Disease relevance of HSPE1

• In addition, large amounts of recombinant rat Cpn10 were produced in Escherichia coli and found to be identical to its authentic counterpart except for the lack of N-terminal acetylation [1].

High impact information on HSPE1

• By comparing these two forms of Cpn10, it was found that acetylation does not influence the oligomeric structure of Cpn10 and is not essential for chaperone activity or mitochondrial import in vitro [1].
• The present work demonstrates that the rhodanese-cpn60 complex can be dissociated by urea to allow folding to proceed, thus removing the obligatory requirement for cpn10 and ATP [2].
• Complementary DNA sequence of bovine cpn10 (Hsp10), a chaperone protein from mitochondria [3].
• It is deduced from overlapping partial cDNAs amplified in polymerase chain reactions from bovine heart cDNA, using in the first instance mixtures of synthetic oligonucleotide primers based on the incomplete sequence of the cpn10 (Hsp10) chaperone protein from rat liver mitochondria [3].
• The ability of the two proteins to refold from 8 M urea to enzymatically active species was similar both for unassisted refolding, and when folding was assisted either by the detergent, lauryl maltoside or by the E. coli chaperonin system composed of cpn60 and cpn10 [4].

Biological context of HSPE1

• In contrast, N-terminal acetylation proved crucial in the protection of Cpn10 against degradation by N-ethylmaleimide-sensitive proteases derived from organellar preparations of rat liver [1].

References