메뉴 건너뛰기




Volumn 135, Issue 2, 2001, Pages 139-146

ATP-induced structural change of the thermosome is temperature-dependent

Author keywords

Chaperonin; Protein folding; SANS; Small angle neutron scattering; Thermosome

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONIN; PROTEIN; RECOMBINANT PROTEIN; THERMOSOME; UNCLASSIFIED DRUG;

EID: 18744389426     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4373     Document Type: Article
Times cited : (35)

References (24)
  • 1
    • 0033598189 scopus 로고    scopus 로고
    • Recurrent paralogy in the evolution of archaeal chaperonins
    • Archibald, J. M., Logsdon, J. M., and Doolittle, W. F. (1999) Recurrent paralogy in the evolution of archaeal chaperonins. Curr. Biol. 9(18), 1053-1056.
    • (1999) Curr. Biol. , vol.9 , Issue.18 , pp. 1053-1056
    • Archibald, J.M.1    Logsdon, J.M.2    Doolittle, W.F.3
  • 3
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel, L., Lowe, J., Stock, D., Stetter, K. O., Huber, H., Huber, R., and Steinbacher, S. (1998) Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 93(1), 125-138.
    • (1998) Cell , vol.93 , Issue.1 , pp. 125-138
    • Ditzel, L.1    Lowe, J.2    Stock, D.3    Stetter, K.O.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 4
    • 0032561205 scopus 로고    scopus 로고
    • Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability
    • Furutani, M., Iida, T., Yoshida, T., and Maruyama, T. (1998) Group II chaperonin in a thermophilic methanogen, Methanococcus thermolithotrophicus. Chaperone activity and filament-forming ability. J. Biol. Chem. 273(43), 28399-28407.
    • (1998) J. Biol. Chem. , vol.273 , Issue.43 , pp. 28399-28407
    • Furutani, M.1    Iida, T.2    Yoshida, T.3    Maruyama, T.4
  • 5
    • 0000897622 scopus 로고
    • A new method for the evaluation of small-angle scattering data
    • Glatter, O. (1977) A new method for the evaluation of small-angle scattering data. J. Appl. Crystallogr. 10, 415-421.
    • (1977) J. Appl. Crystallogr. , vol.10 , pp. 415-421
    • Glatter, O.1
  • 7
  • 8
    • 0034698423 scopus 로고    scopus 로고
    • ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy
    • Gutsche, I., Mihalache, O., Hegerl, R., Typke, D., and Baumeister, W. (2000c) ATPase cycle controls the conformation of an archaeal chaperonin as visualized by cryo-electron microscopy. FEBS Lett. 477(3), 278-282.
    • (2000) FEBS Lett. , vol.477 , Issue.3 , pp. 278-282
    • Gutsche, I.1    Mihalache, O.2    Hegerl, R.3    Typke, D.4    Baumeister, W.5
  • 9
    • 0028559575 scopus 로고
    • Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex
    • Harris, J. R., Pluckthun, A., and Zahn, R. (1994) Transmission electron microscopy of GroEL, GroES, and the symmetrical GroEL/ES complex. J. Struct. Biol. 112, 216-230.
    • (1994) J. Struct. Biol. , vol.112 , pp. 216-230
    • Harris, J.R.1    Pluckthun, A.2    Zahn, R.3
  • 10
    • 0031945917 scopus 로고    scopus 로고
    • The thermosome: Chaperonin with a built-in lid
    • News
    • Horwich, A. L., and Saibil, H. R. (1998) The thermosome: Chaperonin with a built-in lid [News]. Nat. Struct. Biol. 5(5), 333-336.
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.5 , pp. 333-336
    • Horwich, A.L.1    Saibil, H.R.2
  • 11
    • 0030668929 scopus 로고    scopus 로고
    • Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
    • Klumpp, M., Baumeister, W., and Essen, L. O. (1997) Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell 91(2), 263-270.
    • (1997) Cell , vol.91 , Issue.2 , pp. 263-270
    • Klumpp, M.1    Baumeister, W.2    Essen, L.O.3
  • 13
    • 0343907201 scopus 로고    scopus 로고
    • Cytoplasmic chaperonin containing TCP-1: Structural and functional characterization
