Translator Disclaimer
1 April 2000 Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin
Fabrizio Gianguzza, Maria Antonietta Ragusa, Maria Carmela Roccheri, Italia Di Liegro, Anna Maria Rinaldi
Author Affiliations +
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.

Fabrizio Gianguzza, Maria Antonietta Ragusa, Maria Carmela Roccheri, Italia Di Liegro, and Anna Maria Rinaldi "Isolation and characterization of a Paracentrotus lividus cDNA encoding a stress-inducible chaperonin," Cell Stress & Chaperones 5(2), 87-89, (1 April 2000). https://doi.org/10.1379/1466-1268(2000)005<0087:IACOAP>2.0.CO;2
Received: 26 October 1999; Accepted: 1 December 1999; Published: 1 April 2000
JOURNAL ARTICLE
3 PAGES

This article is only available to subscribers.
It is not available for individual sale.
+ SAVE TO M