4.3 Review

Insights into Protein Allostery in the CsoR/RcnR Family of Transcriptional Repressors

期刊

CHEMISTRY LETTERS
卷 43, 期 1, 页码 20-25

出版社

CHEMICAL SOC JAPAN
DOI: 10.1246/cl.130965

关键词

-

资金

  1. NIGMS NIH HHS [R01 GM097225, R01 GM042569] Funding Source: Medline

向作者/读者索取更多资源

CsoR/Rcra transcriptional repressors adopt a disc-shaped, all a-helical dimer of dimers tetrameric architecture, with a four-helix bundle the key structural feature of the dimer. Individual members of this large family of repressors coordinate Cu(I) or Ni(II)/Co(II) or perform cysteine sulfur chemistry in mitigating the effects of metal or metabolite toxicity, respectively. Here we highlight recent insights into the functional diversity of this fascinating family of repressors.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.3
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

Article Biochemistry & Molecular Biology

Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes

Yifan Zhang, Sambuddha Sen, David P. Giedroc

CHEMBIOCHEM (2020)

Article Biochemistry & Molecular Biology

Staphylococcus aureus Glucose-Induced Biofilm Accessory Protein A (GbaA) Is a Monothiol-Dependent Electrophile Sensor

Abhinaba Ray, Katherine A. Edmonds, Lauren D. Palmer, Eric P. Skaar, David P. Giedroc

BIOCHEMISTRY (2020)

Article Biophysics

1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the ABC transporter solute binding protein PiuA from Streptococcus pneumoniae

Katherine A. Edmonds, Yifan Zhang, Daniel J. Raines, Anne-K Duhme-Klair, David P. Giedroc

BIOMOLECULAR NMR ASSIGNMENTS (2020)

Article Microbiology

Clostridioides difficile Senses and Hijacks Host Heme for Incorporation into an Oxidative Stress Defense System

Reece J. Knippel, Aaron G. Wexler, Jeanette M. Miller, William N. Beavers, Andy Weiss, Valerie de Crecy-Lagard, Katherine A. Edmonds, David P. Giedroc, Eric P. Skaar

CELL HOST & MICROBE (2020)

Review Microbiology

Multi-metal nutrient restriction and crosstalk in metallostasis systems in microbial pathogens

Matthew R. Jordan, Jiefei Wang, Daiana A. Capdevila, David P. Giedroc

CURRENT OPINION IN MICROBIOLOGY (2020)

Article Biotechnology & Applied Microbiology

Cell-free biosensors for rapid detection of water contaminants

Jaeyoung K. Jung, Khalid K. Alam, Matthew S. Verosloff, Daiana A. Capdevila, Morgane Desmau, Phillip R. Clauer, Jeong Wook Lee, Peter Q. Nguyen, Pablo A. Pasten, Sandrine J. Matiasek, Jean-Francois Gaillard, David P. Giedroc, James J. Collins, Julius B. Lucks

NATURE BIOTECHNOLOGY (2020)

Article Biochemistry & Molecular Biology

Structural basis for persulfide-sensing specificity in a transcriptional regulator

Daiana A. Capdevila, Brenna J. C. Walsh, Yifan Zhang, Christopher Dietrich, Giovanni Gonzalez-Gutierrez, David P. Giedroc

Summary: Structural and kinetic analyses of the transcriptional repressor protein SqrR reveal its persulfide selectivity mechanism, shedding light on the coordinated regulation function of cysteine thiol-based transcriptional regulators in cellular redox homeostasis.

NATURE CHEMICAL BIOLOGY (2021)

Review Biochemistry & Molecular Biology

Molecular Evolution of Transition Metal Bioavailability at the Host-Pathogen Interface

Giuliano T. Antelo, Alejandro J. Vila, David P. Giedroc, Daiana A. Capdevila

Summary: The molecular evolution of the adaptive response at the host-pathogen interface, known as an 'arms race,' involves strategies employed by the innate immune system to starve microbes of metals, countered by pathogens maintaining access to metal ions. Recent exploration of how evolution repurposes host and pathogen proteins to perform new functions is discussed, with a focus on metalloproteins restricting bacterial access to transition metals. Coevolution with bacterial metal acquisition systems and the evolution of metallo-?-lactamases in the context of host-imposed nutritional immunity are also examined.

