MecA, an adaptor protein necessary for ClpC chaperone activity

scholarly article

MecA, an adaptor protein necessary for ClpC chaperone activity is …
instance of (P31):
scholarly articleQ13442814

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P819ADS bibcode2003PNAS..100.2306S
P356DOI10.1073/PNAS.0535717100
P932PMC publication ID151336
P698PubMed publication ID12598648
P5875ResearchGate publication ID10889117

P50authorBernd BukauQ20742605
David A. DouganQ40570504
Kürşad TurgayQ45344458
Axel MogkQ61961358
Tilman SchlothauerQ114776946
P2860cites workCompetence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factorQ24533414
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteinsQ27931364
Protein disaggregation mediated by heat-shock protein Hsp104.Q27940314
AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexesQ28131706
DNA uptake in bacteriaQ28146170
Molecular chaperones in the cytosol: from nascent chain to folded proteinQ28205903
AAA+ superfamily ATPases: common structure--diverse functionQ28208908
The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperoneQ28301089
Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressorQ28348879
The RssB response regulator directly targets sigma(S) for degradation by ClpXPQ28359852
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaKQ29618850
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.Q30322959
Posttranslational quality control: folding, refolding, and degrading proteins.Q30323825
Chaperone rings in protein folding and degradation.Q33740150
Global transcriptional response of Bacillus subtilis to heat shockQ33997293
ClpS, a substrate modulator of the ClpAP machineQ34121960
Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilisQ34314108
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone networkQ34505864
A specificity-enhancing factor for the ClpXP degradation machineQ34511105
MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a pleiotropic regulator controlling competence gene expression and growth at high temperatureQ34725844
ClpA mediates directional translocation of substrate proteins into the ClpP proteaseQ35039085
A molecular chaperone, ClpA, functions like DnaK and DnaJ.Q35968116
Growth medium-independent genetic competence mutants of Bacillus subtilisQ36257605
Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperonesQ36390259
Regulation of RpoS proteolysis in Escherichia coli: the response regulator RssB is a recognition factor that interacts with the turnover element in RpoSQ37211276
The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteinsQ39499815
Global analysis of the general stress response of Bacillus subtilisQ39504975
A MecA paralog, YpbH, binds ClpC, affecting both competence and sporulationQ39678820
Stress induction of clpC in Bacillus subtilis and its involvement in stress toleranceQ39932157
HSP100/Clp proteins: a common mechanism explains diverse functionsQ41083709
Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.Q42247311
Proteome and transcriptome based analysis of Bacillus subtilis cells overproducing an insoluble heterologous protein.Q43599951
Genome-wide analysis of the general stress response in Bacillus subtilisQ43725791
Roles of the two ClpC ATP binding sites in the regulation of competence and the stress responseQ43808794
Dynamics of substrate denaturation and translocation by the ClpXP degradation machineQ47235359
ClpP of Bacillus subtilis is required for competence development, motility, degradative enzyme synthesis, growth at high temperature and sporulationQ48038992
On the conformation of caseins. Optical rotatory propertiesQ72779852
Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilisQ72988435
ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coliQ73019220
ClpX-mediated remodeling of mu transpososomes: selective unfolding of subunits destabilizes the entire complexQ74484737
Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilisQ77086667
Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX proteaseQ77726447
The N- and C-terminal domains of MecA recognize different partners in the competence molecular switchQ78127833
P433issue5
P407language of work or nameEnglishQ1860
P921main subjectmolecular chaperonesQ422496
P304page(s)2306-2311
P577publication date2003-02-21
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleMecA, an adaptor protein necessary for ClpC chaperone activity
P478volume100

Reverse relations

cites work (P2860)
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