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Volumn 584, Issue 5, 2010, Pages 951-953

ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle

Author keywords

ADP; ATP; Coupled enzyme assay; GroEL; GroES; Nucleotide cycle

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE 7; ADENOSINE TRIPHOSPHATE; CHAPERONIN; LACTATE DEHYDROGENASE; PROTEIN GROEL; PROTEIN GROES; PYRUVATE KINASE; UNCLASSIFIED DRUG;

EID: 76749127971     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.01.021     Document Type: Article
Times cited : (4)

References (20)
  • 1
  • 2
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings
    • Rye H.S., Roseman A.M., Furtak K., Fenton W.A., Saibil H.R., and Horwich A.L. GroEL-GroES cycling: ATP and non-native polypeptide direct alternation of folding-active rings. Cell 97 (1999) 325-338
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Furtak, K.3    Fenton, W.A.4    Saibil, H.R.5    Horwich, A.L.6
  • 3
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity in the oligomeric chaperonin GroEL
    • Yifrach O., and Horovitz A. Nested cooperativity in the ATPase activity in the oligomeric chaperonin GroEL. Biochemistry 34 (1995) 9716-9723
    • (1995) Biochemistry , vol.34 , pp. 9716-9723
    • Yifrach, O.1    Horovitz, A.2
  • 5
    • 73949133922 scopus 로고    scopus 로고
    • GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state
    • Tyagi N., Fenton W.A., and Horwich A.L. GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state. Proc. Natl. Acad. Sci. USA 106 (2009) 20264-20269
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20264-20269
    • Tyagi, N.1    Fenton, W.A.2    Horwich, A.L.3
  • 6
    • 1942469376 scopus 로고    scopus 로고
    • Stopped-flow fluorescent analysis of the conformational changes in the GroEL apical domain
    • Taniguchi M., Yoshimi T., Hongo K., Mizobata T., and Kawata Y. Stopped-flow fluorescent analysis of the conformational changes in the GroEL apical domain. J. Biol. Chem. 279 (2004) 16368-16376
    • (2004) J. Biol. Chem. , vol.279 , pp. 16368-16376
    • Taniguchi, M.1    Yoshimi, T.2    Hongo, K.3    Mizobata, T.4    Kawata, Y.5
  • 7
    • 33746357595 scopus 로고    scopus 로고
    • Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE
    • Cliff M.J., Limpkin C., Cameron A., Burston S.G., and Clarke A.R. Elucidation of steps in the capture of a protein substrate for efficient encapsulation by GroE. J. Biol. Chem. 281 (2006) 21266-21275
    • (2006) J. Biol. Chem. , vol.281 , pp. 21266-21275
    • Cliff, M.J.1    Limpkin, C.2    Cameron, A.3    Burston, S.G.4    Clarke, A.R.5
  • 8
    • 70350020881 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
    • Horwich A.L., and Fenton W.A. Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Quart. Rev. Biophys. 42 (2009) 83-116
    • (2009) Quart. Rev. Biophys. , vol.42 , pp. 83-116
    • Horwich, A.L.1    Fenton, W.A.2
  • 9
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A.M., Chen S., White H., Braig K., and Saibil H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87 (1996) 241-251
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 10
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated folding reaction
    • Weissman J.S., Rye H.S., Fenton W.A., Beechem J.M., and Horwich A.L. Characterization of the active intermediate of a GroEL-GroES-mediated folding reaction. Cell 84 (1996) 481-490
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 14
    • 56249135270 scopus 로고    scopus 로고
    • Chaperonin chamber accelerates protein folding through passive action of preventing aggregation
    • Apetri A.C., and Horwich A.L. Chaperonin chamber accelerates protein folding through passive action of preventing aggregation. Proc. Natl. Acad. Sci. USA 105 (2008) 17351-17355
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17351-17355
    • Apetri, A.C.1    Horwich, A.L.2
  • 15
    • 0031557387 scopus 로고    scopus 로고
    • Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction
    • Ranson N.A., Burston S.G., and Clarke A.R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266 (1997) 656-664
    • (1997) J. Mol. Biol. , vol.266 , pp. 656-664
    • Ranson, N.A.1    Burston, S.G.2    Clarke, A.R.3
  • 16
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding
    • Jackson G.S., Staniforth R.A., Halsall D.J., Atkinson T., Holbrook J.J., Clarke A.R., and Burston S.G. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry 32 (1993) 2554-2563
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burston, S.G.7
  • 17
    • 57649114084 scopus 로고    scopus 로고
    • Triggering protein folding within the GroEL-GroES complex
    • Madan D., Lin Z., and Rye H.S. Triggering protein folding within the GroEL-GroES complex. J. Biol. Chem. 283 (2008) 32003-32013
    • (2008) J. Biol. Chem. , vol.283 , pp. 32003-32013
    • Madan, D.1    Lin, Z.2    Rye, H.S.3
  • 18
    • 0032562652 scopus 로고    scopus 로고
    • Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings
    • Kad N.M., Ranson N.A., Cliff M.J., and Clarke A.R. Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings. J. Mol. Biol. 278 (1999) 267-278
    • (1999) J. Mol. Biol. , vol.278 , pp. 267-278
    • Kad, N.M.1    Ranson, N.A.2    Cliff, M.J.3    Clarke, A.R.4
  • 19
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston S.G., Ranson N.A., and Clarke A.R. The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249 (1995) 138-152
    • (1995) J. Mol. Biol. , vol.249 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 20
    • 77957001185 scopus 로고
    • Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods
    • Williamson J.R., and Corkey B.E. Assays of intermediates of the citric acid cycle and related compounds by fluorometric enzyme methods. Meth. Enzymol. 13 (1969) 434-513
    • (1969) Meth. Enzymol. , vol.13 , pp. 434-513
    • Williamson, J.R.1    Corkey, B.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.