en
Scientific article
English

The J-domain family and the recruitment of chaperone power

ContributorsKelley, William
Published inTrends in biochemical sciences, vol. 23, no. 6, p. 222-227
Publication date1998
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.

Keywords
  • Amino Acid Sequence
  • Animals
  • HSP70 Heat-Shock Proteins/ physiology
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Structure-Activity Relationship
Citation (ISO format)
KELLEY, William. The J-domain family and the recruitment of chaperone power. In: Trends in biochemical sciences, 1998, vol. 23, n° 6, p. 222–227.
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ISSN of the journal0968-0004
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