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

ABSTRACT: 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.

SUBMITTER: Gianguzza F

PROVIDER: S-EPMC312894 | biostudies-literature | 2000 Apr

REPOSITORIES: biostudies-literature

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

Gianguzza F F Ragusa M A MA Roccheri M C MC Di Liegro I I Rinaldi A M AM

Cell stress & chaperones 20000401 2

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 th ...[more]

PMID: 11147969

Dataset Information

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

Publications

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

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