메뉴 건너뛰기




Volumn 186, Issue 17, 2004, Pages 5856-5864

The ClpP peptidase is the major determinant of bulk protein turnover in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL ENZYME; ENDOPEPTIDASE CLP;

EID: 4344696027     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.17.5856-5864.2004     Document Type: Article
Times cited : (57)

References (35)
  • 1
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos, C., and J. Spizizen. 1961. Requirements for transformation in Bacillus subtilis. J. Bacteriol. 81:741-746.
    • (1961) J. Bacteriol. , vol.81 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 2
    • 0344329881 scopus 로고    scopus 로고
    • Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis
    • Bernhardt, J., K. Buttner, C. Scharf, and M. Hecker. 1999. Dual channel imaging of two-dimensional electropherograms in Bacillus subtilis. Electrophoresis 20:2225-2240.
    • (1999) Electrophoresis , vol.20 , pp. 2225-2240
    • Bernhardt, J.1    Buttner, K.2    Scharf, C.3    Hecker, M.4
  • 3
    • 0022471589 scopus 로고
    • Gene encoding the sigma 37 species of RNA polymerase sigma factor from Bacillus subtilis
    • Binnie, C., M. Lampe, and R. Losick. 1986. Gene encoding the sigma 37 species of RNA polymerase sigma factor from Bacillus subtilis. Proc. Natl. Acad. Sci. USA 83:5943-5947.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 5943-5947
    • Binnie, C.1    Lampe, M.2    Losick, R.3
  • 5
    • 0036786262 scopus 로고    scopus 로고
    • A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis
    • Darmon, E., D. Noone, A. Masson, S. Bron, O. P. Kuipers, K. M. Devine, and J. M. van Dijl. 2002. A novel class of heat and secretion stress-responsive genes is controlled by the autoregulated CssRS two-component system of Bacillus subtilis. J. Bacteriol. 184:5661-5671.
    • (2002) J. Bacteriol. , vol.184 , pp. 5661-5671
    • Darmon, E.1    Noone, D.2    Masson, A.3    Bron, S.4    Kuipers, O.P.5    Devine, K.M.6    Van Dijl, J.M.7
  • 6
    • 0032921346 scopus 로고    scopus 로고
    • CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria
    • Derre, I., G. Rapoport, and T. Msadek. 1999. CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria. Mol. Microbiol. 31:117-131.
    • (1999) Mol. Microbiol. , vol.31 , pp. 117-131
    • Derre, I.1    Rapoport, G.2    Msadek, T.3
  • 7
    • 0037010120 scopus 로고    scopus 로고
    • AAA+ proteins and substrate recognition: It all depends on their partner in crime
    • Dougan, D. A., A. Mogk, K. Zeth, K. Turgay, and B. Bukau. 2002. AAA+ proteins and substrate recognition: it all depends on their partner in crime. FEBS Lett. 529:6-10.
    • (2002) FEBS Lett. , vol.529 , pp. 6-10
    • Dougan, D.A.1    Mogk, A.2    Zeth, K.3    Turgay, K.4    Bukau, B.5
  • 9
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman, S. 1996. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30:465-506.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 10
    • 0344824655 scopus 로고    scopus 로고
    • Proteolysis in bacterial regulatory circuits
    • Gottesman, S. 2003. Proteolysis in bacterial regulatory circuits. Annu. Rev. Cell Dev. Biol. 19:565-587.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 565-587
    • Gottesman, S.1
  • 11
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman, S., M. R. Maurizi, and S. Wickner. 1997. Regulatory subunits of energy-dependent proteases. Cell 91:435-438.
    • (1997) Cell , vol.91 , pp. 435-438
    • Gottesman, S.1    Maurizi, M.R.2    Wickner, S.3
  • 13
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud, R., M. Kessel, F. Beuron, A. C. Steven, and M. R. Maurizi. 1998. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273:12476-12481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 15
    • 0023752052 scopus 로고
    • The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component
    • Katayama, Y., S. Gottesman, J. Pumphrey, S. Rudikoff, W. P. Clark, and M. R. Maurizi. 1988. The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J. Biol. Chem. 263:15226-15236.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15226-15236
    • Katayama, Y.1    Gottesman, S.2    Pumphrey, J.3    Rudikoff, S.4    Clark, W.P.5    Maurizi, M.R.6
  • 16
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26S proteasome
    • Kessel, M., M. R. Maurizi, B. Kim, E. Kocsis, B. L. Trus, S. K. Singh, and A. C. Steven, 1995. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26S proteasome. J. Mol. Biol. 250:587-594.
