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261 results on '"STOGIOS, Peter J."'

1. Addendum: A small molecule produced by Lactobacillus species blocks Candida albicans filamentation by inhibiting a DYRK1-family kinase

Author

MacAlpine, Jessie, Daniel-Ivad, Martin, Liu, Zhongle, Yano, Junko, Revie, Nicole M., Todd, Robert T., Stogios, Peter J., Sanchez, Hiram, O’Meara, Teresa R., Tompkins, Thomas A., Savchenko, Alexei, Selmecki, Anna, Veri, Amanda O., Andes, David R., Fidel, Jr., Paul L., Robbins, Nicole, Nodwell, Justin, Whitesell, Luke, and Cowen, Leah E.

Published
2024
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7. Global atlas of predicted functional domains in Legionella pneumophila Dot/Icm translocated effectors

Author

Patel, Deepak T, primary, Stogios, Peter J, additional, Jaroszewski, Lukasz, additional, Urbanus, Malene L, additional, Sedova, Mayya, additional, Semper, Cameron, additional, Le, Cathy, additional, Takkouche, Abraham, additional, Ichii, Keita, additional, Innabi, Julie, additional, Patel, Dhruvin H, additional, Ensminger, Alexander W, additional, Godzik, Adam, additional, and Savchenko, Alexei, additional

Published
2024
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9. Three mutations repurpose a plant karrikin receptor to a strigolactone receptor

Author

Arellano-Saab, Amir, Bunsick, Michael, Galib, Hasan Al, Zhao, Wenda, Schuetz, Stefan, Bradley, James Michael, Xu, Zhenhua, Adityani, Claresta, Subha, Asrinus, McKay, Hayley, de Saint Germain, Alexandre, Boyer, François-Didier, McErlean, Christopher S. P., Toh, Shigeo, McCourt, Peter, Stogios, Peter J., and Lumba, Shelley

Published
2021

14. Functional and structural characterization of an IclR family transcription factor for the development of dicarboxylic acid biosensors.

Author

Pham, Chester, Nasr, Mohamed A., Skarina, Tatiana, Di Leo, Rosa, Kwan, David H., Martin, Vincent J. J., Stogios, Peter J., Mahadevan, Radhakrishnan, and Savchenko, Alexei

Abstract

Prokaryotic transcription factors (TFs) regulate gene expression in response to small molecules, thus representing promising candidates as versatile small molecule‐detecting biosensors valuable for synthetic biology applications. The engineering of such biosensors requires thorough in vitro and in vivo characterization of TF ligand response as well as detailed molecular structure information. In this work, we functionally and structurally characterize the Pca regulon regulatory protein (PcaR) transcription factor belonging to the IclR transcription factor family. Here, we present in vitro functional analysis of the ligand profile of PcaR and the construction of genetic circuits for the characterization of PcaR as an in vivo biosensor in the model eukaryote Saccharomyces cerevisiae. We report the crystal structures of PcaR in the apo state and in complex with one of its ligands, succinate, which suggests the mechanism of dicarboxylic acid recognition by this transcription factor. This work contributes key structural and functional insights enabling the engineering of PcaR for dicarboxylic acid biosensors, in addition to providing more insights into the IclR family of regulators. [ABSTRACT FROM AUTHOR]

Published
2024
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20. The activity of CouR, a MarR family transcriptional regulator, is modulated through a novel molecular mechanism

Author

Otani, Hiroshi, Stogios, Peter J, Xu, Xiaohui, Nocek, Boguslaw, Li, Shu-Nan, Savchenko, Alexei, and Eltis, Lindsay D

Subjects
Biochemistry and Cell Biology, Biological Sciences, Genetics, Acyl Coenzyme A, Alanine, Amino Acid Substitution, Arginine, Bacterial Proteins, Binding Sites, Coenzyme A, Coumaric Acids, Crystallography, X-Ray, DNA, Gene Expression Regulation, Bacterial, Hydrophobic and Hydrophilic Interactions, Ligands, Models, Molecular, Promoter Regions, Genetic, Propionates, Protein Binding, Protein Interaction Domains and Motifs, Protein Multimerization, Repressor Proteins, Rhodococcus, Static Electricity, Transcription, Genetic, Environmental Sciences, Information and Computing Sciences, Developmental Biology, Biological sciences, Chemical sciences, Environmental sciences
Abstract

