6533b832fe1ef96bd129a47d

RESEARCH PRODUCT

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

Fabrizio GianguzzaMaria Antonietta RagusaAnna Maria RinaldiItalia Di LiegroMaria Carmela Roccheri

subject

Messenger RNADNA ComplementaryEmbryo NonmammalianbiologyShort CommunicationMolecular Sequence DataChaperonin 60Cell Biologybiology.organism_classificationBiochemistryMolecular biologyParacentrotus lividusMitochondriaChaperoninCell biologySea UrchinsComplementary DNAAnimalsProtein foldingHSP60Amino Acid SequenceRNA MessengerHeat shockPeptide sequenceHeat-Shock Response

description

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.

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