The J-domain family and the recruitment of chaperone power

Trends Biochem Sci. 1998 Jun;23(6):222-7. doi: 10.1016/s0968-0004(98)01215-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • HSP70 Heat-Shock Proteins / physiology*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Structure-Activity Relationship


  • HSP70 Heat-Shock Proteins