ArticleJournal of molecular biology2010
Structural and biochemical bases for the redox sensitivity of Mycobacterium tuberculosis RslA.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Article
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- DUF2285 is a novel helix-turn-helix domain variant that orchestrates both activation and antiactivation of conjugative element transfer in proteobacteria.Nucleic acids research · 2023Article
- Overlapping SigH and SigE sigma factor regulons inFrontiers in microbiology · 2022Article
- Model peptide for anti-sigma factor domain HHCC zinc fingers: high reactivity towardChemical science · 2019Article
- Selectivity among Anti-σ Factors byJournal of bacteriology · 2019Article
- Themes and variations in gene regulation by extracytoplasmic function (ECF) sigma factors.Current opinion in microbiology · 2017Review
- Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G.The Journal of biological chemistry · 2016Article
- Prediction of redox-sensitive cysteines using sequential distance and other sequence-based features.BMC bioinformatics · 2016Article
- The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core.Nature communications · 2016Article
- Mechanistic Implications of the Unique Structural Features and Dimerization of the Cytoplasmic Domain of the Pseudomonas Sigma Regulator, PupR.Biochemistry · 2015Article
- Structural biology of bacterial RNA polymerase.Biomolecules · 2015Review
- Crystallization and preliminary X-ray crystallographic analysis of carboxyl-terminal region 4 of SigR from Streptomyces coelicolor A3(2).Acta crystallographica. Section F, Structural biology communications · 2014Article
- Insights into redox sensing metalloproteins in Mycobacterium tuberculosis.Journal of inorganic biochemistry · 2014Review
- Comparative genomics of the Mycobacterium signaling architecture and implications for a novel live attenuated Tuberculosis vaccine.Human vaccines & immunotherapeutics · 2014Article
- Oxidant sensing by reversible disulfide bond formation.The Journal of biological chemistry · 2013Review
- A novel P(1B)-type Mn2+-transporting ATPase is required for secreted protein metallation in mycobacteria.The Journal of biological chemistry · 2013Article
- Mycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of σ-factor activity by proteolysis.Nucleic acids research · 2013Article
- Structural basis of a protein partner switch that regulates the general stress response of α-proteobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- ROS-Mediated Signalling in Bacteria: Zinc-Containing Cys-X-X-Cys Redox Centres and Iron-Based Oxidative Stress.Journal of signal transduction · 2012Article
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3 authors.
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Abstract
An effective transcriptional response to redox stimuli is of particular importance for Mycobacterium tuberculosis, as it adapts to the environment of host alveoli and macrophages. The M. tuberculosis sigma factor sigma(L) regulates the expression of genes involved in cell-wall and polyketide syntheses. sigma(L) interacts with the cytosolic anti-sigma domain of a membrane-associated protein, RslA. Here we demonstrate that RslA binds Zn(2+) and can sequester sigma(L) in a reducing environment. In response to an oxidative stimulus, proximal cysteines in the CXXC motif of RslA form a disulfide bond, releasing bound Zn(2+). This results in a substantial rearrangement of the sigma(L)/RslA complex, leading to an 8-fold decrease in the affinity of RslA for sigma(L). The crystal structure of the -35-element recognition domain of sigma(L), sigma(4)(L), bound to RslA reveals that RslA inactivates sigma(L) by sterically occluding promoter DNA and RNA polymerase binding sites. The crystal structure further reveals that the cysteine residues that coordinate Zn(2+) in RslA are solvent exposed in the complex, thus providing a structural basis for the redox sensitivity of RslA. The biophysical parameters of sigma(L)/RslA interactions provide a template for understanding how variations in the rate of Zn(2+) release and associated conformational changes could regulate the activity of a Zn(2+)-associated anti-sigma factor.
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