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Volumn 18, Issue 4, 2004, Pages 369-374

Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates

Author keywords

AAA ATPase; Peptide binding; Protein translocation; Protein unfolding

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ENDOPEPTIDASE CLP; ENDOPEPTIDASE CLPX; PROTEIN; PROTEIN CLPX AAA; UNCLASSIFIED DRUG;

EID: 1542283751     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1170304     Document Type: Article
Times cited : (141)

References (27)
  • 1
    • 0037688128 scopus 로고    scopus 로고
    • Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex
    • Burton, B.M. and Baker, T.A. 2003. Mu transpososome architecture ensures that unfolding by ClpX or proteolysis by ClpXP remodels but does not destroy the complex. Chem. Biol. 10: 463-472.
    • (2003) Chem. Biol. , vol.10 , pp. 463-472
    • Burton, B.M.1    Baker, T.A.2
  • 2
    • 0035875890 scopus 로고    scopus 로고
    • Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
    • Burton, R.E., Siddiqui, S.M., Kim, Y.I., Baker, T.A., and Sauer, R.T. 2001. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J. 20: 3092-3100.
    • (2001) EMBO J. , vol.20 , pp. 3092-3100
    • Burton, R.E.1    Siddiqui, S.M.2    Kim, Y.I.3    Baker, T.A.4    Sauer, R.T.5
  • 3
    • 0035845498 scopus 로고    scopus 로고
    • Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
    • Flynn, J.M., Levchenko, I., Seidel, M., Wickner, S.H., Sauer, R.T., and Baker, T.A. 2001. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc. Natl. Acad. Sci. 98: 10584-10589.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 10584-10589
    • Flynn, J.M.1    Levchenko, I.2    Seidel, M.3    Wickner, S.H.4    Sauer, R.T.5    Baker, T.A.6
  • 4
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn, J.M., Neher, S.B., Kim, Y.I., Sauer, R.T., and Baker, T.A. 2003. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11: 671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 5
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., Roche, E., Zhou, Y., and Sauer, R.T. 1998. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes & Dev. 12: 1338-1347.
    • (1998) Genes & Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 6
    • 0141789762 scopus 로고    scopus 로고
    • Proteolysis in prokaryotes: Protein quality control and regulatory principles
    • Hengge, R. and Bukau, B. 2003. Proteolysis in prokaryotes: Protein quality control and regulatory principles. Mol. Microbiol. 49: 1451-1462.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1451-1462
    • Hengge, R.1    Bukau, B.2
  • 7
    • 0345269855 scopus 로고    scopus 로고
    • C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding
    • Joshi, S.A., Baker, T.A., and Sauer, R.T. 2003. C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding. Mol. Microbiol. 48: 67-76.
    • (2003) Mol. Microbiol. , vol.48 , pp. 67-76
    • Joshi, S.A.1    Baker, T.A.2    Sauer, R.T.3
  • 8
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K.C., Waller, P.R., and Sauer, R.T. 1996. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 9
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston, J.A., Baker, T.A., Fernandez, J.M., and Sauer, R.T. 2003. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114: 511-520.
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 10
    • 0348010311 scopus 로고    scopus 로고
    • Crystal structure of ClpX molecular chaperone from Helicobacter pylori
    • Kim, D.Y. and Kim, K.K. 2003. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J. Biol. Chem. 278: 50664-50670.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50664-50670
    • Kim, D.Y.1    Kim, K.K.2
  • 11
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim, Y.I., Burton, R.E., Burton, B.M., Sauer, R.T., and Baker, T.A. 2000. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5: 639-648.
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 13
    • 0030020897 scopus 로고    scopus 로고
    • ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis
    • Kruklitis, R., Welty, D.J., and Nakai, H. 1996. ClpX protein of Escherichia coli activates bacteriophage Mu transposase in the strand transfer complex for initiation of Mu DNA synthesis. EMBO J. 15: 935-944.
    • (1996) EMBO J. , vol.15 , pp. 935-944
    • Kruklitis, R.1    Welty, D.J.2    Nakai, H.3
  • 14
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M., and Matouschek, A. 2001. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7: 627-637.
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 15
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko, I., Luo, L., and Baker, T.A. 1995. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes & Dev. 9: 2399-2408.
    • (1995) Genes & Dev. , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 16
    • 0031457264 scopus 로고    scopus 로고
    • PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
    • Levchenko, I., Smith, C.K., Walsh, N.P., Sauer, R.T., and Baker, T.A. 1997. PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91: 939-947.
    • (1997) Cell , vol.91 , pp. 939-947
    • Levchenko, I.1    Smith, C.K.2    Walsh, N.P.3    Sauer, R.T.4    Baker, T.A.5
  • 17
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko, I., Seidel, M., Sauer, R.T., and Baker, T.A. 2000. A specificity-enhancing factor for the ClpXP degradation machine. Science 289: 2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 18
    • 0033578322 scopus 로고    scopus 로고
    • Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes
    • Makovets, S., Doronina, V.A., and Murray, N.E. 1999. Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes. Proc. Natl. Acad. Sci. 96: 9757-9762.
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 9757-9762
    • Makovets, S.1    Doronina, V.A.2    Murray, N.E.3
  • 19
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega, J., Singh, S.K., Ishikawa, T., Maurizi, M.R., and Steven, A.C. 2000. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6: 1515-1521.
    • (2000) Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 20
    • 0034254908 scopus 로고    scopus 로고
    • Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP
    • Singh, S.K., Grimaud, R., Hoskins, J.R., Wickner, S., and Maurizi, M.R. 2000. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc. Natl. Acad. Sci. 97: 8898-8903.
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8898-8903
    • Singh, S.K.1    Grimaud, R.2    Hoskins, J.R.3    Wickner, S.4    Maurizi, M.R.5
  • 22
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah, D.A., Levchenko, I., Baker, T.A., and Sauer, R.T. 2002. Characterization of a specificity factor for an AAA+ ATPase: Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 9: 1237-1245.
    • (2002) Chem. Biol. , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 23
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang, J., Hartling, J.A., and Flanagan, J.M. 1997. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91: 447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 25
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C., and Zylicz, M. 1995. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J. 14: 1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 26
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban, E.U., Reid, B.G., Miranker, A.D., and Horwich, A.L. 1999. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401: 90-93.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 27
    • 0348010363 scopus 로고    scopus 로고
    • Conserved pore residues in the AAA protease, FtsH, are important for proteolysis and its coupling to ATP hydrolysis
    • Yamada-Inagawa, T., Okuno, T., Karata, K., Yamanaka, K., and Ogura, T. 2003. Conserved pore residues in the AAA protease, FtsH, are important for proteolysis and its coupling to ATP hydrolysis. J. Biol. Chem. 278: 50182-50187.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50182-50187
    • Yamada-Inagawa, T.1    Okuno, T.2    Karata, K.3    Yamanaka, K.4    Ogura, T.5


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