A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates

被引:271
|
作者
Szabo, A
Korszun, R
Hartl, FU
Flanagan, J
机构
[1] MEM SLOAN KETTERING CANC CTR, HOWARD HUGHES MED INST, NEW YORK, NY 10021 USA
[2] BROOKHAVEN NATL LAB, DEPT BIOL, UPTON, NY 11973 USA
[3] MEM SLOAN KETTERING CANC CTR, CELLULAR BIOCHEM & BIOPHYS PROGRAM, NEW YORK, NY 10021 USA
来源
EMBO JOURNAL | 1996年 / 15卷 / 02期
关键词
chaperone; DnaJ; heat-shock protein; zinc finger-like domain;
D O I
10.1002/j.1460-2075.1996.tb00371.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Escherichia coli heat-shock protein DnaJ cooperates with the Hsp70 homolog DnaK in protein folding in vitro and in vivo, Little is known about the structural features of Dual that mediate its interaction with DnaK and unfolded polypeptide, DnaJ contains at least four blocks of sequence representing potential functional domains which have been conserved throughout evolution, In order to understand the role of each of these regions, we have analyzed DnaJ fragments in reactions corresponding to known functions of the intact protein, Both the N-terminal 70 amino acid 'J-domain' and a 35 amino acid glycine-phenylalanine region following it are required for interactions with DnaK, However, only complete DnaJ can cooperate with DnaK and a third protein, GrpE, in refolding denatured firefly Luciferase, As demonstrated by atomic absorption and extended X-ray absorption fine structure spectroscopy (EXAFS), the 90 amino acid cysteine-rich region of DnaJ contains two Zn atoms tetrahedrally coordinated to four cysteine residues, resembling their arrangement in the C4 Zn binding domains of certain DNA binding proteins, Interestingly, binding experiments and cross-linking studies indicate that this Zn finger-like domain is required for the DnaJ molecular chaperone to specifically recognize and bind to proteins in their denatured state.
引用
收藏
页码:408 / 417
页数:10
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