Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin.

Chaperonins are ubiquitous proteins that facilitate protein folding in an adenosine triphosphate-dependent manner. Here we report the isolation of a sea urchin cDNA (Plhsp60) coding for mitochondrial chaperonin (Cpn60), whose basal expression is further enhanced by heat shock. The described cDNA corresponds to a full-length mRNA encoding a protein of 582 amino acids, the first 32 of which constitute a putative mitochondrial targeting leader sequence. Comparative analysis has demonstrated that this protein is highly conserved in evolution.