Interactions of the M. tuberculosis UsfX with the cognate sigma factor SigF and the anti-anti sigma factor RsfA

Malik, Shuja Shafi; Luthra, Amit; Ramachandran, Ravishankar

doi:10.1016/j.bbapap.2008.11.007

Cited by 13 publications

(13 citation statements)

References 35 publications

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“…It has been reported that Usfx forms stable complex with SigF in a nucleotide independent manner and protein‐protein interaction interfaces are very distal from nucleotide binding sites on Usfx. Also, anti‐sigma‐F factor antagonist RsfA interacts with Usfx in its reduced form and positively regulates SigF activity …”

Section: Introductionmentioning

confidence: 60%

“…Also, anti-sigma-F factor antagonist RsfA interacts with Usfx in its reduced form and positively regulates SigF activity. 12 GTPase-Obg (Obg), a GTP-binding protein, belongs to highly conserved protein family that has homologues in prokaryotes, eukaryotes, and archaea. 13 The Obg has diverse functions in different species of bacteria, including cell proliferation, cell signaling, ribosome biogenesis, regulation of replication, transcription, and translation.…”

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confidence: 99%

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Structural insights ofMycobacteriumGTPase-Obg and anti-sigma-F factor Usfx interaction

et al. 2017

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An essential protein for bacterial growth, GTPase-Obg (Obg), is known to play an unknown but crucial role in stress response as its expression increases in Mycobacterium under stress conditions. It is well reported that Obg interacts with anti-sigma-F factor Usfx; however, a detailed analysis and structural characterization of their physical interaction remain undone. In view of above-mentioned points, this study was conceptualized for performing binding analysis and structural characterization of Obg-Usfx interaction. The binding studies were performed by surface plasmon resonance, while in silico docking analysis was done to identify crucial residues responsible for Obg-Usfx interaction. Surface plasmon resonance results clearly suggest that N-terminal and G domains of Obg mainly contribute to Usfx binding. Also, binding constants display strong affinity that was further evident by intermolecular hydrogen bonds and hydrophobic interactions in the predicted complex. Strong interaction between Obg and Usfx supports the view that Obg plays an important role in stress response, essentially required for Mycobacterium survival. As concluded by various studies that Obg is crucial for Mycobacterium survival under stress, this structural information may help us in designing novel and potential inhibitors against resistant Mycobacterium strains.

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Section: Introductionmentioning

confidence: 60%

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confidence: 99%

Structural insights ofMycobacteriumGTPase-Obg and anti-sigma-F factor Usfx interaction

et al. 2017

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“…Notably, the protein Rv1364c is a PSS module organized in four domains corresponding to a PAS, a phosphatase, an anti-r factor and an anti-r factor antagonist domain ( Fig. 2D) (Parida et al, 2005;Sachdeva et al, 2008;Greenstein et al, 2009;Malik et al, 2009;Jaiswal et al, 2010;King-Scott et al, 2011). Interestingly, Rv1364c seems to detect signals itself without upstream sensing module.…”

Section: Activation Of Partner-switching Systemsmentioning

confidence: 99%

Regulation of σ factors by conserved partner switches controlled by divergent signalling systems

Bouillet

Arabet

Jourlin-Castelli

et al. 2018

Environ Microbiol Rep

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Partner-Switching Systems (PSS) are widespread regulatory systems, each comprising a kinase-anti-σ, a phosphorylatable anti-σ antagonist and a phosphatase module. The anti-σ domain quickly sequesters or delivers the target σ factor according to the phosphorylation state of the anti-σ antagonist induced by environmental signals. The PSS components are proteins alone or merged to other domains probably to adapt to the input signals. PSS are involved in major cellular processes including stress response, sporulation, biofilm formation and pathogenesis. Surprisingly, the target σ factors are often unknown and the sensing modules acting upstream from the PSS diverge according to the bacterial species. Indeed, they belong to either two-component systems or complex pathways as the stressosome or Chemosensory Systems (CS). Based on a phylogenetic analysis, we propose that the sensing module in Gram-negative bacteria is often a CS.

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“…SigF is co-transcribed with its anti-σ factor, UsfX, since both genes lie adjacent to each other on the genome. Additionally, UsfX does not appear to contain the HXXXCXXC motif and thus displays a unique method of interaction as well as redox sensing to regulate SigF activity [71]. Intriguingly, this system also has two anti-anti-σ factors, RsfA and RsfB.…”

Section: Regulation Of σ Factors In Response To Redox Stressmentioning

confidence: 99%

“…Intriguingly, this system also has two anti-anti-σ factors, RsfA and RsfB. RsfA and RsfB were shown to bind the UsfX/SigF complex through UsfX interactions under reducing conditions and in an ATP-dependent manner, respectively [71]. In particular, RsfA, which contains four cysteine residues, is stable and complexed to UsfX/SigF under reducing conditions but rapidly degrades under oxidizing conditions when Cys73 and Cys109 form a disulfide bond.…”

Section: Regulation Of σ Factors In Response To Redox Stressmentioning

confidence: 99%

Insights into redox sensing metalloproteins in Mycobacterium tuberculosis

Chim¹,

Johnson²,

Goulding³

2014

Journal of Inorganic Biochemistry

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Mycobacterium tuberculosis, the pathogen that causes tuberculosis, has evolved sophisticated mechanisms for evading assault by the human host. This review focuses on M. tuberculosis regulatory metalloproteins that are sensitive to exogenous stresses attributed to changes in the levels of gaseous molecules (i.e., molecular oxygen, carbon monoxide and nitric oxide) to elicit an intracellular response. In particular, we highlight recent developments on the subfamily of Whi proteins, redox sensing WhiB-like proteins that contain iron-sulfur clusters, sigma factors and their cognate anti-sigma factors of which some are zinc-regulated, and the dormany survival regulon DosS/DosT-DosR heme sensory system. Mounting experimental evidence suggests that these systems contribute to a highly complex and interrelated regulatory network that controls M. tuberculosis biology. This review concludes with a discussion of strategies M. tuberculosis has developed to maintain redox homeostasis, including mechanisms to regulate endogenous nitric oxide and carbon monoxide levels.

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Interactions of the M. tuberculosis UsfX with the cognate sigma factor SigF and the anti-anti sigma factor RsfA

Cited by 13 publications

References 35 publications

Structural insights ofMycobacteriumGTPase-Obg and anti-sigma-F factor Usfx interaction

Structural insights ofMycobacteriumGTPase-Obg and anti-sigma-F factor Usfx interaction

Regulation of σ factors by conserved partner switches controlled by divergent signalling systems

Insights into redox sensing metalloproteins in Mycobacterium tuberculosis

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