메뉴 건너뛰기




Volumn 25, Issue 1, 2007, Pages 161-166

Altered Specificity of a AAA+ Protease

Author keywords

PROTEINS

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ENDOPEPTIDASE CLPX;

EID: 33845981507     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.11.018     Document Type: Article
Times cited : (35)

References (26)
  • 1
    • 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. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J. 20 (2001) 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
  • 2
    • 17844377879 scopus 로고    scopus 로고
    • Nucleotide-dependent substrate recognition by the AAA+ HslUV protease
    • Burton R.E., Baker T.A., and Sauer R.T. Nucleotide-dependent substrate recognition by the AAA+ HslUV protease. Nat. Struct. Mol. Biol. 12 (2005) 245-251
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 245-251
    • Burton, R.E.1    Baker, T.A.2    Sauer, R.T.3
  • 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. Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis. Proc. Natl. Acad. Sci. USA 11 (2001) 10584-10589
    • (2001) Proc. Natl. Acad. Sci. USA , vol.11 , 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. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell 11 (2003) 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
  • 6
    • 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. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12 (1998) 1338-1347
    • (1998) Genes Dev. , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 7
    • 2642666491 scopus 로고    scopus 로고
    • Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)
    • Herman C., Thevenet D., Bouloc P., Walker G.C., and D'Ari R. Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH). Genes Dev. 12 (1998) 1348-1355
    • (1998) Genes Dev. , vol.12 , pp. 1348-1355
    • Herman, C.1    Thevenet, D.2    Bouloc, P.3    Walker, G.C.4    D'Ari, R.5
  • 8
    • 0037036431 scopus 로고    scopus 로고
    • Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP
    • Kang S.G., Ortega J., Singh S.K., Wang N., Huang N.N., Steven A.C., and Maurizi M.R. Functional proteolytic complexes of the human mitochondrial ATP-dependent protease, hClpXP. J. Biol. Chem. 277 (2002) 21095-21102
    • (2002) J. Biol. Chem. , vol.277 , pp. 21095-21102
    • Kang, S.G.1    Ortega, J.2    Singh, S.K.3    Wang, N.4    Huang, N.N.5    Steven, A.C.6    Maurizi, M.R.7
  • 9
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide-tagging system in degradation of proteins translated from damaged mRNA
    • Keiler K.C., Waller P.R.H., and Sauer R.T. Role of a peptide-tagging system in degradation of proteins translated from damaged mRNA. Science 271 (1996) 990-993
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 10
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of a AAA+ degradation machine
    • Kenniston J.A., Baker T.A., Fernandez J.M., and Sauer R.T. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of a AAA+ degradation machine. Cell 114 (2003) 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
  • 11
    • 1642308732 scopus 로고    scopus 로고
    • Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation
    • Kenniston J.A., Burton R.E., Siddiqui S.M., Baker T.A., and Sauer R.T. Effects of local protein stability and the geometric position of the substrate degradation tag on the efficiency of ClpXP denaturation and degradation. J. Struct. Biol. 146 (2004) 130-140
    • (2004) J. Struct. Biol. , vol.146 , pp. 130-140
    • Kenniston, J.A.1    Burton, R.E.2    Siddiqui, S.M.3    Baker, T.A.4    Sauer, R.T.5
  • 12
    • 13444306170 scopus 로고    scopus 로고
    • Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing
    • Kenniston J.A., Baker T.A., and Sauer R.T. Partitioning between unfolding and release of native domains during ClpXP degradation determines substrate selectivity and partial processing. Proc. Natl. Acad. Sci. USA 102 (2005) 1390-1395
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1390-1395
    • Kenniston, J.A.1    Baker, T.A.2    Sauer, R.T.3
  • 14
    • 0348010311 scopus 로고    scopus 로고
    • Crystal structure of ClpX molecular chaperone from Helicobacter pylori
    • Kim D.Y., and Kim K.K. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J. Biol. Chem. 278 (2003) 50664-50670
    • (2003) J. Biol. Chem. , vol.278 , pp. 50664-50670
    • Kim, D.Y.1    Kim, K.K.2
  • 15
    • 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. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5 (2000) 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
  • 16
    • 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. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7 (2001) 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
  • 17
    • 0030908043 scopus 로고    scopus 로고
    • ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway
    • Levchenko I., Yamauchi M., and Baker T.A. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11 (1997) 1561-1572
    • (1997) Genes Dev. , vol.11 , pp. 1561-1572
    • Levchenko, I.1    Yamauchi, M.2    Baker, T.A.3
  • 18
    • 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. A specificity-enhancing factor for the ClpXP degradation machine. Science 289 (2000) 2354-2356
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 19
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATP-fueled machines
    • Martin A., Baker T.A., and Sauer R.T. Rebuilt AAA+ motors reveal operating principles for ATP-fueled machines. Nature 437 (2005) 1115-1120
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 20
    • 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. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6 (2000) 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
  • 21
    • 16844376945 scopus 로고    scopus 로고
    • The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer
    • Piszczek G., Rozycki J., Singh S.K., Ginsburg A., and Maurizi M.R. The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer. J. Biol. Chem. 280 (2005) 12221-12230
    • (2005) J. Biol. Chem. , vol.280 , pp. 12221-12230
    • Piszczek, G.1    Rozycki, J.2    Singh, S.K.3    Ginsburg, A.4    Maurizi, M.R.5
  • 24
    • 1542283751 scopus 로고    scopus 로고
    • Role of the protein-processing pore of ClpX, a AAA+ ATPase, in recognition and engagement of specific protein substrates
    • Siddiqui S.M., Sauer R.T., and Baker T.A. Role of the protein-processing pore of ClpX, a AAA+ ATPase, in recognition and engagement of specific protein substrates. Genes Dev. 18 (2004) 369-374
    • (2004) Genes Dev. , vol.18 , pp. 369-374
    • Siddiqui, S.M.1    Sauer, R.T.2    Baker, T.A.3
  • 25
  • 26
    • 0037184939 scopus 로고    scopus 로고
    • Directed evolution of substrate-optimized GroEL/S chaperonins
    • Wang J.D., Herman C., Tipton K.A., Gross C.A., and Weissman J.S. Directed evolution of substrate-optimized GroEL/S chaperonins. Cell 111 (2002) 1027-1039
    • (2002) Cell , vol.111 , pp. 1027-1039
    • Wang, J.D.1    Herman, C.2    Tipton, K.A.3    Gross, C.A.4    Weissman, J.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.