The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) σ factor protein family

Staroń, Anna; Sofia, Heidi J.; Dietrich, Sascha; Ulrich, Luke E.; Liesegang, Heiko; Mascher, Thorsten

doi:10.1111/j.1365-2958.2009.06870.x

Cited by 368 publications

(685 citation statements)

References 108 publications

(249 reference statements)

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“…This sequence matches the known EcfG regulatory sequence described by Mascher and colleagues (32). Our data inform a model in which the PhyR/ E1 regulatory system controls acute stress response genes but also functions to modulate components of the B. abortus cell envelope (O-chain and flagellum).…”

Section: E1mentioning

confidence: 48%

“…It is now known that ␣-proteobacterial species encode a novel regulatory system in which the hybrid -like/receiver protein, PhyR, functions as a positive regulator of the EcfG -dependent GSR (10). Specifically, PhyRϳP activates an ECF factor of the EcfG family (32) by directly binding the antiEcfG protein, NepR (10). In other words, PhyR is a phosphorylation-dependent anti-antifactor.…”

Section: Discussionmentioning

confidence: 99%

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The Brucella abortus General Stress Response System Regulates Chronic Mammalian Infection and Is Controlled by Phosphorylation and Proteolysis

Kim

Caswell

Foreman

et al. 2013

Journal of Biological Chemistry

119

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Background: Virulence of pathogenic bacteria is often determined by their ability to adapt to stress. Results: The Brucella abortus general stress response (GSR) system is required for chronic mammalian infection and is regulated by phosphorylation and proteolysis. Conclusion: The B. abortus GSR signaling pathway has multiple layers of post-translational control and is a determinant of chronic infection. Significance: This study provides new, molecular level insight into chronic Brucella infection.

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Section: E1mentioning

confidence: 48%

Section: Discussionmentioning

confidence: 99%

The Brucella abortus General Stress Response System Regulates Chronic Mammalian Infection and Is Controlled by Phosphorylation and Proteolysis

Kim

Caswell

Foreman

et al. 2013

Journal of Biological Chemistry

119

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“…Alternative sigma factors, the RNA polymerase subunits that confer promoter specificity, provide a powerful way to redirect gene expression globally toward specific regulons (2). The largest and most diverse group of alternative sigma factors comprises the group IV (or extracytoplasmic function [ECF]) sigma factors of the σ 70 superfamily, which are best known for their role in adaptation to environmental changes (3,4). In contrast to other sigma factors, ECF sigma factors consist only of the two core domains, σ 2 and σ 4 , which are required for recognition of the -10 and -35 promoter binding determinants, respectively, in addition to RNA polymerase binding.…”

mentioning

confidence: 99%

Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria

Campagne

Damberger

Kaczmarczyk³

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Reprogramming gene expression is an essential component of adaptation to changing environmental conditions. In bacteria, a widespread mechanism involves alternative sigma factors that redirect transcription toward specific regulons. The activity of sigma factors is often regulated through sequestration by cognate anti-sigma factors; however, for most systems, it is not known how the activity of the anti-sigma factor is controlled to release the sigma factor. Recently, the general stress response sigma factor in Alphaproteobacteria, σ EcfG , was identified. σ EcfG is inactivated by the anti-sigma factor NepR, which is itself regulated by the response regulator PhyR. This key regulator sequesters NepR upon phosphorylation of its PhyR receiver domain via its σ EcfG sigma factor-like output domain (PhyR SL ). To understand the molecular basis of the PhyR-mediated partner-switching mechanism, we solved the structure of the PhyR SL –NepR complex using NMR. The complex reveals an unprecedented anti-sigma factor binding mode: upon PhyR SL binding, NepR forms two helices that extend over the surface of the PhyR SL subdomains. Homology modeling and comparative analysis of NepR, PhyR SL , and σ EcfG mutants indicate that NepR contacts both proteins with the same determinants, showing sigma factor mimicry at the atomic level. A lower density of hydrophobic interactions, together with the absence of specific polar contacts in the σ EcfG –NepR complex model, is consistent with the higher affinity of NepR for PhyR compared with σ EcfG . Finally, by reconstituting the partner switch in vitro, we demonstrate that the difference in affinity of NepR for its partners is sufficient for the switch to occur.

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“…Sigma factors are small subunits that associate with the RNA polymerase core enzyme, allowing promoter recognition and initiation of gene transcription. Apart from a primary sigma factor that controls expression of genes required for general functions, bacteria contain a variable number of alternative sigma factors of which the ECF constitute the largest group (10,11).…”

mentioning

confidence: 99%

“…ECF are usually co-expressed with antisigma factors that bind to and sequester the sigma factor to keep it in an inactive state (10,11). In Gram-negative bacteria, these anti-sigma factors are typically cytoplasmic membrane proteins that contain a short cytosolic N-terminal domain of 85-90 amino acids that binds the ECF linked to a larger periplasmic C-terminal region by a single transmembrane segment (8) (see Fig.…”

mentioning

confidence: 99%

Self-cleavage of the Pseudomonas aeruginosa Cell-surface Signaling Anti-sigma Factor FoxR Occurs through an N-O Acyl Rearrangement

Bastiaansen

Ulsen

Bitter

et al. 2015

Journal of Biological Chemistry

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Background: Many transmembrane anti-sigma factors, including P. aeruginosa FoxR, undergo periplasmic self-cleavage by an unknown mechanism. Results: Presence of an OH or SH group at ϩ1 of the cleavage site is essential for FoxR self-cleavage. Conclusion: FoxR self-cleavage is mediated by an N-O acyl rearrangement. Significance: The complex proteolytic network that modulates alternative sigma factor activity in Gram-negative bacteria also includes an enzyme-independent step.

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The third pillar of bacterial signal transduction: classification of the extracytoplasmic function (ECF) σ factor protein family

Abstract: SummaryThe ability of a bacterial cell to monitor and adaptively respond to its environment is crucial for survival.

Cited by 368 publications

References 108 publications

The Brucella abortus General Stress Response System Regulates Chronic Mammalian Infection and Is Controlled by Phosphorylation and Proteolysis

The Brucella abortus General Stress Response System Regulates Chronic Mammalian Infection and Is Controlled by Phosphorylation and Proteolysis

Structural basis for sigma factor mimicry in the general stress response of Alphaproteobacteria

Self-cleavage of the Pseudomonas aeruginosa Cell-surface Signaling Anti-sigma Factor FoxR Occurs through an N-O Acyl Rearrangement

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