Dongen, Maarten, Petkovic, Hrvoje, Keller, Andreas, Peyrane, Frederic, Donadio, Stefano, Fraisse, Laurent, Piddock, Laura J. V., Gilbert, Ian H., Moser, Heinz E., and Müller, Rolf

Abstract

An ever-increasing demand for novel antimicrobials to treat life-threatening infections caused by the global spread of multidrug-resistant bacterial pathogens stands in stark contrast to the current level of investment in their development, particularly in the fields of natural-product-derived and synthetic small molecules. New agents displaying innovative chemistry and modes of action are desperately needed worldwide to tackle the public health menace posed by antimicrobial resistance. Here, our consortium presents a strategic blueprint to substantially improve our ability to discover and develop new antibiotics. We propose both short-term and long-term solutions to overcome the most urgent limitations in the various sectors of research and funding, aiming to bridge the gap between academic, industrial and political stakeholders, and to unite interdisciplinary expertise in order to efficiently fuel the translational pipeline for the benefit of future generations.

Published
2021
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10. Reproducible molecular networking of untargeted mass spectrometry data using GNPS

Author

Aron, Allegra T., Gentry, Emily C., McPhail, Kerry L., Nothias, Louis Félix, Nothias-Esposito, Mélissa, Bouslimani, Amina, Petras, Daniel, Gauglitz, Julia M., Sikora, Nicole, Vargas, Fernando, van der Hooft, Justin J.J., Ernst, Madeleine, Kang, Kyo Bin, Aceves, Christine M., Caraballo-Rodríguez, Andrés Mauricio, Koester, Irina, Weldon, Kelly C., Bertrand, Samuel, Roullier, Catherine, Sun, Kunyang, Tehan, Richard M., Boya P, Cristopher A., Christian, Martin H., Gutiérrez, Marcelino, Ulloa, Aldo Moreno, Tejeda Mora, Javier Andres, Mojica-Flores, Randy, Lakey-Beitia, Johant, Vásquez-Chaves, Victor, Zhang, Yilue, Calderón, Angela I., Tayler, Nicole, Keyzers, Robert A., Tugizimana, Fidele, Ndlovu, Nombuso, Aksenov, Alexander A., Jarmusch, Alan K., Schmid, Robin, Truman, Andrew W., Bandeira, Nuno, Wang, Mingxun, Dorrestein, Pieter C., Aron, Allegra T., Gentry, Emily C., McPhail, Kerry L., Nothias, Louis Félix, Nothias-Esposito, Mélissa, Bouslimani, Amina, Petras, Daniel, Gauglitz, Julia M., Sikora, Nicole, Vargas, Fernando, van der Hooft, Justin J.J., Ernst, Madeleine, Kang, Kyo Bin, Aceves, Christine M., Caraballo-Rodríguez, Andrés Mauricio, Koester, Irina, Weldon, Kelly C., Bertrand, Samuel, Roullier, Catherine, Sun, Kunyang, Tehan, Richard M., Boya P, Cristopher A., Christian, Martin H., Gutiérrez, Marcelino, Ulloa, Aldo Moreno, Tejeda Mora, Javier Andres, Mojica-Flores, Randy, Lakey-Beitia, Johant, Vásquez-Chaves, Victor, Zhang, Yilue, Calderón, Angela I., Tayler, Nicole, Keyzers, Robert A., Tugizimana, Fidele, Ndlovu, Nombuso, Aksenov, Alexander A., Jarmusch, Alan K., Schmid, Robin, Truman, Andrew W., Bandeira, Nuno, Wang, Mingxun, and Dorrestein, Pieter C.

Abstract

Global Natural Product Social Molecular Networking (GNPS) is an interactive online small molecule–focused tandem mass spectrometry (MS2) data curation and analysis infrastructure. It is intended to provide as much chemical insight as possible into an untargeted MS2 dataset and to connect this chemical insight to the user’s underlying biological questions. This can be performed within one liquid chromatography (LC)-MS2 experiment or at the repository scale. GNPS-MassIVE is a public data repository for untargeted MS2 data with sample information (metadata) and annotated MS2 spectra. These publicly accessible data can be annotated and updated with the GNPS infrastructure keeping a continuous record of all changes. This knowledge is disseminated across all public data; it is a living dataset. Molecular networking—one of the main analysis tools used within the GNPS platform—creates a structured data table that reflects the molecular diversity captured in tandem mass spectrometry experiments by computing the relationships of the MS2 spectra as spectral similarity. This protocol provides step-by-step instructions for creating reproducible, high-quality molecular networks. For training purposes, the reader is led through a 90- to 120-min procedure that starts by recalling an example public dataset and its sample information and proceeds to creating and interpreting a molecular network. Each data analysis job can be shared or cloned to disseminate the knowledge gained, thus propagating information that can lead to the discovery of molecules, metabolic pathways, and ecosystem/community interactions.

Published
2020

11. Rapid deacetylation of yeast Hsp70 mediates the cellular response to heat stress.

Author

Xu, Linan, Nitika, Hasin, Naushaba, Cuskelly, Daragh, Wolfgeher, Donald, Doyle, Sean, Moynagh, Paul N., Perrett, Sarah, Jones, Gary W., Truman, Andrew W., Xu, Linan, Nitika, Hasin, Naushaba, Cuskelly, Daragh, Wolfgeher, Donald, Doyle, Sean, Moynagh, Paul N., Perrett, Sarah, Jones, Gary W., and Truman, Andrew W.

Abstract

Hsp70 is a highly conserved molecular chaperone critical for the folding of new and denatured proteins. While traditional models state that cells respond to stress by upregulating inducible HSPs, this response is relatively slow and is limited by transcriptional and translational machinery. Recent studies have identifed a number of post-translational modifcations (PTMs) on Hsp70 that act to fne-tune its function. We utilized mass spectrometry to determine whether yeast Hsp70 (Ssa1) is diferentially modifed upon heat shock. We uncovered four lysine residues on Ssa1, K86, K185, K354 and K562 that are deacetylated in response to heat shock. Mutation of these sites cause a substantial remodeling of the Hsp70 interaction network of co-chaperone partners and client proteins while preserving essential chaperone function. Acetylation/deacetylation at these residues alter expression of other heat-shock induced chaperones as well as directly infuencing Hsf1 activity. Taken together our data suggest that cells may have the ability to respond to heat stress quickly though Hsp70 deacetylation, followed by a slower, more traditional transcriptional response.

