Cloning and characterization of the yeast chaperonin HSP60 gene

Gene. 1989 Dec 14;84(2):295-302. doi: 10.1016/0378-1119(89)90503-9.

Abstract

The heat-shock protein, HSP60, is abundant in prokaryotes and eukaryotes and is required in the assembly of specific proteins. We have cloned the Saccharomyces cerevisiae HSP60 gene from a lambda gt11 genomic library using monoclonal antibodies, have obtained its sequence, determined its transcription start point, and shown that it exists as a single copy. The predicted HSP60 contains a mitochondrial target sequence and exhibits striking amino acid sequence similarity to its counterparts in bacteria, plants, and humans. These data indicate a high level of evolutionary conservation and are consistent with the suggestion of evolutionarily conserved function [Hemmingsen et al., Nature 333 (1988), 330-334].

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal
  • Base Sequence
  • Chaperonins
  • DNA, Fungal / genetics
  • DNA, Fungal / isolation & purification
  • Fungal Proteins / genetics*
  • Gene Library
  • Genes, Bacterial
  • Genes, Fungal*
  • Heat-Shock Proteins / genetics*
  • Humans
  • Molecular Sequence Data
  • Plants / genetics
  • Promoter Regions, Genetic
  • Proteins / genetics*
  • Saccharomyces cerevisiae / genetics*
  • Sequence Homology, Nucleic Acid
  • Single-Strand Specific DNA and RNA Endonucleases

Substances

  • Antibodies, Monoclonal
  • DNA, Fungal
  • Fungal Proteins
  • Heat-Shock Proteins
  • Proteins
  • Single-Strand Specific DNA and RNA Endonucleases
  • Chaperonins