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5. Convergent evolution of plant pattern recognition receptors sensing cysteine-rich patterns from three microbial kingdoms

Author

Sub Bioinformatics, Theoretical Biology and Bioinformatics, Yang, Yuankun, Steidele, Christina E, Rössner, Clemens, Löffelhardt, Birgit, Kolb, Dagmar, Leisen, Thomas, Zhang, Weiguo, Ludwig, Christina, Felix, Georg, Seidl, Michael F, Becker, Annette, Nürnberger, Thorsten, Hahn, Matthias, Gust, Bertolt, Gross, Harald, Hückelhoven, Ralph, Gust, Andrea A, Sub Bioinformatics, Theoretical Biology and Bioinformatics, Yang, Yuankun, Steidele, Christina E, Rössner, Clemens, Löffelhardt, Birgit, Kolb, Dagmar, Leisen, Thomas, Zhang, Weiguo, Ludwig, Christina, Felix, Georg, Seidl, Michael F, Becker, Annette, Nürnberger, Thorsten, Hahn, Matthias, Gust, Bertolt, Gross, Harald, Hückelhoven, Ralph, and Gust, Andrea A

Published
2023

6. Convergent evolution of plant pattern recognition receptors sensing cysteine-rich patterns from three microbial kingdoms

Author

Yang, Yuankun, primary, Steidele, Christina E., additional, Löffelhardt, Birgit, additional, Kolb, Dagmar, additional, Leisen, Thomas, additional, Zhang, Weiguo, additional, Ludwig, Christina, additional, Felix, Georg, additional, Seidl, Michael F., additional, Nürnberger, Thorsten, additional, Hahn, Matthias, additional, Gust, Bertolt, additional, Gross, Harald, additional, Hückelhoven, Ralph, additional, and Gust, Andrea A., additional

Published
2022
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10. Additional file 1 of Origin of the 3-methylglutaryl moiety in caprazamycin biosynthesis

Author

Bär, Daniel, Konetschny, Benjamin, Kulik, Andreas, Xu, Houchao, Paccagnella, Davide, Beller, Patrick, Ziemert, Nadine, Dickschat, Jeroen S., and Gust, Bertolt

Abstract

Additional file 1: Figure S1. Degradation of leucine and isovalerate via the Liu-pathway as described for P. aeruginosa PAO1 [29]. Figure S2. Genetic organization of the caprazamycin biosynthetic gene cluster. Genes putatively involved in colour coding according to McErlean et al. [17]. Figure S3. Extracted ion chromatograms of S. coelicolor M1154 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S4. Extracted ion chromatograms of S. coelicolor M1154/cpzLK09 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S5. Extracted ion chromatograms of S. coelicolor M1154/cpzDB04 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S6. Genetic organization of clusters encoding for Liu-pathway from P. aeruginosa PAO1, caprazamycin wildtype producer S. sp. MK730-62F2 and the heterologous caprazamycin producer S. coelicolor M1154. Additional genes in Streptomyces strains are shown transparent. Table shows genes from P. aeruginosa PAO1 and their proposed function along with homologue genes found in S. sp. MK730-62F2 and S. coelicolor M1154. Values in brackets indicate % identities/similarities (n.s. no significant similarities). Figure S7. Distribution of liu clusters in Actinobacteria and Streptomyces. A: Cblaster detected 4837 similar clusters containing at least three genes homolog to the query sequence sco2775-sco2779 from S. coelicolor M1154. We discovered that 1.431 out of 31.598 (4.5%) Actinobacteria assemblies and 1.344 out of 2.574 (52.2%) Streptomyces assemblies and listed in the GTDB contain a liu cluster with homologues of all five query genes. B: Cblaster detected 5009 similar clusters containing at least three genes homolog to the query sequence sco2774-sco2779 from S. coelicolor M1154. We discovered that 1.246 out of 31.598 (3.9%) Actinobacteria assemblies and 1.241 out of 2.574 (48.2%) Streptomyces assemblies and listed in the GTDB contain a liu cluster with homologues of all six query genes. A homologue of sco2774 could only be found in 1.376 out of 5009 (27,5%) of the Actinobacteria clusters detected by cblaster, whereas the majority of detected Streptomyces cluster contain this gene with 1.343 out of 1.652 sequences (81,3%). Figure S8. Extracted ion chromatograms of S. coelicolor M1154Δsco2776-sco2779/cpzLK09 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S9. Extracted ion chromatograms of S. coelicolor M1154Δsco2776-sco2779/cpzDB04 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S10. Total ion chromatograms of S. coelicolor M1154Δsco2776-sco2779/cpzDB04 and S. coelicolor M1154Δsco2776-sco2779/cpzLK09. MS2-fragmentation patterns of peak 1 (hydoxyacylcaprazol E, Rt 12.9 min) and peak 2 (caprazamycin aglycon E, Rt 13.8 min) are shown together with corresponding fragmentation schemes. Figure S11. Extracted ion chromatograms of S. coelicolor M1154Δsco2779/cpzLK09 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S12. Extracted ion chromatograms of S. coelicolor M1154Δsco2779/cpzDB04 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S13. Extracted ion chromatograms of S. coelicolor M1154Δsco2776/cpzLK09 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z of 830.5. Figure S14. Extracted ion chromatograms of S. coelicolor M1154Δsco2776/cpzDB04 (three individual mutants). Masses are shown for caprazamycin aglycons E/F with m/z of 930.5, caprazamycin aglycons C/D/G with m/z of 944.5, caprazamycin aglycons A/B with m/z of 958.5 and the respective hydroxyacylcaprazols E/F with m/z of 802.5, hydroxyacylcaprazols C/D/G with m/z of 816.5 and hydroxyacylcaprazols A/B with m/z

