Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1.

Abstract

3Corresponding author reveals a change in the overall shape and conformation of the protein consistent with reduced interactions between the two domains. These data suggest that the EEVD motif is involved in the intramolecular regulation of Hsp7O function and intermolecular interactions with HDJ-1.

Genome-wide identification of Hsp70 genes in channel catfish and their regulated expression after bacterial infection

“…However, in the liver at late stages of disease development, more hsp40 genes (nine) were found to be down-regulated. These findings could be explained by the co-chaperon system of Hsp40 and Hsp70 [48,49]. Hsp70 regulates the intracellular function and fate of proteins through the formation of direct proteinprotein interactions that occur largely through an EEVD-binding domain in its C terminus [50][51][52].…”

Cloning and expression of heat shock protein 70 gene in the haemocytes of pearl oyster (Pinctada fucata, Gould 1850) responding to bacterial challenge

“…In the whole Hsp70 amino acid sequences, the conservation of the N-terminus was higher than the C-terminus. However, the last four amino acids form a motif of EEVD which is highly conserved throughout all plant and animal Hsp70 family members [16].…”

“…Of these proteins, Hsp70s have been most extensively studied [1,2,[6][7][8][10][11][12][13][14][15][16][17][18][19][20][21][22]. A major inducing factor for Hsp70 upregulation is the occurrence of damaged cellular proteins, and the regulation of Hsp70 gene expression occurs mainly at the transcription level [8,9].…”

Hsp72 chaperone function is dispensable for protection against stress-induced apoptosis

“…The chaperone cycle is further regulated by the presence of co-chaperones, such as Hsp40, that stimulate or inhibit ATP hydrolysis and nucleotide exchange, as well as targeting Hsp70 molecules to specific organelles and substrates (Mayer and Bukau 2005;Young et al 2003). The C-terminal EEVD motif conserved in all cytosolic Hsp70 family members is known to interact with co-chaperones (Brinker et al 2002) as well as with the N-terminal ATP-binding domain and is essential for Hsp70 function (Freeman et al 1995).…”