期刊论文详细信息
FEBS Letters
Co‐operative binding of hsp60 may promote transfer hsp70 and correct folding of imported proteins in mitochondria
Endo, Toshiya1 
[1] Department of Chemistry, Faculty of Science, Nagoya University, Chikusa-ku, Nagoya 464-01, Japan
关键词: Molecular chaperone;    Hsp70: Hsp60;    Mitochondrion;    Protein import;   
DOI  :  10.1016/0014-5793(91)81139-Y
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

I propose that a molecular chaperone hsp60 binds to and dissociates from the unfolded polypeptide or folding intermediate in a positively co-operative manner, but another chaperone hsp70 shows no such co-operativity. This could simply explain the fact that the protein newly imported in the mitochondrial matrix is transferred from hsp70 to hsp60 and hsp6O promotes corrert folding or the substrate protein while hsp70 does not.

【 授权许可】

Unknown   

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