    • Melki, R., Batelier, G., Soulie, S., and Williams, R. C., Jr. (1997) Cytoplasmic chaperonin containing TCP-1: Structural and functional characterization. Biochemistry 36(19), 5817-5826.
    • (1997) Biochemistry , vol.36 , Issue.19 , pp. 5817-5826
    • Melki, R.1    Batelier, G.2    Soulie, S.3    Williams R.C., Jr.4
  • 14
    • 0031719642 scopus 로고    scopus 로고
    • Group II chaperonin in an open conformation examined by electron tomography
    • Nitsch, M., Walz, J., Typke, D., Klumpp, M., Essen, L. O., and Baumeister, W. (1998) Group II chaperonin in an open conformation examined by electron tomography. Nat. Struct. Biol. 5(10), 855-857.
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.10 , pp. 855-857
    • Nitsch, M.1    Walz, J.2    Typke, D.3    Klumpp, M.4    Essen, L.O.5    Baumeister, W.6
  • 15
    • 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. (1996) The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87(2), 241-251.
    • (1996) Cell , vol.87 , Issue.2 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 16
    • 0034636980 scopus 로고    scopus 로고
    • Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin
    • Schoehn, G., Hayes, M., Cliff, M., Clarke, A. R., and Saibil, H. R. (2000) Domain rotations between open, closed and bullet-shaped forms of the thermosome, an archaeal chaperonin. J. Mol. Biol. 301, 323-332.
    • (2000) J. Mol. Biol. , vol.301 , pp. 323-332
    • Schoehn, G.1    Hayes, M.2    Cliff, M.3    Clarke, A.R.4    Saibil, H.R.5
  • 17
    • 0032498233 scopus 로고    scopus 로고
    • The solution structure of functionally active human proliferating cell nuclear antigen determined by small-angle neutron scattering
    • Schurtenberger, P., Egelhaaf, S. U., Hindges, R., Maga, G., Jonsson, Z. O., May, R. P., Glatter, O., and Hubscher, U. (1998) The solution structure of functionally active human proliferating cell nuclear antigen determined by small-angle neutron scattering. J. Mol. Biol. 275, 123-132.
    • (1998) J. Mol. Biol. , vol.275 , pp. 123-132
    • Schurtenberger, P.1    Egelhaaf, S.U.2    Hindges, R.3    Maga, G.4    Jonsson, Z.O.5    May, R.P.6    Glatter, O.7    Hubscher, U.8
  • 20
    • 0032478214 scopus 로고    scopus 로고
    • Protein hydration in solution: Experimental observation by X-ray and neutron scattering
    • Svergun, D. I., Richard, S., Koch, M. H., Sayers, Z., Kuprin, S., and Zaccai, G. (1998) Protein hydration in solution: Experimental observation by X-ray and neutron scattering. Proc. Natl. Acad. Sci. USA 95(5), 2267-2272.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.5 , pp. 2267-2272
    • Svergun, D.I.1    Richard, S.2    Koch, M.H.3    Sayers, Z.4    Kuprin, S.5    Zaccai, G.6
  • 21
    • 0029643911 scopus 로고    scopus 로고
    • Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
    • Thiyagarajan, P., Henderson, S. J., and Joachimiak, A. (1996) Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure 4, 79-88.
    • (1996) Structure , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 22
    • 0031822749 scopus 로고    scopus 로고
    • The role of chaperonins in vivo: The next frontier
    • Trent, J. D., Kagawa, H. K., and Yaoi, T. (1998) The role of chaperonins in vivo: The next frontier. Ann. N.Y. Acad. Sci. 851, 36-47.
    • (1998) Ann. N.Y. Acad. Sci. , vol.851 , pp. 36-47
    • Trent, J.D.1    Kagawa, H.K.2    Yaoi, T.3
  • 24
    • 0032147230 scopus 로고    scopus 로고
    • Chaperonin filaments: Their formation and an evaluation of methods for studying them
    • Yaoi, T., Kagawa, H. K., and Trent, J. D. (1998) Chaperonin filaments: Their formation and an evaluation of methods for studying them. Arch. Biochem. Biophys. 356, 55-62.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 55-62
    • Yaoi, T.1    Kagawa, H.K.2    Trent, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.