Cotranslational folding of proteins.

作者: M. A. Basharov

DOI: 10.1023/A:1002800822475

关键词: Protein foldingChaperone (protein)Bioorganic chemistryPhi value analysisBiophysicsChromosomal translocationBiochemistryRibosomeProtein translocationElongationBiology

摘要: We suppose that folding of proteins occurs cotranslationally by the following scheme. The polypeptide chains enter sites from protein translocation complexes (ribosome, machinery incorporated in membranes) directionally with N-terminus and gradually. chain starts to fold as soon its N-terminal residue enters site complex. process accompanies is completed after C-terminal leaves Proteins sequential stages, their into compartments. At each stage a particular conformation part has emerged complex formed. formation both conformations segment at final native last time does not exceed duration fastest elongation cycle on ribosome.

参考文章(54)
Ian J. Purvis, Andrew J.E. Bettany, T.Chinnappan Santiago, John R. Coggins, Kenneth Duncan, Robert Eason, Alistair J.P. Brown, The efficiency of folding of some proteins is increased by controlled rates of translation in vivo: A hypothesis Journal of Molecular Biology. ,vol. 193, pp. 413- 417 ,(1987) , 10.1016/0022-2836(87)90230-0
J. Kim, P.G. Klein, J.E. Mullet, Ribosomes pause at specific sites during synthesis of membrane-bound chloroplast reaction center protein D1. Journal of Biological Chemistry. ,vol. 266, pp. 14931- 14938 ,(1991) , 10.1016/S0021-9258(18)98567-4
K. John Ellis, F.‐Ulrich Hartl, Protein folding in the cell: competing models of chaperonin function. The FASEB Journal. ,vol. 10, pp. 20- 26 ,(1996) , 10.1096/FASEBJ.10.1.8566542
Kunihiro Kuwajima, Yoshiki Hiraoka, Masamichi Ikeguchi, Shintaro Sugai, Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin. Biochemistry. ,vol. 24, pp. 874- 881 ,(1985) , 10.1021/BI00325A010
Skip Williams, Timothy P. Causgrove, Rudolf Gilmanshin, Karen S. Fang, Robert H. Callender, William H. Woodruff, R. Brian Dyer, Fast events in protein folding: helix melting and formation in a small peptide. Biochemistry. ,vol. 35, pp. 691- 697 ,(1996) , 10.1021/BI952217P
Shingo Kato, Motoyoshi Okamura, Nobuo Shimamoto, Hiroyasu Utiyama, Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme. Biochemistry. ,vol. 20, pp. 1080- 1085 ,(1981) , 10.1021/BI00508A006
Cammon B. Arrington, Andrew D. Robertson, Microsecond protein folding kinetics from native-state hydrogen exchange. Biochemistry. ,vol. 36, pp. 8686- 8691 ,(1997) , 10.1021/BI970872M
Kathleen S. Crowley, Shuren Liao, Veronica E. Worrell, Gregory D. Reinhart, Arthur E. Johnson, Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore Cell. ,vol. 78, pp. 461- 471 ,(1994) , 10.1016/0092-8674(94)90424-3
CG Kurland, None, Strategies for efficiency and accuracy in gene expression Trends in Biochemical Sciences. ,vol. 12, pp. 126- 128 ,(1987) , 10.1016/0968-0004(87)90060-0