Published
2019

12. Minimum Information about a Biosynthetic Gene cluster: commentary

Author

Medema, Marnix H, Kottmann, Renzo, Yilmaz, Pelin, Cummings, Matthew, Biggins, John B, Blin, Kai, de Bruijn, Irene, Chooi, Yit Heng, Claesen, Jan, Coates, R Cameron, Cruz-Morales, Pablo, Duddela, Srikanth, Dusterhus, Stephanie, Edwards, Daniel J, Fewer, David P, Garg, Neha, Geiger, Christoph, Gomez-Escribano, Juan Pablo, Greule, Anja, Hadjithomas, Michalis, Haines, Anthony S, Helfrich, Eric J N, Hillwig, Matthew L, Ishida, Keishi, Jones, Adam C, Jones, Carla S, Jungmann, Katrin, Kegler, Carsten, Kim, Hyun Uk, Kotter, Peter, Krug, Daniel, Masschelein, Joleen, Melnik, Alexey V, Mantovani, Simone M, Monroe, Emily A, Moore, Marcus, Moss, Nathan, Nutzmann, Hans-Wilhelm, Pan, Guohui, Pati, Amrita, Petras, Daniel, Reen, F Jerry, Rosconi, Federico, Rui, Zhe, Tian, Zhenhua, Tobias, Nicholas J, Tsunematsu, Yuta, Wiemann, Philipp, Wyckoff, Elizabeth, Yan, Xiaohui, Yim, Grace, Yu, Fengan, Xie, Yunchang, Aigle, Bertrand, Apel, Alexander K, Balibar, Carl J, Balskus, Emily P, Barona-Gomez, Francisco, Bechthold, Andreas, Bode, Helge B, Borriss, Rainer, Brady, Sean F, Brakhage, Axel A, Caffrey, Patrick, Cheng, Yi-Qiang, Clardy, Jon, Cox, Russell J, De Mot, Rene, Donadio, Stefano, Donia, Mohamed S, van der Donk, Wilfred A, Dorrestein, Pieter C, Doyle, Sean, Driessen, Arnold J M, Ehling-Schulz, Monika, Entian, Karl-Dieter, Fischbach, Michael A, Gerwick, Lena, Gerwick, William H, Gross, Harald, Gust, Bertolt, Hertweck, Christian, Hofte, Monica, Jensen, Susan E, Ju, Jianhua, Katz, Leonard, Kaysser, Leonard, Klassen, Jonathan L, Keller, Nancy P, Kormanec, Jan, Kuipers, Oscar P, Kuzuyama, Tomohisa, Kyrpides, Nikos C, Kwon, Hyung-Jin, Lautru, Sylvie, Lavigne, Rob, Lee, Chia Y, Linquan, Bai, Liu, Xinyu, Liu, Wen, Luzhetskyy, Andriy, Mahmud, Taifo, Mast, Yvonne, Mendez, Carmen, Metsa-Ketela, Mikko, Micklefield, Jason, Mitchell, Douglas A, Moore, Bradley S, Moreira, Leonilde M, Muller, Rolf, Neilan, Brett A, Nett, Markus, Nielsen, Jens, O'Gara, Fergal, Oikawa, Hideaki, Osbourn, Anne, Osburne, Marcia S, Ostash, Bohdan, Payne, Shelley M, Pernodet, Jean-Luc, Petricek, Miroslav, Piel, Jorn, Ploux, Olivier, Raaijmakers, Jos M, Salas, Jose A, Schmitt, Esther K, Scott, Barry, Seipke, Ryan F, Shen, Ben, Sherman, David H, Sivonen, Kaarina, Smanski, Michael J, Sosio, Margherita, Stegmann, Evi, Sussmuth, Roderich D, Tahlan, Kapil, Thomas, Christopher M, Tang, Yi, Truman, Andrew W, Viaud, Muriel, Walton, Jonathan D, Walsh, Christopher T, Weber, Tilmann, van Wezel, Gilles P, Wilkinson, Barrie, Willey, Joanne M, Wohlleben, Wolfgang, Wright, Gerard D, Ziemert, Nadine, Zhang, Changsheng, Zotchev, Sergey B, Breitling, Rainer, Takano, Eriko, Glockner, Frank Oliver, Medema, Marnix H, Kottmann, Renzo, Yilmaz, Pelin, Cummings, Matthew, Biggins, John B, Blin, Kai, de Bruijn, Irene, Chooi, Yit Heng, Claesen, Jan, Coates, R Cameron, Cruz-Morales, Pablo, Duddela, Srikanth, Dusterhus, Stephanie, Edwards, Daniel J, Fewer, David P, Garg, Neha, Geiger, Christoph, Gomez-Escribano, Juan Pablo, Greule, Anja, Hadjithomas, Michalis, Haines, Anthony S, Helfrich, Eric J N, Hillwig, Matthew L, Ishida, Keishi, Jones, Adam C, Jones, Carla S, Jungmann, Katrin, Kegler, Carsten, Kim, Hyun Uk, Kotter, Peter, Krug, Daniel, Masschelein, Joleen, Melnik, Alexey V, Mantovani, Simone M, Monroe, Emily A, Moore, Marcus, Moss, Nathan, Nutzmann, Hans-Wilhelm, Pan, Guohui, Pati, Amrita, Petras, Daniel, Reen, F Jerry, Rosconi, Federico, Rui, Zhe, Tian, Zhenhua, Tobias, Nicholas J, Tsunematsu, Yuta, Wiemann, Philipp, Wyckoff, Elizabeth, Yan, Xiaohui, Yim, Grace, Yu, Fengan, Xie, Yunchang, Aigle, Bertrand, Apel, Alexander K, Balibar, Carl J, Balskus, Emily P, Barona-Gomez, Francisco, Bechthold, Andreas, Bode, Helge B, Borriss, Rainer, Brady, Sean F, Brakhage, Axel A, Caffrey, Patrick, Cheng, Yi-Qiang, Clardy, Jon, Cox, Russell J, De Mot, Rene, Donadio, Stefano, Donia, Mohamed S, van der Donk, Wilfred A, Dorrestein, Pieter C, Doyle, Sean, Driessen, Arnold J M, Ehling-Schulz, Monika, Entian, Karl-Dieter, Fischbach, Michael A, Gerwick, Lena, Gerwick, William H, Gross, Harald, Gust, Bertolt, Hertweck, Christian, Hofte, Monica, Jensen, Susan E, Ju, Jianhua, Katz, Leonard, Kaysser, Leonard, Klassen, Jonathan L, Keller, Nancy P, Kormanec, Jan, Kuipers, Oscar P, Kuzuyama, Tomohisa, Kyrpides, Nikos C, Kwon, Hyung-Jin, Lautru, Sylvie, Lavigne, Rob, Lee, Chia Y, Linquan, Bai, Liu, Xinyu, Liu, Wen, Luzhetskyy, Andriy, Mahmud, Taifo, Mast, Yvonne, Mendez, Carmen, Metsa-Ketela, Mikko, Micklefield, Jason, Mitchell, Douglas A, Moore, Bradley S, Moreira, Leonilde M, Muller, Rolf, Neilan, Brett A, Nett, Markus, Nielsen, Jens, O'Gara, Fergal, Oikawa, Hideaki, Osbourn, Anne, Osburne, Marcia S, Ostash, Bohdan, Payne, Shelley M, Pernodet, Jean-Luc, Petricek, Miroslav, Piel, Jorn, Ploux, Olivier, Raaijmakers, Jos M, Salas, Jose A, Schmitt, Esther K, Scott, Barry, Seipke, Ryan F, Shen, Ben, Sherman, David H, Sivonen, Kaarina, Smanski, Michael J, Sosio, Margherita, Stegmann, Evi, Sussmuth, Roderich D, Tahlan, Kapil, Thomas, Christopher M, Tang, Yi, Truman, Andrew W, Viaud, Muriel, Walton, Jonathan D, Walsh, Christopher T, Weber, Tilmann, van Wezel, Gilles P, Wilkinson, Barrie, Willey, Joanne M, Wohlleben, Wolfgang, Wright, Gerard D, Ziemert, Nadine, Zhang, Changsheng, Zotchev, Sergey B, Breitling, Rainer, Takano, Eriko, and Glockner, Frank Oliver