CouR, a MarR-type transcriptional repressor, regulates the cou genes, encoding p-hydroxycinnamate catabolism in the soil bacterium Rhodococcus jostii RHA1. The CouR dimer bound two molecules of the catabolite p-coumaroyl-CoA (Kd = 11 ± 1 μM). The presence of p-coumaroyl-CoA, but neither p-coumarate nor CoASH, abrogated CouR's binding to its operator DNA in vitro. The crystal structures of ligand-free CouR and its p-coumaroyl-CoA-bound form showed no significant conformational differences, in contrast to other MarR regulators. The CouR-p-coumaroyl-CoA structure revealed two ligand molecules bound to the CouR dimer with their phenolic moieties occupying equivalent hydrophobic pockets in each protomer and their CoA moieties adopting non-equivalent positions to mask the regulator's predicted DNA-binding surface. More specifically, the CoA phosphates formed salt bridges with predicted DNA-binding residues Arg36 and Arg38, changing the overall charge of the DNA-binding surface. The substitution of either arginine with alanine completely abrogated the ability of CouR to bind DNA. By contrast, the R36A/R38A double variant retained a relatively high affinity for p-coumaroyl-CoA (Kd = 89 ± 6 μM). Together, our data point to a novel mechanism of action in which the ligand abrogates the repressor's ability to bind DNA by steric occlusion of key DNA-binding residues and charge repulsion of the DNA backbone.

Published
2016

21. A small molecule produced by Lactobacillus species blocks Candida albicans filamentation by inhibiting a DYRK1-family kinase

Author

MacAlpine, Jessie, Daniel-Ivad, Martin, Liu, Zhongle, Yano, Junko, Revie, Nicole M., Todd, Robert T., Stogios, Peter J., Sanchez, Hiram, O’Meara, Teresa R., Tompkins, Thomas A., Savchenko, Alexei, Selmecki, Anna, Veri, Amanda O., Andes, David R., Fidel, Jr., Paul L., Robbins, Nicole, Nodwell, Justin, Whitesell, Luke, and Cowen, Leah E.

Published
2021
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22. An interbacterial toxin inhibits target cell growth by synthesizing (p)ppApp

Author

Ahmad, Shehryar, Wang, Boyuan, Walker, Matthew D., Tran, Hiu-Ki R., Stogios, Peter J., Savchenko, Alexei, and Grant, Robert A.

Subjects
Metabolites -- Usage, Bacterial toxins -- Physiological aspects -- Structure, Cells -- Control -- Growth, Pseudomonas aeruginosa -- Physiological aspects, Company growth, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Bacteria have evolved sophisticated mechanisms to inhibit the growth of competitors.sup.1. One such mechanism involves type VI secretion systems, which bacteria can use to inject antibacterial toxins directly into neighbouring cells. Many of these toxins target the integrity of the cell envelope, but the full range of growth inhibitory mechanisms remains unknown.sup.2. Here we identify a type VI secretion effector, Tas1, in the opportunistic pathogen Pseudomonas aeruginosa. The crystal structure of Tas1 shows that it is similar to enzymes that synthesize (p)ppGpp, a broadly conserved signalling molecule in bacteria that modulates cell growth rate, particularly in response to nutritional stress.sup.3. However, Tas1 does not synthesize (p)ppGpp; instead, it pyrophosphorylates adenosine nucleotides to produce (p)ppApp at rates of nearly 180,000 molecules per minute. Consequently, the delivery of Tas1 into competitor cells drives rapid accumulation of (p)ppApp, depletion of ATP, and widespread dysregulation of essential metabolic pathways, thereby resulting in target cell death. Our findings reveal a previously undescribed mechanism for interbacterial antagonism and demonstrate a physiological role for the metabolite (p)ppApp in bacteria. The bacterium Pseudomonas aeruginosa attacks competing bacteria using the toxin Tas1, which pyrophosphorylates adenosine nucleotides to generate (p)ppApp, thereby depleting ATP and disrupting multiple cellular functions., Author(s): Shehryar Ahmad [sup.1] [sup.2] , Boyuan Wang [sup.3] , Matthew D. Walker [sup.2] , Hiu-Ki R. Tran [sup.1] [sup.2] , Peter J. Stogios [sup.4] [sup.5] , Alexei Savchenko [sup.4] [...]

