Disease relevance of HSP10

• The heterologous combination of cpn60 from E. coli plus yeast cpn10 is also functional [1].

High impact information on HSP10

• For these, the lack of hsp60 function has a more pronounced effect than inactivation of hsp10 [2].
• Mitochondria also contain a homologue of the cochaperonin GroES, called Hsp10, which is a functional regulator of the chaperonin [3].
• Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria [3].
• When dimeric ribulose-1,5-bisphosphate carboxylase (Rubisco) is denatured and allowed to bind to yeast cpn60, subsequent refolding of Rubisco is strictly dependent upon yeast cpn10 [1].
• A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast [4].

Chemical compound and disease context of HSP10

• 5. Using circular dichroism it is shown that, unlike E. coli cpn10, yeast cpn10 is not able to refold spontaneously after first being fully unfolded in 8 M urea [5].

Biological context of HSP10

• Haploid cells lacking a functional copy of CPN10 fail to grow at temperatures between 23 and 37 degrees C [6].
• Monomeric yeast cpn10 does not bind to GroEL in the presence of nucleotides, whereas under identical conditions E. coli cpn10 (GroES), having a strong sequence homology to the yeast form but a pI of 5.2, shows no pH-dependent dissociation and is able to complex with GroEL at both pH 7.5 and 4 [5].

Associations of HSP10 with chemical compounds

• Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpn10 by photoaffinity labeling with 2-azido-adenosine 5'-triphosphate [7].

Physical interactions of HSP10

• In the presence of ADP, one molecule of hsp10 binds to hsp60 with an apparent Kd of 0.9 nM and a second molecule of hsp10 binds with a Kd of 24 nM [8].

Other interactions of HSP10

• Our results identify Hsp10 as an essential component of the mitochondrial protein folding apparatus, participating in various aspects of Hsp60 function [3].
• Substitution of a single residue in the Hsp10-like domain of endogenous Mcm10 results in a dramatic reduction of steady-state Cdc17 levels [4].

Analytical, diagnostic and therapeutic context of HSP10

• In the presence of MgATP, yeast cpn60 and yeast cpn10 form a stable complex that can be isolated by gel filtration and that facilitates refolding of denatured Rubisco [1].

References