Abstract

A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.

Published
2015

13. Minimum information about a biosynthetic gene cluster

Author

Medema, Marnix H., Kottmann, Renzo, Yilmaz, Pelin, Cummings, Matthew, Biggins, John B., Kai, Blin, de Bruijn, Irene, Chooi, Yit Heng, Claesen, Jan, Coates, R. Cameron, Cruz-Morales, Pablo, Duddela, Srikanth, Düsterhus, Stephanie, Edwards, Daniel J., Fewer, David P., Garg, Neha, Geiger, Christoph, Gomez-Escribano, Juan Pablo, Greule, Anja, Hadjithomas, Michalis, Haines, Anthony S., Helfrich, Eric J. N., Hillwig, Matthew L., Ishida, Keishi, Jones, Adam C., Jones, Carla S., Jungmann, Katrin, Kegler, Carsten, Kim, Hyun Uk, Kötter, Peter, Krug, Daniel, Masschelein, Joleen, Melnik, Alexey V., Mantovan, Simone M., Monroe, Emily A., Moore, Marcus, Moss, Nathan, Nützmann, Hans-Wilhelm, Pan, Guohui, Pati, Amrita, Petras, Daniel, Reen, F. Jerry, Rosconi, Federico, Rui, Zhe, Tian, Zhenhua, Tobias, Nicholas J., Tsunematsu, Yuta, Wiemann, Philipp, Wyckoff, Elizabeth, Yan, Xiaohui, Yim, Grace, Yu, Fengan, Xie, Yunchang, Aigle, Bertrand, Apel, Alexander K., Balibar, Carl J., Balskus, Emily P., Barona-Gómez, Francisco, Bechthold, Andreas, Bode, Helge Björn, Borriss, Rainer, Brady, Sean F., Brakhage, Axel A., Caffrey, Patrick, Cheng, Yi-Qiang, Clardy, Jon, Cox, Russell J., De Mot, René, Donadio, Stefano, Donia, Mohamed S., van der Donk, Wilfred A., Dorrestein, Pieter C., Doyle, Sean, Driessen, Arnold J. M., Ehling-Schulz, Monika, Entian, Karl-Dieter, Fischbach, Michael A., Gerwick, Lena, Gerwick, William H., Gross, Harald, Gust, Bertolt, Hertweck, Christian, Höfte, Monica, Jensen, Susan E., Ju, Jianhua, Katz, Leonard, Kaysser, Leonard, Klassen, Jonathan L., Keller, Nancy P., Kormanec, Jan, Kuipers, Oscar P., Kuzuyama, Tomohisa, Kyrpides, Nikos C., Kwon, Hyung-Jin, Lautru, Sylvie, Lavigne, Rob, Lee, Chia Y., Linquan, Bai, Liu, Xinyu, Liu, Wen, Luzhetskyy, Andriy, Mahmud, Taifo, Mast, Yvonne, Méndez, Carmen, Metsä-Ketelä, Mikko, Micklefield, Jason, Mitchell, Douglas A., Moore, Bradley S., Moreira, Leonilde M., Müller, Rolf, Neilan, Brett A., Nett, Markus, Nielsen, Jens, O’Gara, Fergal, Oikawa, Hideaki, Osbourn, Anne, Osburne, Marcia S., Ostash, Bohdan, Payne, Shelley M., Pernodet, Jean-Luc, Petricek, Miroslav, Piel, Jörn, Ploux, Olivier, Raaijmakers, Jos M., Salas, José A., Schmitt, Esther K., Scott, Barry, Seipke, Ryan F., Shen, Ben, Sherman, David H., Sivonen, Kaarina, Smanski, Michael J., Sosio, Margherita, Stegmann, Evi, Süssmuth, Roderich D., Tahlan, Kapil, Thomas, Christopher M., Tang, Yi, Truman, Andrew W., Viaud, Muriel, Walton, Jonathan D., Walsh, Christopher T., Weber, Tilmann, van Wezel, Gilles P., Wilkinson, Barrie, Willey, Joanne M., Wohlleben, Wolfgang, Wright, Gerard D., Ziemert, Nadine, Zhang, Changsheng, Zotchev, Sergey