Published
2019
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28. Legionella pneumophila S1P-lyase targets host sphingolipid metabolism and restrains autophagy

Author

Rolando, Monica, Escoll, Pedro, Nora, Tamara, Botti, Joëlle, Boitez, Valérie, Bedia, Carmen, Daniels, Craig, Abraham, Gilu, Stogios, Peter J., Skarina, Tatiana, Christophe, Charlotte, Dervins-Ravault, Delphine, Cazalet, Christel, Hilbi, Hubert, Rupasinghe, Thusitha W. T., Tull, Dedreia, McConville, Malcolm J., Ong, Sze Ying, Hartland, Elizabeth L., Codogno, Patrice, Levade, Thierry, Naderer, Thomas, Savchenko, Alexei, and Buchrieser, Carmen

Published
2016

40. Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT family

Author

Stogios, Peter J, primary, Bordeleau, Emily, additional, Xu, Zhiyu, additional, Skarina, Tatiana, additional, Evdokimova, Elena, additional, Chou, Sommer, additional, Luke, Diorio-Toth, additional, D'Souza, Alaric, additional, Patel, Sanket, additional, Dantas, Gautam, additional, Wright, Gerard, additional, and Savchenko, Alexei, additional

Published
2021
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43. Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats

Author

Alcaide, María, Stogios, Peter J., Lafraya, Álvaro, Tchigvintsev, Anatoli, Flick, Robert, Bargiela, Rafael, Chernikova, Tatyana N., Reva, Oleg N., Hai, Tran, Leggewie, Christian C., Katzke, Nadine, La Cono, Violetta, Matesanz, Ruth, Jebbar, Mohamed, Jaeger, Karl-Erich, Yakimov, Michail M., Yakunin, Alexander F., Golyshin, Peter N., Golyshina, Olga V., Savchenko, Alexei, and Ferrer, Manuel

Published
2015
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44. Structural analysis of a hormone-bound Strigastrigolactone receptor

Author

Arellano-Saab, Amir, Skarina, Tatiana, Xu, Zhenhua, McErlean, Christopher S. P., Savchenko, Alexei, Lumba, Shelley, Stogios, Peter J., and McCourt, Peter

Abstract

Strigolactones (SLs) regulate many aspects of plant development, but ambiguities remain about how this hormone is perceived because SL-complexed receptor structures do not exist. We find that when SL binds the Strigareceptor, ShHTL5, a series of conformational changes relative to the unbound state occur, but these events are not sufficient for signalling. Ligand-complexed receptors, however, form internal tunnels that posit an explanation for how SL exits its receptor after hydrolysis.

Published
2023
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46. An interbacterial toxin inhibits target cell growth by synthesizing (p)ppApp

Author

Massachusetts Institute of Technology. Department of Biology, Ahmad, Shehryar, Wang, Boyuan, Walker, Matthew D., Tran, Hiu-Ki R., Stogios, Peter J., Savchenko, Alexei, Grant, Robert A, McArthur, Andrew G., Laub, Michael T, Whitney, John C., Massachusetts Institute of Technology. Department of Biology, Ahmad, Shehryar, Wang, Boyuan, Walker, Matthew D., Tran, Hiu-Ki R., Stogios, Peter J., Savchenko, Alexei, Grant, Robert A, McArthur, Andrew G., Laub, Michael T, and Whitney, John C.

Abstract

Bacteria have evolved sophisticated mechanisms to inhibit the growth of competitors1. One such mechanism involves type VI secretion systems, which bacteria can use to inject antibacterial toxins directly into neighbouring cells. Many of these toxins target the integrity of the cell envelope, but the full range of growth inhibitory mechanisms remains unknown2. Here we identify a type VI secretion effector, Tas1, in the opportunistic pathogen Pseudomonas aeruginosa. The crystal structure of Tas1 shows that it is similar to enzymes that synthesize (p)ppGpp, a broadly conserved signalling molecule in bacteria that modulates cell growth rate, particularly in response to nutritional stress3. However, Tas1 does not synthesize (p)ppGpp; instead, it pyrophosphorylates adenosine nucleotides to produce (p)ppApp at rates of nearly 180,000 molecules per minute. Consequently, the delivery of Tas1 into competitor cells drives rapid accumulation of (p)ppApp, depletion of ATP, and widespread dysregulation of essential metabolic pathways, thereby resulting in target cell death. Our findings reveal a previously undescribed mechanism for interbacterial antagonism and demonstrate a physiological role for the metabolite (p)ppApp in bacteria., National Institutes of Health (Grant R01-GM082899)

Published
2020

47. The BACK domain in BTB-kelch proteins

Author

Stogios, Peter J. and Prive, Gilbert G.

Subjects
Biochemistry -- Research, Proteins -- Research, Biological sciences, Chemistry
Abstract

A novel conserved motif--the BACK (for BTB and C-terminal Kelch) domain--is found in the majority of proteins that contain both the BTB domain and kelch repeats. Many kelch-repeat proteins are involved in organization of the cytoskeleton via interaction with actin and intermediate filaments, whereas BTB domains have multiple cellular roles, including recruitment to E3 ubiquitin ligase complexes. The identification of the BACK domain in BTB and kelch proteins, and its high conservation across metazoan genomes, suggest an important function for this domain with a possible role in substrate orientation in Cullin3-based E3 ligase complexes.

Published
2004

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