HSP70 — Pisum sativum

Summary

PsHSP70-8 (PSAT2G051360) on chromosome 2LG1 encodes a heat shock 70 kDa protein, a member of the Hsp70 family with an ATPase nucleotide-binding domain and a peptide-binding domain. The gene product is a protein folding chaperone with ATP hydrolase activity and heat shock protein binding, and is associated with ATP binding. In pea, PsHSP70-8 is associated with mitochondrial protein import and biogenesis, protein folding in the endoplasmic reticulum, the ERAD pathway, and the unfolded protein response. It has been linked to seed maturation, embryogenesis, cell development, DNA replication, and response to virus and stress. The protein localizes to the ER lumen and chaperone complex, chloroplast membrane, tonoplast, cytoplasm, and nucleus. Studies of related genes in other species further link the family to similar chaperone and stress-response functions.