B., Breitling, Rainer, Takano, Eriko, Glöckner, Frank Oliver, Medema, Marnix H., Kottmann, Renzo, Yilmaz, Pelin, Cummings, Matthew, Biggins, John B., Kai, Blin, de Bruijn, Irene, Chooi, Yit Heng, Claesen, Jan, Coates, R. Cameron, Cruz-Morales, Pablo, Duddela, Srikanth, Düsterhus, Stephanie, Edwards, Daniel J., Fewer, David P., Garg, Neha, Geiger, Christoph, Gomez-Escribano, Juan Pablo, Greule, Anja, Hadjithomas, Michalis, Haines, Anthony S., Helfrich, Eric J. N., Hillwig, Matthew L., Ishida, Keishi, Jones, Adam C., Jones, Carla S., Jungmann, Katrin, Kegler, Carsten, Kim, Hyun Uk, Kötter, Peter, Krug, Daniel, Masschelein, Joleen, Melnik, Alexey V., Mantovan, Simone M., Monroe, Emily A., Moore, Marcus, Moss, Nathan, Nützmann, Hans-Wilhelm, Pan, Guohui, Pati, Amrita, Petras, Daniel, Reen, F. Jerry, Rosconi, Federico, Rui, Zhe, Tian, Zhenhua, Tobias, Nicholas J., Tsunematsu, Yuta, Wiemann, Philipp, Wyckoff, Elizabeth, Yan, Xiaohui, Yim, Grace, Yu, Fengan, Xie, Yunchang, Aigle, Bertrand, Apel, Alexander K., Balibar, Carl J., Balskus, Emily P., Barona-Gómez, Francisco, Bechthold, Andreas, Bode, Helge Björn, Borriss, Rainer, Brady, Sean F., Brakhage, Axel A., Caffrey, Patrick, Cheng, Yi-Qiang, Clardy, Jon, Cox, Russell J., De Mot, René, Donadio, Stefano, Donia, Mohamed S., van der Donk, Wilfred A., Dorrestein, Pieter C., Doyle, Sean, Driessen, Arnold J. M., Ehling-Schulz, Monika, Entian, Karl-Dieter, Fischbach, Michael A., Gerwick, Lena, Gerwick, William H., Gross, Harald, Gust, Bertolt, Hertweck, Christian, Höfte, Monica, Jensen, Susan E., Ju, Jianhua, Katz, Leonard, Kaysser, Leonard, Klassen, Jonathan L., Keller, Nancy P., Kormanec, Jan, Kuipers, Oscar P., Kuzuyama, Tomohisa, Kyrpides, Nikos C., Kwon, Hyung-Jin, Lautru, Sylvie, Lavigne, Rob, Lee, Chia Y., Linquan, Bai, Liu, Xinyu, Liu, Wen, Luzhetskyy, Andriy, Mahmud, Taifo, Mast, Yvonne, Méndez, Carmen, Metsä-Ketelä, Mikko, Micklefield, Jason, Mitchell, Douglas A., Moore, Bradley S., Moreira, Leonilde M., Müller, Rolf, Neilan, Brett A., Nett, Markus, Nielsen, Jens, O’Gara, Fergal, Oikawa, Hideaki, Osbourn, Anne, Osburne, Marcia S., Ostash, Bohdan, Payne, Shelley M., Pernodet, Jean-Luc, Petricek, Miroslav, Piel, Jörn, Ploux, Olivier, Raaijmakers, Jos M., Salas, José A., Schmitt, Esther K., Scott, Barry, Seipke, Ryan F., Shen, Ben, Sherman, David H., Sivonen, Kaarina, Smanski, Michael J., Sosio, Margherita, Stegmann, Evi, Süssmuth, Roderich D., Tahlan, Kapil, Thomas, Christopher M., Tang, Yi, Truman, Andrew W., Viaud, Muriel, Walton, Jonathan D., Walsh, Christopher T., Weber, Tilmann, van Wezel, Gilles P., Wilkinson, Barrie, Willey, Joanne M., Wohlleben, Wolfgang, Wright, Gerard D., Ziemert, Nadine, Zhang, Changsheng, Zotchev, Sergey B., Breitling, Rainer, Takano, Eriko, and Glöckner, Frank Oliver

Abstract

A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.