    • (1995) J. Mol. Biol. , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Kocsis, E.4    Trus, B.L.5    Singh, S.K.6    Steven, A.C.7
  • 17
    • 1442349820 scopus 로고    scopus 로고
    • MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis
    • Kock, H., U. Gerth, and M. Hecker. 2004. MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis. Mol. Microbiol. 51:1087-1102.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1087-1102
    • Kock, H.1    Gerth, U.2    Hecker, M.3
  • 18
    • 0034072580 scopus 로고    scopus 로고
    • The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins
    • Kruger, E., E. Witt, S. Ohlmeier, R. Hanschke, and M. Hecker. 2000. The clp proteases of Bacillus subtilis are directly involved in degradation of misfolded proteins. J. Bacteriol. 182:3259-3265.
    • (2000) J. Bacteriol. , vol.182 , pp. 3259-3265
    • Kruger, E.1    Witt, E.2    Ohlmeier, S.3    Hanschke, R.4    Hecker, M.5
  • 19
    • 0035865140 scopus 로고    scopus 로고
    • Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor
    • Kruger, E., D. Zuhlke, E. Witt, H. Ludwig, and M. Hecker. 2001. Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor. EMBO J. 20:852-863.
    • (2001) EMBO J. , vol.20 , pp. 852-863
    • Kruger, E.1    Zuhlke, D.2    Witt, E.3    Ludwig, H.4    Hecker, M.5
  • 20
    • 0025323156 scopus 로고
    • ClpP represents a unique family of serine proteases
    • Maurizi, M. R., W. P. Clark, S. H. Kim, and S. Gottesman. 1990. ClpP represents a unique family of serine proteases. J. Biol. Chem. 265:12546-12552.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12546-12552
    • Maurizi, M.R.1    Clark, W.P.2    Kim, S.H.3    Gottesman, S.4
  • 21
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., T. Tomoyasu, P. Goloubinoff, S. Rudiger, D. Roder, H. Langen, and B. Bukau. 1999. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18:6934-6949.
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 22
    • 0031749920 scopus 로고    scopus 로고
    • ClpP of Bacillus subtilis is required for competence development, motility, degradative enzyme synthesis, growth at high temperature and sporulation
    • Msadek, T., V. Dartois, F. Kunst, M. L. Herbaud, F. Denizot, and G. Rapoport. 1998. ClpP of Bacillus subtilis is required for competence development, motility, degradative enzyme synthesis, growth at high temperature and sporulation. Mol. Microbiol. 27:899-914.
    • (1998) Mol. Microbiol. , vol.27 , pp. 899-914
    • Msadek, T.1    Dartois, V.2    Kunst, F.3    Herbaud, M.L.4    Denizot, F.5    Rapoport, G.6
  • 23
    • 0344392193 scopus 로고    scopus 로고
    • Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis
    • Nakano, S., E. Kuster-Schock, A. D. Grossman, and P. Zuber. 2003. Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis. Proc. Natl. Acad. Sci. USA 100:13603-13608.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13603-13608
    • Nakano, S.1    Kuster-Schock, E.2    Grossman, A.D.3    Zuber, P.4
  • 24
    • 0037386620 scopus 로고    scopus 로고
    • A regulatory protein that interferes with activator-stimulated transcription in bacteria
    • Nakano, S., M. M. Nakano, Y. Zhang, M. Leelakriangsak, and P. Zuber. 2003. A regulatory protein that interferes with activator-stimulated transcription in bacteria. Proc. Natl. Acad. Sci. USA 100:4233-4238.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4233-4238
    • Nakano, S.1    Nakano, M.M.2    Zhang, Y.3    Leelakriangsak, M.4    Zuber, P.5
  • 25
    • 0036283489 scopus 로고    scopus 로고
    • Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis
    • Nakano, S., G. Zheng, M. M. Nakano, and P. Zuber. 2002. Multiple pathways of Spx (YjbD) proteolysis in Bacillus subtilis. J. Bacteriol. 184:3664-3670.
