Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP.
作者： Tomonao Inobe , Tadashi Makio , Etsuko Takasu-Ishikawa , Tomoki P. Terada , Kunihiro Kuwajima
DOI: 10.1016/S0167-4838(00)00274-0
关键词:
摘要: Chaperonin-assisted protein folding proceeds through cycles of ATP binding and hydrolysis by GroEL, which undergoes a large structural change the or hydrolysis. One main concerns GroEL is mechanism productive cooperative induced nucleotide. We studied nature nucleotide titration using isothermal calorimetry fluorescence spectroscopy. Our results indicated that ADP analogs to single ring mutant (SR1), as well was non-cooperative. Only induces an apparently conformational in both proteins. Furthermore, changes pyrene-labeled has two kinds sites. The result fits with model sites are non-cooperative independent each other. These suggest may be necessary for transition GroEL.
elsevier.com
sci-hub.se 参考文章(44)
Kerstin Braig, Zbyszek Otwinowski, Rashmi Hegde, David C. Boisvert, Andrzej Joachimiak, Arthur L. Horwich, Paul B. Sigler, The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature. ,vol. 371, pp. 578- 586 ,(1994) , 10.1038/371578A0
Bernd Bukau, Arthur L Horwich, The Hsp70 and Hsp60 Chaperone Machines Cell. ,vol. 92, pp. 351- 366 ,(1998) , 10.1016/S0092-8674(00)80928-9
K. Ito, Y. Akiyama, In vivo analysis of integration of membrane proteins in Escherichia coli Molecular Microbiology. ,vol. 5, pp. 2243- 2253 ,(1991) , 10.1111/J.1365-2958.1991.TB02154.X
Jonathan S. Weissman, Corinne M. Hohl, Oleg Kovalenko, Yechezkel Kashi, Shaoxia Chen, Kerstin Braig, Helen R. Saibil, Wayne A. Fenton, Arthur L. Norwich, Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under groes Cell. ,vol. 83, pp. 577- 587 ,(1995) , 10.1016/0092-8674(95)90098-5
Jean Chatellier, Ashley M Buckle, Alan R Fersht, GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices. Journal of Molecular Biology. ,vol. 292, pp. 163- 172 ,(1999) , 10.1006/JMBI.1999.3040
Matthew J Cliff, Neil M Kad, Nicky Hay, Peter A Lund, Martin R Webb, Steven G Burston, Anthony R Clarke, A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL Journal of Molecular Biology. ,vol. 293, pp. 667- 684 ,(1999) , 10.1006/JMBI.1999.3138
J. D. Wang, M. D. Michelitsch, J. S. Weissman, GroEL-GroES-mediated protein folding requires an intact central cavity Proceedings of the National Academy of Sciences of the United States of America. ,vol. 95, pp. 12163- 12168 ,(1998) , 10.1073/PNAS.95.21.12163
A. P. Ben-Zvi, J. Chatellier, A. R. Fersht, P. Goloubinoff, Minimal and optimal mechanisms for GroE-mediated protein folding Proceedings of the National Academy of Sciences of the United States of America. ,vol. 95, pp. 15275- 15280 ,(1998) , 10.1073/PNAS.95.26.15275
Z. Lin, E. Eisenstein, Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 93, pp. 1977- 1981 ,(1996) , 10.1073/PNAS.93.5.1977
Steven G. Burston, Neil A. Ranson, Anthony R. Clarke, The origins and consequences of asymmetry in the chaperonin reaction cycle Journal of Molecular Biology. ,vol. 249, pp. 138- 152 ,(1995) , 10.1006/JMBI.1995.0285