Published
2015

14. Minimum Information about a Biosynthetic Gene cluster

Author

Medema, M.H., Kottmann, Renzo, Yilmaz, Pelin, Cummings, Matthew, Biggins, J.B., Blin, Kai, De Bruijn, Irene, Chooi, Yit Heng, Claesen, Jan, Coates, R.C., Cruz-Morales, Pablo, Duddela, Srikanth, Düsterhus, Stephanie, Edwards, Daniel J., Fewer, David P., Garg, Neha, Geiger, Christoph, Gomez-Escribano, Juan Pablo, Greule, Anja, Hadjithomas, Michalis, Haines, Anthony S., Helfrich, Eric J.N., Hillwig, Matthew L., Ishida, Keishi, Jones, Adam C., Jones, Carla S., Jungmann, Katrin, Kegler, Carsten, Kim, Hyun Uk, Kötter, Peter, Krug, Daniel, Masschelein, Joleen, Melnik, Alexey V., Mantovani, Simone M., Monroe, Emily A., Moore, Marcus, Moss, Nathan, Nützmann, Hans Wilhelm, Pan, Guohui, Pati, Amrita, Petras, Daniel, Reen, F.J., Rosconi, Federico, Rui, Zhe, Tian, Zhenhua, Tobias, Nicholas J., Tsunematsu, Yuta, Wiemann, Philipp, Wyckoff, Elizabeth, Yan, Xiaohui, Yim, Grace, Yu, Fengan, Xie, Yunchang, Aigle, Bertrand, Apel, Alexander K., Balibar, Carl J., Balskus, Emily P., Barona-Gómez, Francisco, Bechthold, Andreas, Bode, Helge B., Borriss, Rainer, Brady, Sean F., Brakhage, Axel A., Caffrey, Patrick, Cheng, Yi Qiang, Clardy, Jon, Cox, Russell J., De Mot, René, Donadio, Stefano, Donia, Mohamed S., Van Der Donk, Wilfred A., Dorrestein, Pieter C., Doyle, Sean, Driessen, Arnold J.M., Ehling-Schulz, Monika, Entian, Karl Dieter, Fischbach, Michael A., Gerwick, Lena, Gerwick, William H., Gross, Harald, Gust, Bertolt, Hertweck, Christian, Höfte, Monica, Jensen, Susan E., Ju, Jianhua, Katz, Leonard, Kaysser, Leonard, Klassen, Jonathan L., Keller, Nancy P., Kormanec, Jan, Kuipers, Oscar P., Kuzuyama, Tomohisa, Kyrpides, Nikos C., Kwon, Hyung Jin, Lautru, Sylvie, Lavigne, Rob, Lee, Chia Y., Linquan, Bai, Liu, Xinyu, Liu, Wen, Luzhetskyy, Andriy, Mahmud, Taifo, Mast, Yvonne, Méndez, Carmen, Metsä-Ketelä, Mikko, Micklefield, Jason, Mitchell, Douglas A., Moore, Bradley S., Moreira, Leonilde M., Müller, Rolf, Neilan, Brett A., Nett, Markus, Nielsen, Jens, O'Gara, Fergal, Oikawa, Hideaki, Osbourn, Anne, Osburne, Marcia S., Ostash, Bohdan, Payne, Shelley M., Pernodet, Jean Luc, Petricek, Miroslav, Piel, Jörn, Ploux, Olivier, Raaijmakers, Jos M., Salas, José A., Schmitt, Esther K., Scott, Barry, Seipke, Ryan F., Shen, Ben, Sherman, David H., Sivonen, Kaarina, Smanski, Michael J., Sosio, Margherita, Stegmann, Evi, Süssmuth, Roderich D., Tahlan, Kapil, Thomas, Christopher M., Tang, Yi, Truman, Andrew W., Viaud, Muriel, Walton, Jonathan D., Walsh, Christopher T., Weber, Tilmann, Van Wezel, Gilles P., Wilkinson, Barrie, Willey, Joanne M., Wohlleben, Wolfgang, Wright, Gerard D., Ziemert, Nadine, Zhang, Changsheng, Zotchev, Sergey B., Breitling, Rainer, Takano, Eriko, Glöckner, Frank Oliver, Medema, M.H., Kottmann, Renzo, Yilmaz, Pelin, Cummings, Matthew, Biggins, J.B., Blin, Kai, De Bruijn, Irene, Chooi, Yit Heng, Claesen, Jan, Coates, R.C., Cruz-Morales, Pablo, Duddela, Srikanth, Düsterhus, Stephanie, Edwards, Daniel J., Fewer, David P., Garg, Neha, Geiger, Christoph, Gomez-Escribano, Juan Pablo, Greule, Anja, Hadjithomas, Michalis, Haines, Anthony S., Helfrich, Eric J.N., Hillwig, Matthew L., Ishida, Keishi, Jones, Adam C., Jones, Carla S., Jungmann, Katrin, Kegler, Carsten, Kim, Hyun Uk, Kötter, Peter, Krug, Daniel, Masschelein, Joleen, Melnik, Alexey V., Mantovani, Simone M., Monroe, Emily A., Moore, Marcus, Moss, Nathan, Nützmann, Hans Wilhelm, Pan, Guohui, Pati, Amrita, Petras, Daniel, Reen, F.J., Rosconi, Federico, Rui, Zhe, Tian, Zhenhua, Tobias, Nicholas J., Tsunematsu, Yuta, Wiemann, Philipp, Wyckoff, Elizabeth, Yan, Xiaohui, Yim, Grace, Yu, Fengan, Xie, Yunchang, Aigle, Bertrand, Apel, Alexander K., Balibar, Carl J., Balskus, Emily P., Barona-Gómez, Francisco, Bechthold, Andreas, Bode, Helge B., Borriss, Rainer, Brady, Sean F., Brakhage, Axel A., Caffrey, Patrick, Cheng, Yi Qiang, Clardy, Jon, Cox, Russell J., De Mot, René, Donadio, Stefano, Donia, Mohamed S., Van Der Donk, Wilfred A., Dorrestein, Pieter C., Doyle, Sean, Driessen, Arnold J.M., Ehling-Schulz, Monika, Entian, Karl Dieter, Fischbach, Michael A., Gerwick, Lena, Gerwick, William H., Gross, Harald, Gust, Bertolt, Hertweck, Christian, Höfte, Monica, Jensen, Susan E., Ju, Jianhua, Katz, Leonard, Kaysser, Leonard, Klassen, Jonathan L., Keller, Nancy P., Kormanec, Jan, Kuipers, Oscar P., Kuzuyama, Tomohisa, Kyrpides, Nikos C., Kwon, Hyung Jin, Lautru, Sylvie, Lavigne, Rob, Lee, Chia Y., Linquan, Bai, Liu, Xinyu, Liu, Wen, Luzhetskyy, Andriy, Mahmud, Taifo, Mast, Yvonne, Méndez, Carmen, Metsä-Ketelä, Mikko, Micklefield, Jason, Mitchell, Douglas A., Moore, Bradley S., Moreira, Leonilde M., Müller, Rolf, Neilan, Brett A., Nett, Markus, Nielsen, Jens, O'Gara, Fergal, Oikawa, Hideaki, Osbourn, Anne, Osburne, Marcia S., Ostash, Bohdan, Payne, Shelley M., Pernodet, Jean Luc, Petricek, Miroslav, Piel, Jörn, Ploux, Olivier, Raaijmakers, Jos M., Salas, José A., Schmitt, Esther K., Scott, Barry, Seipke, Ryan F., Shen, Ben, Sherman, David H., Sivonen, Kaarina, Smanski, Michael J., Sosio, Margherita, Stegmann, Evi, Süssmuth, Roderich D., Tahlan, Kapil, Thomas, Christopher M., Tang, Yi, Truman, Andrew W., Viaud, Muriel, Walton, Jonathan D., Walsh, Christopher T., Weber, Tilmann, Van Wezel, Gilles P., Wilkinson, Barrie, Willey, Joanne M., Wohlleben, Wolfgang, Wright, Gerard D., Ziemert, Nadine, Zhang, Changsheng, Zotchev, Sergey B., Breitling, Rainer, Takano, Eriko, and Glöckner, Frank Oliver