    • (2002) J. Bacteriol. , vol.184 , pp. 3664-3670
    • Nakano, S.1    Zheng, G.2    Nakano, M.M.3    Zuber, P.4
  • 26
    • 0034764908 scopus 로고    scopus 로고
    • Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilis
    • Pan, Q., D. A. Garsin, and R. Losick. 2001. Self-reinforcing activation of a cell-specific transcription factor by proteolysis of an anti-sigma factor in B. subtilis. Mol. Cell 8:873-883.
    • (2001) Mol. Cell , vol.8 , pp. 873-883
    • Pan, Q.1    Garsin, D.A.2    Losick, R.3
  • 27
    • 0041888264 scopus 로고    scopus 로고
    • Unique degradation signal for ClpCP in Bacillus subtilis
    • Pan, Q., and R. Losick. 2003. Unique degradation signal for ClpCP in Bacillus subtilis. J. Bacteriol. 185:5275-5278.
    • (2003) J. Bacteriol. , vol.185 , pp. 5275-5278
    • Pan, Q.1    Losick, R.2
  • 30
    • 0030028240 scopus 로고    scopus 로고
    • hrcA, the first gene of the Bacillus subtilis dnaK operon, encodes a negative regulator of class I heat shock genes
    • Schulz, A., and W. Schumann. 1996. hrcA, the first gene of the Bacillus subtilis dnaK operon, encodes a negative regulator of class I heat shock genes. J. Bacteriol. 178:1088-1093.
    • (1996) J. Bacteriol. , vol.178 , pp. 1088-1093
    • Schulz, A.1    Schumann, W.2
  • 31
    • 0002547666 scopus 로고    scopus 로고
    • Regulation and function of heat-inducible genes in Bacillus subtilis
    • A. Sonenshein (ed.). ASM Press, Washington, D.C.
    • Schumann, W., M. Hecker, and T. Msadek. 2002. Regulation and function of heat-inducible genes in Bacillus subtilis, p. 359-368. In A. Sonenshein (ed.), Bacillus subtilis and its closest relatives: from genes to cells. ASM Press, Washington, D.C.
    • (2002) Bacillus Subtilis and Its Closest Relatives: From Genes to Cells , pp. 359-368
    • Schumann, W.1    Hecker, M.2    Msadek, T.3
  • 32
    • 0032538886 scopus 로고    scopus 로고
    • Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
    • Turgay, K., J. Hahn, J. Burghoorn, and D. Dubnau. 1998. Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor. EMBO J. 17:6730-6738.
    • (1998) EMBO J. , vol.17 , pp. 6730-6738
    • Turgay, K.1    Hahn, J.2    Burghoorn, J.3    Dubnau, D.4
  • 33
    • 0029658301 scopus 로고    scopus 로고
    • The Clp ATPases define a novel class of molecular chaperones
    • Wawrzynow, A., B. Banecki, and M. Zylicz. 1996. The Clp ATPases define a novel class of molecular chaperones. Mol. Microbiol. 21:895-899.
    • (1996) Mol. Microbiol. , vol.21 , pp. 895-899
    • Wawrzynow, A.1    Banecki, B.2    Zylicz, M.3
  • 34
    • 0033587680 scopus 로고    scopus 로고
    • Here's the hook: Similar substrate binding sites in the chaperone domains of Clp and Lon
    • Wickner, S., and M. R. Maurizi. 1999. Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon. Proc. Natl. Acad. Sci. USA 96:8318-8320.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8318-8320
    • Wickner, S.1    Maurizi, M.R.2
  • 35
    • 0028804756 scopus 로고
    • Isolation and characterization of Bacillus subtilis groE regulatory mutants: Evidence for orf39 in the dnaK operon as a repressor gene in regulating the expression of both groE and dnaK
    • Yuan, G., and S. L. Wong. 1995. Isolation and characterization of Bacillus subtilis groE regulatory mutants: evidence for orf39 in the dnaK operon as a repressor gene in regulating the expression of both groE and dnaK. J. Bacteriol. 177:6462-6468.
    • (1995) J. Bacteriol. , vol.177 , pp. 6462-6468
    • Yuan, G.1    Wong, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.