Published
2022
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15. Transcriptional regulation of the novobiocin biosynthetic gene cluster

Author

Dangel, Volker, Harle, Johannes, Goerke, Christiane, Wolz, Christiane, Gust, Bertolt, Pernodet, Jean-Luc, and Heide, Lutz

Subjects
Antibacterial agents -- Health aspects, Antibacterial agents -- Research, Bacterial genetics -- Research, Genetic regulation -- Research, Polymerase chain reaction -- Usage, Biological sciences
Abstract

The aminocoumarin antibiotic novobiocin is a gyrase inhibitor formed by a Streptomyces strain. The biosynthetic gene cluster of novobiocin spans 23.4 kb and contains 20 coding sequences, among them the two regulatory genes novE and novG. We investigated the location of transcriptional promoters within this cluster by insertion of transcriptional terminator cassettes and RT-PCR analysis of the resulting mutants. The cluster was found to contain eight DNA regions with promoter activity. The regulatory protein NovG binds to a previously identified binding site within the promoter region located upstream of novH, but apparently not to any of the other seven promoters. Quantitative real-time PCR was used to compare the number of transcripts in a strain carrying an intact novobiocin cluster with strains carrying mutated clusters. Both in-frame deletion of the regulatory gene novG and insertion of a terminator cassette into the biosynthetic gene novH led to a strong reduction of the number of transcripts of the genes located between novH and novW. This suggested that these 16 biosynthetic genes form a single operon. Three internal promoters are located within this operon but appear to be of minor importance, if any, under our experimental conditions. Transcription of novG was found to depend on the presence of NovE, suggesting that the two regulatory genes, novE and novG, act in a cascade-like mechanism. The resistance gene [gyrB.sup.R], encoding an aminocoumarin-resistant gyrase B subunit, may initially be co-transcribed with the genes from novH to novW. However, when the gyrase inhibitor novobiocin accumulates in the cultures, [gyrB.sup.R] is transcribed from its own promoter. Previous work has suggested that this promoter is controlled by the superhelical density of chromosomal DNA. DOI 10.1099/mic.0.032649-0

Published
2009

17. Genetic Engineering in Combination with Semi‐Synthesis Leads to a New Route for Gram‐Scale Production of the Immunosuppressive Natural Product Brasilicardin A

Author

Botas, Alma, primary, Eitel, Michael, additional, Schwarz, Paul N., additional, Buchmann, Anina, additional, Costales, Paula, additional, Núñez, Luz Elena, additional, Cortés, Jesús, additional, Morís, Francisco, additional, Krawiec, Michał, additional, Wolański, Marcin, additional, Gust, Bertolt, additional, Rodriguez, Mirna, additional, Fischer, Wolf‐Nicolas, additional, Jandeleit, Bernd, additional, Zakrzewska‐Czerwińska, Jolanta, additional, Wohlleben, Wolfgang, additional, Stegmann, Evi, additional, Koch, Pierre, additional, Méndez, Carmen, additional, and Gross, Harald, additional