Abstract

A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.

Published
2015

15. Ribosomally synthesized and post-translationally modified peptide natural products : overview and recommendations for a universal nomenclature

Author

Arnison, Paul G., Bibb, Mervyn J., Bierbaum, Gabriele, Bowers, Albert A., Bugni, Tim S., Bulaj, Grzegorz, Camarero, Julio A., Campopiano, Dominic J., Challis, Gregory L., Clardy, Jon, Cotter, Paul D., Craik, David J., Dawson, Michael, Dittmann, Elke, Donadio, Stefano, Dorrestein, Pieter C., Entian, Karl-Dieter, Fischbach, Michael A., Garavelli, John S., Göransson, Ulf, Gruber, Christian W., Haft, Daniel H., Hemscheidt, Thomas K., Hertweck, Christian, Hill, Colin, Horswill, Alexander R., Jaspars, Marcel, Kelly, Wendy L., Klinman, Judith P., Kuipers, Oscar P., Link, A. James, Liu, Wen, Marahiel, Mohamed A., Mitchell, Douglas A., Moll, Gert N., Moore, Bradley S., Mueller, Rolf, Nair, Satish K., Nes, Ingolf F., Norris, Gillian E., Olivera, Baldomero M., Onaka, Hiroyasu, Patchett, Mark L., Piel, Joern, Reaney, Martin J. T., Rebuffat, Sylvie, Ross, R. Paul, Sahl, Hans-Georg, Schmidt, Eric W., Selsted, Michael E., Severinov, Konstantin, Shen, Ben, Sivonen, Kaarina, Smith, Leif, Stein, Torsten, Suessmuth, Roderich D., Tagg, John R., Tang, Gong-Li, Truman, Andrew W., Vederas, John C., Walsh, Christopher T., Walton, Jonathan D., Wenzel, Silke C., Willey, Joanne M., van der Donk, Wilfred A., Arnison, Paul G., Bibb, Mervyn J., Bierbaum, Gabriele, Bowers, Albert A., Bugni, Tim S., Bulaj, Grzegorz, Camarero, Julio A., Campopiano, Dominic J., Challis, Gregory L., Clardy, Jon, Cotter, Paul D., Craik, David J., Dawson, Michael, Dittmann, Elke, Donadio, Stefano, Dorrestein, Pieter C., Entian, Karl-Dieter, Fischbach, Michael A., Garavelli, John S., Göransson, Ulf, Gruber, Christian W., Haft, Daniel H., Hemscheidt, Thomas K., Hertweck, Christian, Hill, Colin, Horswill, Alexander R., Jaspars, Marcel, Kelly, Wendy L., Klinman, Judith P., Kuipers, Oscar P., Link, A. James, Liu, Wen, Marahiel, Mohamed A., Mitchell, Douglas A., Moll, Gert N., Moore, Bradley S., Mueller, Rolf, Nair, Satish K., Nes, Ingolf F., Norris, Gillian E., Olivera, Baldomero M., Onaka, Hiroyasu, Patchett, Mark L., Piel, Joern, Reaney, Martin J. T., Rebuffat, Sylvie, Ross, R. Paul, Sahl, Hans-Georg, Schmidt, Eric W., Selsted, Michael E., Severinov, Konstantin, Shen, Ben, Sivonen, Kaarina, Smith, Leif, Stein, Torsten, Suessmuth, Roderich D., Tagg, John R., Tang, Gong-Li, Truman, Andrew W., Vederas, John C., Walsh, Christopher T., Walton, Jonathan D., Wenzel, Silke C., Willey, Joanne M., and van der Donk, Wilfred A.

Abstract

This review presents recommended nomenclature for the biosynthesis of ribosomally synthesized and post-translationally modified peptides (RiPPs), a rapidly growing class of natural products. The current knowledge regarding the biosynthesis of the >20 distinct compound classes is also reviewed, and commonalities are discussed.

Published
2013
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16. CDK-Dependent Hsp70 Phosphorylation Controls G1 Cyclin Abundance and Cell-Cycle Progression

Author

Truman, Andrew W., Kristjansdottir, Kolbrun, Wolfgeher, Donald, Hasin, Naushaba, Polier, Sigrun, Zhang, Hong, Perrett, Sarah, Prodromou, Chrisostomos, Jones, Gary W., Kron, Stephen J., Truman, Andrew W., Kristjansdottir, Kolbrun, Wolfgeher, Donald, Hasin, Naushaba, Polier, Sigrun, Zhang, Hong, Perrett, Sarah, Prodromou, Chrisostomos, Jones, Gary W., and Kron, Stephen J.

Abstract

In budding yeast, the essential functions of Hsp70 chaperones Ssa1–4 are regulated through expression level, isoform specificity, and cochaperone activity. Suggesting a novel regulatory paradigm, we find that phosphorylation of Ssa1 T36 within a cyclin-dependent kinase (CDK) consensus site conserved among Hsp70 proteins alters cochaperone and client interactions. T36 phosphorylation triggers displacement of Ydj1, allowing Ssa1 to bind the G1 cyclin Cln3 and promote its degradation. The stress CDK Pho85 phosphorylates T36 upon nitrogen starvation or pheromone stimulation, destabilizing Cln3 to delay onset of S phase. In turn, the mitotic CDK Cdk1 phosphorylates T36 to block Cln3 accumulation in G2/M. Suggesting broad conservation from yeast to human, CDK-dependent phosphorylation of Hsc70 T38 similarly regulates Cyclin D1 binding and stability. These results establish an active role for Hsp70 chaperones as signal transducers mediating growth control of G1 cyclin abundance and activity.

