메뉴 건너뛰기




Volumn 193, Issue 19, 2011, Pages 5465-5476

Stepwise Activity of ClpY (HslU) mutants in the processive degradation of Escherichia coli ClpYQ (HslUV) protease substrates

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; MUTANT PROTEIN; PEPTIDASE; POLYPEPTIDE; PROTEIN CLPQ; PROTEIN CLPY; PROTEINASE; TYROSINE; UNCLASSIFIED DRUG;

EID: 80053577853     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05128-11     Document Type: Article
Times cited : (10)

References (50)
  • 1
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman, M., et al. 2006. Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16:686-691.
    • (2006) Genome Res , vol.16 , pp. 686-691
    • Arifuzzaman, M.1
  • 2
    • 17744364699 scopus 로고    scopus 로고
    • Characterization of the HslU chaperone affinity for HslV protease
    • Azim, M. K., et al. 2005. Characterization of the HslU chaperone affinity for HslV protease. Protein Sci. 14:1357-1362.
    • (2005) Protein Sci , vol.14 , pp. 1357-1362
    • Azim, M.K.1
  • 3
    • 0034677361 scopus 로고    scopus 로고
    • The structures of HsIU and the ATP-dependent protease HsIU-HsIV
    • Bochtler, M., et al. 2000. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature 403:800-805.
    • (2000) Nature , vol.403 , pp. 800-805
    • Bochtler, M.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0027445907 scopus 로고
    • Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli
    • Chuang, S. E., V. Burland, G. Plunkett III, D. L. Daniels, and F. R. Blattner. 1993. Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. Gene 134:1-6.
    • (1993) Gene , vol.134 , pp. 1-6
    • Chuang, S.E.1    Burland, V.2    Plunkett III, G.3    Daniels, D.L.4    Blattner, F.R.5
  • 9
    • 0033992441 scopus 로고    scopus 로고
    • A set of temperature sensitive-replication/-segregation and temperature resistant plasmid vectors with different copy numbers and in an isogenic background (chloramphenicol, kanamycin, lacZ, repA, par, polA)
    • Hashimoto-Gotoh, T., et al. 2000. A set of temperature sensitive-replication/-segregation and temperature resistant plasmid vectors with different copy numbers and in an isogenic background (chloramphenicol, kanamycin, lacZ, repA, par, polA). Gene 241:185-191.
    • (2000) Gene , vol.241 , pp. 185-191
    • Hashimoto-Gotoh, T.1
  • 10
    • 0030943075 scopus 로고    scopus 로고
    • Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon
    • Higashitani, A., Y. Ishii, Y. Kato, and K. Horiuchi. 1997. Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon. Mol. Gen. Genet. 254:351-357.
    • (1997) Mol. Gen. Genet. , vol.254 , pp. 351-357
    • Higashitani, A.1    Ishii, Y.2    Kato, Y.3    Horiuchi, K.4
  • 11
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch, J., W. A. Fenton, K. J. Furtak, G. W. Farr, and A. L. Horwich. 2005. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121:1029-1041.
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 12
    • 34250166903 scopus 로고    scopus 로고
    • Support for a potential role of E. coli oligopeptidase A in protein degradation
    • Jain, R., and M. K. Chan. 2007. Support for a potential role of E. coli oligopeptidase A in protein degradation. Biochem. Biophys. Res. Commun. 359:486-490.
    • (2007) Biochem. Biophys. Res. Commun. , vol.359 , pp. 486-490
    • Jain, R.1    Chan, M.K.2
  • 13
    • 0345269855 scopus 로고    scopus 로고
    • C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding
    • Joshi, S. A., T. A. Baker, and R. T. Sauer. 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
  • 14
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of σ32 and abnormal proteins in Escherichia coli
    • Kanemori, M., K. Nishihara, H. Yanagi, and T. Yura. 1997. Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of σ32 and abnormal proteins in Escherichia coli. J. Bacteriol. 179:7219-7225.
    • (1997) J. Bacteriol. , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 15
    • 0033023919 scopus 로고    scopus 로고
    • The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli
    • Kanemori, M., H. Yanagi, and T. Yura. 1999. The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli. J. Bacteriol. 181:3674-3680.
    • (1999) J. Bacteriol. , vol.181 , pp. 3674-3680
    • Kanemori, M.1    Yanagi, H.2    Yura, T.3
  • 16
    • 0033618309 scopus 로고    scopus 로고
    • Marked instability of the σ32 heat shock transcription factor at high temperature. Implications for heat shock regulation
    • Kanemori, M., H. Yanagi, and T. Yura. 1999. Marked instability of the σ32 heat shock transcription factor at high temperature. Implications for heat shock regulation. J. Biol. Chem. 274:22002-22007.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22002-22007
    • Kanemori, M.1    Yanagi, H.2    Yura, T.3
  • 17
    • 0030566824 scopus 로고    scopus 로고
    • Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY
    • Kessel, M., et al. 1996. Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. FEBS Lett. 398:274-278.
    • (1996) FEBS Lett , vol.398 , pp. 274-278
    • Kessel, M.1
  • 18
    • 0031559883 scopus 로고    scopus 로고
    • Overexpression of the hslVU operon suppresses SOSmediated inhibition of cell division in Escherichia coli
    • Khattar, M. M. 1997. Overexpression of the hslVU operon suppresses SOSmediated inhibition of cell division in Escherichia coli. FEBS Lett. 414:402-404.
    • (1997) FEBS Lett , vol.414 , pp. 402-404
    • Khattar, M.M.1
  • 20
    • 79952293131 scopus 로고    scopus 로고
    • Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase
    • Kravats, A., M. Jayasinghe, and G. Stan. 2011. Unfolding and translocation pathway of substrate protein controlled by structure in repetitive allosteric cycles of the ClpY ATPase. Proc. Natl. Acad. Sci. U. S. A. 108:2234-2239.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2234-2239
    • Kravats, A.1    Jayasinghe, M.2    Stan, G.3
  • 21
    • 71749085013 scopus 로고    scopus 로고
    • Clp chaperone-proteases: structure and function
    • Kress, W., Z. Maglica, and E. Weber-Ban. 2009. Clp chaperone-proteases: structure and function. Res. Microbiol. 160:618-628.
    • (2009) Res. Microbiol. , vol.160 , pp. 618-628
    • Kress, W.1    Maglica, Z.2    Weber-Ban, E.3
  • 22
    • 1242273739 scopus 로고    scopus 로고
    • Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli
    • Kuo, M. S., K. P. Chen, and W. F. Wu. 2004. Regulation of RcsA by the ClpYQ (HslUV) protease in Escherichia coli. Microbiology 150:437-446.
    • (2004) Microbiology , vol.150 , pp. 437-446
    • Kuo, M.S.1    Chen, K.P.2    Wu, W.F.3
  • 23
    • 0038122858 scopus 로고    scopus 로고
    • Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome
    • Kwon, A. R., B. M. Kessler, H. S. Overkleeft, and D. B. McKay. 2003. Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome. J. Mol. Biol. 330:185-195.
    • (2003) J. Mol. Biol. , vol.330 , pp. 185-195
    • Kwon, A.R.1    Kessler, B.M.2    Overkleeft, H.S.3    McKay, D.B.4
  • 24
    • 37749018166 scopus 로고    scopus 로고
    • Activation of the Cpx regulon destabilizes the F plasmid transfer activator, TraJ, via the HslVU protease in Escherichia coli
    • Lau-Wong, I. C., T. Locke, M. J. Ellison, T. L. Raivio, and L. S. Frost. 2008. Activation of the Cpx regulon destabilizes the F plasmid transfer activator, TraJ, via the HslVU protease in Escherichia coli. Mol. Microbiol. 67:516-527.
    • (2008) Mol. Microbiol. , vol.67 , pp. 516-527
    • Lau-Wong, I.C.1    Locke, T.2    Ellison, M.J.3    Raivio, T.L.4    Frost, L.S.5
  • 25
    • 70450235042 scopus 로고    scopus 로고
    • HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis
    • Lee, J. W., et al. 2009. HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis. J. Biol. Chem. 284: 33475-33484.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33475-33484
    • Lee, J.W.1
  • 26
    • 0037384151 scopus 로고    scopus 로고
    • Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo proteinprotein interactions in the yeast two-hybrid system
    • Lee, Y. Y., et al. 2003. Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo proteinprotein interactions in the yeast two-hybrid system. J. Bacteriol. 185:2393-2401.
    • (2003) J. Bacteriol. , vol.185 , pp. 2393-2401
    • Lee, Y.Y.1
  • 27
    • 67649414445 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system
    • Lien, H. Y., et al. 2009. Characterization of the Escherichia coli ClpY (HslU) substrate recognition site in the ClpYQ (HslUV) protease using the yeast two-hybrid system. J. Bacteriol. 191:4218-4231.
    • (2009) J. Bacteriol. , vol.191 , pp. 4218-4231
    • Lien, H.Y.1
  • 29
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi, M. R. 1992. Proteases and protein degradation in Escherichia coli. Experientia 48:178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 30
    • 80053615004 scopus 로고    scopus 로고
    • Structure and function of ATP-dependent Clp protease
    • E. Kutejova (ed.), Research Signpost, Kerala, India
    • Maurizi, M. R. 2008. Structure and function of ATP-dependent Clp protease, p. 41-86. In E. Kutejova (ed.), ATP-dependent proteases. Research Signpost, Kerala, India.
    • (2008) ATP-dependent proteases , pp. 41-86
    • Maurizi, M.R.1
  • 32
    • 0030462757 scopus 로고    scopus 로고
    • Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli
    • Missiakas, D., F. Schwager, J. M. Betton, C. Georgopoulos, and S. Raina. 1996. Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15:6899-6909.
    • (1996) EMBO J , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.M.3    Georgopoulos, C.4    Raina, S.5
  • 33
    • 0023809599 scopus 로고
    • Coupled assay of Na, K-ATPase activity
    • Nørby, J. G. 1988. Coupled assay of Na, K-ATPase activity. Methods Enzymol. 156:116-119.
    • (1988) Methods Enzymol , vol.156 , pp. 116-119
    • Nørby, J.G.1
  • 34
    • 57749083505 scopus 로고    scopus 로고
    • Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent
    • Park, E., J. W. Lee, S. H. Eom, J. H. Seol, and C. H. Chung. 2008. Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent. J. Biol. Chem. 283:33258-33266.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33258-33266
    • Park, E.1    Lee, J.W.2    Eom, S.H.3    Seol, J.H.4    Chung, C.H.5
  • 35
    • 20744457369 scopus 로고    scopus 로고
    • Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase
    • Park, E., et al. 2005. Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase. J. Biol. Chem. 280:22892-22898.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22892-22898
    • Park, E.1
  • 37
    • 84855271946 scopus 로고    scopus 로고
    • U.S. National Institutes of Health, Bethesda, MD
    • Rasband, W. S. 2011. ImageJ. U.S. National Institutes of Health, Bethesda, MD. http://imagej.nih.gov/ij/.
    • (2011) ImageJ
    • Rasband, W.S.1
  • 38
    • 0030614496 scopus 로고    scopus 로고
    • The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome
    • Rohrwild, M., et al. 1997. The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome. Nat. Struct. Biol. 4:133-139.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 133-139
    • Rohrwild, M.1
  • 39
    • 0037135539 scopus 로고    scopus 로고
    • The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase
    • Seong, I. S., et al. 2002. The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase. J. Biol. Chem. 277:25976-25982.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25976-25982
    • Seong, I.S.1
  • 40
    • 0030566835 scopus 로고    scopus 로고
    • Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli
    • Shin, D. H., et al. 1996. Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli. FEBS Lett. 398:151-154.
    • (1996) FEBS Lett , vol.398 , pp. 151-154
    • Shin, D.H.1
  • 41
    • 0001507666 scopus 로고    scopus 로고
    • Mutational studies on HslU and its docking mode with HslV
    • Song, H. K., et al. 2000. Mutational studies on HslU and its docking mode with HslV. Proc. Natl. Acad. Sci. U. S. A. 97:14103-14108.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14103-14108
    • Song, H.K.1
  • 42
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HslUV protease-chaperone complex
    • Sousa, M. C., et al. 2000. Crystal and solution structures of an HslUV protease-chaperone complex. Cell 103:633-643.
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1
  • 44
    • 0035096082 scopus 로고    scopus 로고
    • Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
    • Wang, J., et al. 2001. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure 9:177-184.
    • (2001) Structure , vol.9 , pp. 177-184
    • Wang, J.1
  • 45
    • 0035184442 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU
    • Wang, J., et al. 2001. Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU. Structure 9:1107-1116.
    • (2001) Structure , vol.9 , pp. 1107-1116
    • Wang, J.1
  • 46
    • 67650075092 scopus 로고    scopus 로고
    • HslUV (ClpYQ), an ATP-dependent protease with unique characteristics
    • E. Kutejova (ed.), Research Signpost, Kerala, India
    • Wu, W.-F., C.-S. Yang, H.-Y. Lien, F.-C. Hsieh, and C.-Y. Chang. 2008. HslUV (ClpYQ), an ATP-dependent protease with unique characteristics, p. 115-143. In E. Kutejova (ed.), ATP-dependent proteases. Research Signpost, Kerala, India.
    • (2008) ATP-dependent proteases , pp. 115-143
    • Wu, W.-F.1    Yang, C.-S.2    Lien, H.-Y.3    Hsieh, F.-C.4    Chang, C.-Y.5
  • 47
    • 0033016759 scopus 로고    scopus 로고
    • Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) Protease
    • Wu, W.-F., Y. N. Zhou, and S. Gottesman. 1999. Redundant in vivo proteolytic activities of Escherichia coli Lon and the ClpYQ (HslUV) Protease. J. Bacteriol. 181:3681-3687.
    • (1999) J. Bacteriol. , vol.181 , pp. 3681-3687
    • Wu, W.-F.1    Zhou, Y.N.2    Gottesman, S.3
  • 48
    • 45849107940 scopus 로고    scopus 로고
    • Asymmetric nucleotide transactions of the HslUV protease
    • Yakamavich, J. A., T. A. Baker, and R. T. Sauer. 2008. Asymmetric nucleotide transactions of the HslUV protease. J. Mol. Biol. 380:946-957.
    • (2008) J. Mol. Biol. , vol.380 , pp. 946-957
    • Yakamavich, J.A.1    Baker, T.A.2    Sauer, R.T.3
  • 49
    • 0001588962 scopus 로고    scopus 로고
    • Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
    • Yoo, S. J., et al. 1996. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J. Biol. Chem. 271:14035-14040.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14035-14040
    • Yoo, S.J.1
  • 50
    • 33747058216 scopus 로고    scopus 로고
    • A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
    • Zolkiewski, M. 2006. A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases. Mol. Microbiol. 61:1094-1100.
    • (2006) Mol. Microbiol. , vol.61 , pp. 1094-1100
    • Zolkiewski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.