Review
doi: 10.1016/s0968-0004(98)01215-8.
The J-domain family and the recruitment of chaperone power
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- PMID: 9644977
- DOI: 10.1016/s0968-0004(98)01215-8
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Review
The J-domain family and the recruitment of chaperone power
Trends Biochem Sci.
1998 Jun.
Abstract
The defining feature of the Hsp40 chaperone family is a approximately 70-amino-acid-residue signature, termed the J domain, that is necessary for orchestrating interactions with its Hsp70 chaperone partner(s). J-domain proteins play important regulatory roles as co-chaperones, recruiting Hsp70 partners and accelerating the ATP-hydrolysis step of the chaperone cycle. Certain proteins could have acquired a J domain in order to present a specific substrate(s) to an Hsp70 partner and thus capitalize upon chaperone activities when carrying out cellular functions. J-domain proteins participate in complex biological processes, such as cell-cycle control by DNA tumor viruses, regulation of protein kinases and exocytosis.
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