Published
2012

18. Activation of Secondary Metabolite Gene Clusters in Streptomyces clavuligerus by the PimM Regulator of Streptomyces natalensis

Author

Microbiologia, Martínez Burgo, Yolanda, Santos Aberturas, Javier, Rodríguez García, Antonio, García Barreales, Eva, Tormo, José Rubén, Truman, Andrew W., Reyes, Fernando, Aparicio Fernández, Jesús Manuel, Liras Padín, Paloma, Microbiologia, Martínez Burgo, Yolanda, Santos Aberturas, Javier, Rodríguez García, Antonio, García Barreales, Eva, Tormo, José Rubén, Truman, Andrew W., Reyes, Fernando, Aparicio Fernández, Jesús Manuel, and Liras Padín, Paloma

Abstract

[EN] Expression of non-native transcriptional activators may be a powerful general method to activate secondary metabolites biosynthetic pathways. PAS-LuxR regulators, whose archetype is PimM, activate the biosynthesis of polyene macrolide antifungals and other antibiotics, and have been shown to be functionally preserved across multiple Streptomyces strains. In this work we show that constitutive expression of pimM in Streptomyces clavuligerus ATCC 27064 significantly affected its transcriptome and modifies secondary metabolism. Almost all genes in three secondary metabolite clusters were overexpressed, including the clusters responsible for the biosynthesis of the clinically important clavulanic acid and cephamycin C. In comparison to a control strain, this resulted in 10- and 7-fold higher production levels of these metabolites, respectively. Metabolomic and bioactivity studies of S. clavuligerus::pimM also revealed deep metabolic changes. Antifungal activity absent in the control strain was detected in S. clavuligerus::pimM, and determined to be the result of a fivefold increase in the production of the tunicamycin complex

19. Hsp90 and phosphorylation of the Slt2(Mpk1) MAP kinase activation loop are essential for catalytic, but not non-catalytic, Slt2-mediated transcription in yeast

Author

Millson, Stefan H., Truman, Andrew W., Piper, Peter W., Millson, Stefan H., Truman, Andrew W., and Piper, Peter W.

Abstract

In yeast, the Slt2(Mpk1) stress-activated protein kinase directs the activation of two transcription factors, Rlm1 and Swi4/Swi6, in response to cell wall stress. Rlm1 is activated through a phosphorylation by Slt2, whereas the Swi4/Swi6 activation is noncatalytic and triggered by the binding of phosphorylated forms of both Slt2 and a catalytically inactive pseudokinase (Mlp1). Previous studies have delineated a role for the molecular chaperone Hsp90 in the activation of Slt2, but the involvement of Hsp90 in these events of catalytic versus non-catalytic cell integrity signaling has remained elusive. In cells lacking Mlp1, the Hsp90 inhibitor radicicol was found to inhibit the Slt2-mediated catalytic activation of Rlm1, but not the noncatalytic activation of Swi4/Swi6. Mutation of residues in the TEY motif of the Slt2 activation loop strongly impacted both Hsp90 binding and Rlm1-mediated transcription. In contrast, many of these same mutations had only modest effects on Swi4/6 (Slt2-mediated, non-catalytic) transcription, although one that blocked both the Slt2:Hsp90 interaction and Rlm1-mediated transcription (E191G) triggered a hyperactivation of Swi4/6. Taken together, our results cement the importance of the Slt2 activation loop for both the binding of Hsp90 by Slt2 and the catalytic activation of cell integrity signaling.

20. A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)

Author

Millson, Stefan H., Truman, Andrew W., King, Victoria, Prodromou, Crisostomos, Pearl, Lawrence H., Piper, Peter W., Millson, Stefan H., Truman, Andrew W., King, Victoria, Prodromou, Crisostomos, Pearl, Lawrence H., and Piper, Peter W.

Abstract

The Hsp90 chaperone cycle catalyzes the final activation step of several important eukaryotic proteins (Hsp90 “clients”). Although largely a functional form of Hsp90, an Hsp90-Gal4p DNA binding domain fusion (Hsp90-BD) displays no strong interactions in the yeast two-hybrid system, consistent with a general transience of most Hsp90-client associations. Strong in vivo interactions are though detected when the E33A mutation is introduced into this bait, a mutation that should arrest Hsp90-client complexes at a stage where the client is stabilized, yet prevented from attaining its active form. This E33A mutation stabilized the two-hybrid interactions of the Hsp90-BD fusion with ∼3% of the Saccharomyces cerevisiae proteome in a screen of the 6,000 yeast proteins expressed as fusions to the Gal4p activation domain (AD). Among the detected interactors were the two stress-activated mitogen-activated protein (MAP) kinases of yeast, Hog1p and Slt2p (Mpk1p). Column retention experiments using wild-type and mutant forms of Hsp90 and Slt2p MAP kinase, as well as quantitative measurements of the effects of stress on the two-hybrid interaction of mutant Hsp90-BD and AD-Slt2p fusions, revealed that Hsp90 binds exclusively to the dually Thr/Tyr-phosphorylated, stress-activated form of Slt2p [(Y-P,T-P)Slt2p] and also to the MAP kinase domain within this (Y-P,T-P)Slt2p. Phenotypic analysis of a yeast mutant that expresses a mutant Hsp90 (T22Ihsp82) revealed that Hsp90 function is essential for this (Y-P,T-P)Slt2p to activate one of its downstream targets, the Rlm1p transcription factor. The interaction between Hsp90 and (Y-P,T-P)Slt2p, characterized in this study, is probably essential in this Hsp90 facilitation of the Rlm1p activation by Slt2p.

