RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis
about
Mycobacterium tuberculosis RsdA provides a conformational rationale for selective regulation of -factor activity by proteolysisA Mycobacterium tuberculosis sigma factor network responds to cell-envelope damage by the promising anti-mycobacterial thioridazineInteraction of Mycobacterium tuberculosis RshA and SigH is mediated by salt bridgesMycobacterium tuberculosis MT2816 encodes a key stress-response regulatorCharacterization of a Clp protease gene regulator and the reaeration response in Mycobacterium tuberculosisNon-monotonic Response to Monotonic Stimulus: Regulation of Glyoxylate Shunt Gene-Expression Dynamics in Mycobacterium tuberculosisPhenotypic heterogeneity in mycobacterial stringent response.Comparative genomics of the Mycobacterium signaling architecture and implications for a novel live attenuated Tuberculosis vaccine.The C-terminus of ClpC1 of Mycobacterium tuberculosis is crucial for its oligomerization and functionRegulated Expression Systems for Mycobacteria and Their ApplicationsMycobacterium tuberculosis ClpP proteases are co-transcribed but exhibit different substrate specificities.The HtrA-like serine protease PepD interacts with and modulates the Mycobacterium tuberculosis 35-kDa antigen outer envelope protein.The Mycobacterium tuberculosis Clp gene regulator is required for in vitro reactivation from hypoxia-induced dormancy.The Mycobacterium tuberculosis Rv2745c plays an important role in responding to redox stress.Oxidative stress protection by polyphosphate--new roles for an old playerInteraction of Mycobacterium tuberculosis elongation factor Tu with GTP is regulated by phosphorylation.Pharmacological inhibition of the ClpXP protease increases bacterial susceptibility to host cathelicidin antimicrobial peptides and cell envelope-active antibiotics.The interplay of multiple feedback loops with post-translational kinetics results in bistability of mycobacterial stress responseRv2744c Is a PspA Ortholog That Regulates Lipid Droplet Homeostasis and Nonreplicating Persistence in Mycobacterium tuberculosis.Dual positive feedback regulation of protein degradation of an extra-cytoplasmic function σ factor for cell differentiation in Streptomyces coelicolor.Osmosensory signaling in Mycobacterium tuberculosis mediated by a eukaryotic-like Ser/Thr protein kinase.The MprB extracytoplasmic domain negatively regulates activation of the Mycobacterium tuberculosis MprAB two-component system.Insights into redox sensing metalloproteins in Mycobacterium tuberculosis.Proteases in Mycobacterium tuberculosis pathogenesis: potential as drug targets.σ(ECF) factors of gram-positive bacteria: a focus on Bacillus subtilis and the CMNR groupRedox regulation of cancer metastasis: molecular signaling and therapeutic opportunities.Improved understanding of pathogenesis from protein interactions in Mycobacterium tuberculosis.Thiol-based redox switches in prokaryotes.Components of the Rv0081-Rv0088 locus, which encodes a predicted formate hydrogenlyase complex, are coregulated by Rv0081, MprA, and DosR in Mycobacterium tuberculosis.The Ser/Thr Protein Kinase Protein-Protein Interaction Map of M. tuberculosis.Validation of the essential ClpP protease in Mycobacterium tuberculosis as a novel drug target.σ(E) -dependent activation of RbpA controls transcription of the furA-katG operon in response to oxidative stress in mycobacteria.AAA+ Machines of Protein Destruction in Mycobacteria.Novel mechanism of gene regulation: the protein Rv1222 of Mycobacterium tuberculosis inhibits transcription by anchoring the RNA polymerase onto DNA.The Psp system of Mycobacterium tuberculosis integrates envelope stress-sensing and envelope-preserving functions.Xer site-specific recombination, an efficient tool to introduce unmarked deletions into mycobacteria.Monitoring global protein thiol-oxidation and protein S-mycothiolation in Mycobacterium smegmatis under hypochlorite stress.The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring.Substrate delivery by the AAA+ ClpX and ClpC1 unfoldases activates the mycobacterial ClpP1P2 peptidaseThe prokaryotic ClpQ protease plays a key role in growth and development of mitochondria in Plasmodium falciparum.
P2860
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P2860
RseA, the SigE specific anti-sigma factor of Mycobacterium tuberculosis, is inactivated by phosphorylation-dependent ClpC1P2 proteolysis
description
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2010
@ast
im Februar 2010 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2010/02/01)
@sk
vědecký článek publikovaný v roce 2010
@cs
wetenschappelijk artikel (gepubliceerd op 2010/02/01)
@nl
наукова стаття, опублікована в лютому 2010
@uk
مقالة علمية (نشرت في فبراير 2010)
@ar
name
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@ast
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@en
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@nl
type
label
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@ast
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@en
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@nl
prefLabel
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@ast
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@en
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@nl
P2093
P2860
P921
P1476
RseA, the SigE specific anti-s ...... -dependent ClpC1P2 proteolysis
@en
P2093
Joyoti Basu
Kamakshi Sureka
Manikuntala Kundu
Partha Mukherjee
Subhasis Barik
P2860
P304
P356
10.1111/J.1365-2958.2009.07008.X
P407
P577
2010-02-01T00:00:00Z