Published
2021
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19. Effects of deletions of mbtH-like genes on clorobiocin biosynthesis in Streptomyces coelicolor

Author

Wolpert, Manuel, Gust, Bertolt, Kammerer, Bernd, and Heide, Lutz

Subjects
Gene mutations -- Research, Streptomyces -- Research, Antibiotics -- Research, Biological sciences
Abstract

In the biosynthetic gene cluster of the aminocoumarin antibiotic clorobiocin, the small ORF cloY encodes a 71 aa protein which shows significant sequence similarity to mbtH from the mycobactin biosynthetic gene cluster of Mycobacterium tuberculosis, mbtH-like genes are frequently found in the biosynthetic gene clusters of peptide antibiotics and siderophores, but their function has remained enigmatic. In a recent publication it has been suggested that these genes may have no function for secondary metabolite biosynthesis. An in-frame deletion of cloY in the clorobiocin cluster has now been carried out. When the modified cluster was expressed in the heterologous host Streptomyces coelicolor M512, clorobiocin was still formed. However, when the two further mbtH-like genes from elsewhere in the host genome were inactivated as well, clorobiocin formation was reduced dramatically. Complementation with cloy or with any of three other mbtH-like genes restored clorobiocin formation. This is the first report proving the requirement of an mbtH-like gene for secondary metabolite formation, and the first proof that different mbtH-like genes can functionally replace each other. Feeding of an mbtH-defective triple mutant strain with an intact 3-amino-4,7-dihydroxy-coumarin moiety restored antibiotic production, showing that cloY is specifically required for the formation of this moiety of the clorobiocin molecule.

Published
2007

20. RNA 3'-tail synthesis in Streptomyces: in vitro and in vivo activities of RNase PH, the SC03896 gene product and polynucleotide phosphorylase

Author

Bralley, Patricia, Gust, Bertolt, Chang, Samantha, Chater, Keith F., and Jones, George H.

Subjects
Streptomyces -- Genetic aspects, Streptomyces -- Physiological aspects, RNA -- Research, Bacterial genetics -- Research, Biological sciences
Abstract

As in other bacteria, 3'-tails are added post-transcriptionally to Streptomyces coeficolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified. This paper reports on three candidates for this role. First, it is confirmed that the product of S. coelicolor gene SC03896, although it bears significant sequence similarity to Escherichia coil poly(A) polymerase I, is a tRNA nucleotidyltransferase, not a poly(A) polymerase. It is further shown that SC02904 encodes an RNase PH homologue that possesses the polymerization and phosphorolysis activities expected for enzymes of that family. S. coelicolor RNase PH can add poly(A) tails to a model RNA transcript in vitro. However, disruption of the RNase PH gene has no effect on RNA 3'-tail length or composition in S. coeficolor; thus, RNase PH does not function as the RNA 3'-polyribonucleotide polymerase [poly(A) polymerase] in that organism. These results strongly suggest that the enzyme responsible for RNA 3'-tail synthesis in S. coeficolor and other streptomycetes is polynucleotide phosphorylase (PNPase). Moreover, this study shows that both PNPase and the product of SC03896 are essential. It is possible that the dual functions of PNPase in the synthesis and degradation of RNA 3'-tails make it indispensable in Streptomyces.

Published
2006

22. Developmental-stage-specific assembly of ParB complexes in Streptomyces coelicolor hyphae

Author

Jakimowicz, Dagmara, Gust, Bertolt, Zakrzewska-Czerwinska, Jolanta, and Chater, Keith F.

Subjects
Chromosomes -- Research, Streptomyces -- Research, Hyphae -- Research, Biological sciences
Abstract

In Streptomyces coelicolor ParB is required for accurate chromosome partitioning during sporulation. Using a functional ParB-enhanced green fluorescent protein fusion, we observed bright tip-associated foci and other weaker, irregular foci in S. coelicolor vegetative hyphae. In contrast, in aerial hyphae regularly spaced bright loci accompanied sporulation-associated chromosome condensation and septation.