21. Cdc37 engages in stable, S14A mutation-reinforced association with the most atypical member of the yeast kinome, Cdk-activating kinase (Cak1)

Author

Millson, Stefan, van Oosten-Hawle, Patricija, Alkuriji, Mohammed A., Truman, Andrew, Siderius, Marco, Piper, Peter W., Millson, Stefan, van Oosten-Hawle, Patricija, Alkuriji, Mohammed A., Truman, Andrew, Siderius, Marco, and Piper, Peter W.

Abstract

In most eukaryotes, Cdc37 is an essential chaperone, transiently associating with newly synthesised protein kinases in order to promote their stabilisation and activation. To determine whether the yeast Cdc37 participates in any stable protein interactions in vivo, genomic two-hybrid screens were conducted using baits that are functional as they preserve the integrity of the conserved N-terminal region of Cdc37, namely a Cdc37-Gal4 DNA binding domain (BD) fusion in both its wild type and its S14 nonphosphorylatable (Cdc37(S14A)) mutant forms. While this failed to identify the protein kinases previously identified as Cdc37 interactors in pull-down experiments, it did reveal Cdc37 engaging in a stable association with the most atypical member of the yeast kinome, cyclin-dependent kinase (Cdk1)-activating kinase (Cak1). Phosphorylation of the conserved S14 of Cdc37 is normally crucial for the interaction with, and stabilisation of, those protein kinase targets of Cdc37, Cak1 is unusual in that the lack of this Cdc37 S14 phosphorylation both reinforces Cak1:Cdc37 interaction and does not compromise Cak1 expression in vivo. Thus, this is the first Cdc37 client kinase found to be excluded from S14 phosphorylation-dependent interaction. The unusual stability of this Cak1:Cdc37 association may partly reflect unique structural features of the fungal Cak1.

22. In the yeast heat shock response, Hsf1-directed induction of Hsp90 facilitates the activation of the Slt2 (Mpk1) mitogen-activated protein kinase required for cell integrity

Author

Truman, Andrew W., Millson, Stefan H., Nuttall, James M., Mollapour, Mehdi, Prodromou, Chrisostomos, Piper, Peter W., Truman, Andrew W., Millson, Stefan H., Nuttall, James M., Mollapour, Mehdi, Prodromou, Chrisostomos, and Piper, Peter W.

Abstract

Yeast is rendered temperature sensitive with loss of the C-terminal (CT) domain of heat shock transcription factor (Hsf1). This domain loss was found to abrogate heat stimulation of Slt2 (Mpk1), the mitogen-activated protein kinase that directs the reinforced cell integrity gene expression needed for high-temperature growth. In Hsf1 CT domain-deficient cells, Slt2 still undergoes Mkk1/2-directed dual-Thr/Tyr phosphorylation in response to the heat stimulation of cell integrity pathway signaling, but the low Hsp90 expression level suppresses any corresponding increase in Slt2 kinase activity due to Slt2 being a “client” of the Hsp90 chaperone. A non-Hsf1-directed Hsp90 overexpression restored the heat induction of Slt2 activity in these cells, as well as both Slt2-dependent (Rlm1, Swi4) and Slt2-independent (MBF) transcriptional activities. Their high-temperature growth was also rescued, not just by this Hsp90 overexpression but by osmotic stabilization, by the expression of a Slt2-independent form of the Rlm1 transcriptional regulator of cell integrity genes, and by a multicopy SLT2 gene vector. In providing the elevated Hsp90 needed for an efficient activation of Slt2, heat activation of Hsf1 indirectly facilitates (Slt2-directed) heat activation of yet another transcription factor (Rlm1). This provides an explanation as to why, in earlier transcript analysis compared to chromatin immunoprecipitation studies, many more genes of yeast displayed an Hsf1-dependent transcriptional activation by heat than bound Hsf1 directly. The levels of Hsp90 expression affecting transcription factor regulation by Hsp90 client protein kinases also provides a mechanistic model for how heat shock factor can influence the expression of several non-hsp genes in higher organisms.

23. A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p)

Author

Millson, Stefan H., Truman, Andrew W., King, Victoria, Prodromou, Chrisostomos, Pearl, Laurence H., Piper, Peter W., Millson, Stefan H., Truman, Andrew W., King, Victoria, Prodromou, Chrisostomos, Pearl, Laurence H., and Piper, Peter W.

Abstract

The Hsp90 chaperone cycle catalyzes the final activation step of several important eukaryotic proteins (Hsp90 “clients”). Although largely a functional form of Hsp90, an Hsp90-Gal4p DNA binding domain fusion (Hsp90-BD) displays no strong interactions in the yeast two-hybrid system, consistent with a general transience of most Hsp90-client associations. Strong in vivo interactions are though detected when the E33A mutation is introduced into this bait, a mutation that should arrest Hsp90-client complexes at a stage where the client is stabilized, yet prevented from attaining its active form. This E33A mutation stabilized the two-hybrid interactions of the Hsp90-BD fusion with ∼3% of the Saccharomyces cerevisiae proteome in a screen of the 6,000 yeast proteins expressed as fusions to the Gal4p activation domain (AD). Among the detected interactors were the two stress-activated mitogen-activated protein (MAP) kinases of yeast, Hog1p and Slt2p (Mpk1p). Column retention experiments using wild-type and mutant forms of Hsp90 and Slt2p MAP kinase, as well as quantitative measurements of the effects of stress on the two-hybrid interaction of mutant Hsp90-BD and AD-Slt2p fusions, revealed that Hsp90 binds exclusively to the dually Thr/Tyr-phosphorylated, stress-activated form of Slt2p [(Y-P,T-P)Slt2p] and also to the MAP kinase domain within this (Y-P,T-P)Slt2p. Phenotypic analysis of a yeast mutant that expresses a mutant Hsp90 (T22Ihsp82) revealed that Hsp90 function is essential for this (Y-P,T-P)Slt2p to activate one of its downstream targets, the Rlm1p transcription factor. The interaction between Hsp90 and (Y-P,T-P)Slt2p, characterized in this study, is probably essential in this Hsp90 facilitation of the Rlm1p activation by Slt2p.

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