The Carboxy-Terminal Domain of Hsc70 Provides Binding Sites for a Distinct Set of Chaperone Cofactors

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 present study, the deduced amino acid sequence of PFHsp70 lacks the GGMP tetrapeptide repeats, which is in agreement with previous study in the mediterranean mussel, Mytilus galloprovincialis [45]. Fewer studies on the molecular or biochemical characterization of the bivalve Hsp70 and Hsc70 genes are available [17][18][19], and therefore, further investigation is necessary to reveal whether such structural variations affects the expression profiles of Hsp70 and Hsc70 as hypothesized in vertebrates [17], which could also provide insights to functional specificities between them.…”

“…The function of the GGMP repeats at the C-terminus has not been revealed, while it may form a structural entity together with the helical subdomain and the EEVD motif to mediate chaperone cofactors binding [18]. Based on the amino acid sequences comparison, Piano et al [36] pointed out that the GGMP repeats are present in the bivalve constitutive heat shock cognate 70 (Hsc70), while absent in the inducible heat shock protein 70 (Hsp70), as seen between mammalian Hsc70 and Hsp70 [17].…”

“…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].…”

hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria

“…32 We report here that the ATPase domain and C-terminal EEVD motif of hsp70 are crucial for antiapoptotic activity in CHOP-induced apoptosis. Similar results were noted in case of TNFa-induced apoptosis, 52 and in heat-shock-induced apoptosis.…”

“…On the other hand, the C-terminal EEVD motif of hsp70 is responsible for binding with co-chaperone hop and chip. 32,33 We investigated whether the ATPase domain and Cterminal motif are essential for antiapoptotic function of hsp70 ( Figure 6). We constructed expression plasmids for hsp70 mutant forms, lacking the ATPase domain or the Cterminal EEVD motif.…”