Hsp70 members occupy a central role in proteostasis and are found in different eukaryotic
cellular compartments. The mitochondrial Hsp70/J-protein machinery performs multiple functions vital
for the proper functioning of the mitochondria, including forming part of the import motor that
transports proteins from the cytosol into the matrix and inner membrane, and subsequently folds these
proteins in the mitochondria. However, unlike other Hsp70s, mitochondrial Hsp70 (mtHsp70) has the
propensity to self-aggregate, accumulating as insoluble aggregates. The self-aggregation of mtHsp70 is
caused by both interdomain and intramolecular communication within the ATPase and linker domains.
Since mtHsp70 is unable to fold itself into an active conformation, it requires an Hsp70 escort protein
(Hep) to both inhibit self-aggregation and promote the correct folding. Hep1 orthologues are present in
the mitochondria of many eukaryotic cells but are absent in prokaryotes. Hep1 proteins are relatively
small and contain a highly conserved zinc-finger domain with one tetracysteine motif that is essential
for binding zinc ions and maintaining the function and solubility of the protein. The zinc-finger domain
lies towards the C-terminus of Hep1 proteins, with very little conservation outside of this domain.
Other than maintaining mtHsp70 in a functional state, Hep1 proteins play a variety of other roles in the
cell and have been proposed to function as both chaperones and co-chaperones. The cellular
localisation and some of the functions are often speculative and are not common to all Hep1 proteins
analysed to date.
The
ANGULATA
7
gene encodes a DnaJ‐like zinc finger‐domain protein involved in chloroplast function and leaf development in Arabidopsis