TRENDS IN MICROBIOLOGY (2021)

Article Biochemistry & Molecular Biology

Functional asymmetry and chemical reactivity of CsoR family persulfide sensors

Joseph N. Fakhoury, Yifan Zhang, Katherine A. Edmonds, Mauro Bringas, Justin L. Luebke, Giovanni Gonzalez-Gutierrez, Daiana A. Capdevila, David P. Giedroc

Summary: CstR is a protein that senses persulfides and regulates bacterial response to hydrogen sulfide and other oxidized reactive sulfur species. Research suggests that the specificity of CstRs to different oxidants is determined by their sequence, structural, and kinetic features.

NUCLEIC ACIDS RESEARCH (2021)

Article Biochemistry & Molecular Biology

Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis

Andy Weiss, Caitlin C. Murdoch, Katherine A. Edmonds, Matthew R. Jordan, Andrew J. Monteith, Yasiru R. Perera, Aslin M. Rodriguez Nassif, Amber M. Petoletti, William N. Beavers, Matthew J. Munneke, Sydney L. Drury, Evan S. Krystofiak, Kishore Thalluri, Hongwei Wu, Angela R. S. Kruse, Richard D. DiMarchi, Richard M. Caprioli, Jeffrey M. Spraggins, Walter J. Chazin, David P. Giedroc, Eric P. Skaar

Summary: This study reveals the existence of a conserved COG0523 protein family in vertebrates and assigns them an important role in regulating cellular zinc homeostasis.
Article Microbiology

Bacterial hydrophilins promote pathogen desiccation tolerance

Erin R. Green, Joseph N. Fakhoury, Andrew J. Monteith, Hualiang Pi, David P. Giedroc, Eric P. Skaar

Summary: This study reveals that Acinetobacter baumannii causes more virulent pneumonia following desiccation and identifies the genetic requirements for desiccation. The disruption of Lon protease enhances desiccation tolerance, while bacterial hydrophilins DtpA and DtpB play a crucial role in this process.

CELL HOST & MICROBE (2022)

Article Biochemistry & Molecular Biology

SifR is an Rrf2-family quinone sensor associated with catechol iron uptake in Streptococcus pneumoniae D39

Yifan Zhang, Julia E. Martin, Katherine A. Edmonds, Malcolm E. Winkler, David P. Giedroc

Summary: The novel virulence associated Rrf2-family transcriptional repressor SifR regulates genes involved in iron uptake and stress response in Streptococcus pneumoniae, providing insight into how the bacterium acquires iron sources in the host environment. This study sheds light on the mechanisms by which the pathogen adapts to oxidative stress and utilizes catechol-derived iron sources for survival.

JOURNAL OF BIOLOGICAL CHEMISTRY (2022)

Article Biochemistry & Molecular Biology

Metabolic and Structural Insights into Hydrogen Sulfide Mis-Regulation in Enterococcus faecalis

Brenna J. C. Walsh, Sofia Soares Costa, Katherine A. Edmonds, Jonathan C. Trinidad, Federico M. Issoglio, Jose A. Brito, David P. Giedroc

Summary: Hydrogen sulfide (H2S) is a cytoprotective agent used by bacteria in response to stress, and this study found that exogenous sulfide alters protein abundance and metabolic reactions in the gut microorganism Enterococcus faecalis, potentially affecting fatty acid pathways.

ANTIOXIDANTS (2022)

Article Biochemistry & Molecular Biology

COG0523 proteins: a functionally diverse family of transition metal-regulated G3E P-loop GTP hydrolases from bacteria to man

Katherine A. Edmonds, Matthew R. Jordan, David P. Giedroc

Summary: This study uses genomic enzymology tools to analyze over 80,000 sequences related to zinc metallochaperones, revealing multiple distinct clusters including characterized and uncharacterized COG0523 proteins. Through the analysis of these clusters, new perspectives on COG0523 proteins as cellular reporters of nutrient stress induced by zinc limitation are discussed.

METALLOMICS (2021)

Article Biology

Proteomics Profiling of S-sulfurated Proteins in Acinetobacter baumannii

Brenna J. C. Walsh, David P. Giedroc

Summary: Hydrogen sulfide has been found to play a crucial role in bacterial cytoprotection against host immune response, possibly through the formation of reactive sulfur species derived from H2S. A new analytical method has been developed and successfully applied to studying protein persulfidation in bacterial cells, particularly in a major human pathogen. This method allows quantification and identification of persulfidation sites in the proteome, which may serve as regulatory modifications that can be validated through biochemical studies.

BIO-PROTOCOL (2021)

暂无数据