Published
2005

26. Region-specific transcriptional activity in the genome of Streptomyces coelicolor A3(2)

Author

Gust, Bertolt, Spatz, Kerstin, Spychaj, Alexander, and Redenbach, Matthias

Subjects
Gene expression -- Research, Streptomyces -- Genetic aspects, Bacterial genetics -- Research, Biological sciences
Abstract

Researchers used subtractive hybridization between genome-specific DNA and total RNA and PCR to analyze gene expression in Streptomyces coelicolor A3(2) and the accessory linear plasmid SCP1. About 24 genes in the silent regions of S. coelicolor A3(2) chromosomes are expressed.

Published
2001

30. Formation and attachment of the deoxysugar moiety and assembly of the gene cluster for caprazamycin biosynthesis

Author

Kaysser, Leonard, Wemakor, Emmanuel, Siebenberg, Stefanie, Salas, Jose A., Jae Kyung Sohng, Kammerer, Bernd, and Gust, Bertolt

Subjects
Biosynthesis -- Analysis, Streptomyces -- Genetic aspects, Streptomyces -- Physiological aspects, Genetic research, Biological sciences
Abstract

In vitro study was conducted to understand the role of coexpression Cpz31 in Streptomyces coelicolor for the attachment of the L-rhamnose to the caprazamycins aglycones, generating a rare acylated deoxyhexose. The recombineering approach used might provide a useful tool for the assembly of biosynthetic building blocks for heterologous production of microbial compounds.

Published
2010

31. Heterologous expression of novobiocin and clorobiocin biosynthetic gene clusters

Author

Eustaquio, Alessandra S., Gust, Bertolt, Galm, Ute, Shu-Ming Li, Chater, Keith F., and Heide, Lutz

Subjects
Escherichia coli -- Research, Streptomyces -- Genetic aspects, Streptomyces -- Research, Biological sciences
Abstract

An efficient method for the heterologous expression of biosynthetic gene clusters in different Streptomyces strains is described. Lambda-Red-mediated recombination in Escherichia coli is used for the introduction of integration functions into the cosmid backbones, which allowed subsequent site-specific integration into the genome of the heterologous host.

Published
2005

33. 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, and Microbial Ecology (ME)

Subjects
international
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

36. 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

37. 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

38. Identification of Novel α-Pyrones from Conexibacter woeseiServing as Sulfate Shuttles

Author

Wiker, Franziska, Konnerth, Martin, Helmle, Irina, Kulik, Andreas, Kaysser, Leonard, Gross, Harald, and Gust, Bertolt

Abstract

Pyrones comprise a structurally diverse class of compounds. Although they are widespread in nature, their specific physiological functions remain unknown in most cases. We recently described that triketide pyrones mediate the sulfotransfer in caprazamycin biosynthesis. Herein, we report the identification of conexipyrones A–C, three previously unrecognized tetra-substituted α-pyrones, from the soil actinobacterium Conexibacter woesei. Insights into their biosynthesis via a type III polyketide synthase were obtained by feeding studies using isotope-enriched precursors. In vitroassays employing the genetically associated 3′-phosphoadenosine-5′-phosphosulfate (PAPS)-dependent sulfotransferase CwoeST revealed conexipyrones as the enzymes’ genuine sulfate acceptor substrates. Furthermore, conexipyrones were determined to function as sulfate shuttles in a two-enzyme assay, because their sulfated derivatives were accepted as donor molecules by the PAPS-independent arylsulfate sulfotransferase (ASST) Cpz4 to yield sulfated caprazamycin intermediates.

Published
2019
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45. Activation of a silent phenazine biosynthetic gene cluster reveals a novel natural product and a new resistance mechanism against phenazines

Author

Saleh, Orwah, primary, Bonitz, Tobias, additional, Flinspach, Katrin, additional, Kulik, Andreas, additional, Burkard, Nadja, additional, Mühlenweg, Agnes, additional, Vente, Andreas, additional, Polnick, Stefan, additional, Lämmerhofer, Michael, additional, Gust, Bertolt, additional, Fiedler, Hans-Peter, additional, and Heide, Lutz, additional

Published
2012
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