Isolation and characterization of two cytoplasmic hsp90s from Mytilus galloprovincialis (Mollusca: Bivalvia) that contain a complex promoter with a p53 binding site

Gene. 2009 Feb 15;431(1-2):47-54. doi: 10.1016/j.gene.2008.10.028. Epub 2008 Nov 13.

Abstract

The commercially important marine bivalve Mytilus galloprovincialis (Mediterranean mussel) is considered a valuable bioindicator, due to its exposure to various pollutants and extreme environmental conditions. Environmental responsive genes, such as the hsp90s, protect the structure and function of cells and accomplish a significant task in cellular homeostasis. To study the hsp90s in M. galloprovincialis a genomic library was screened and two hsp90s were isolated. Sequence analysis revealed that the two genes exhibit great similarities in both the 5' non-coding and the coding region but differ in the 3' non-coding region, as well as in three introns, due to the presence of repeated sequences. Few synonymous substitutions in the coding region of the genes result to an identical predicted polypeptide, which belongs to the cytoplasmic HSP90 subfamily. The 5' non-coding region contains a non-translated exon and multiple binding sites for various transcription factors. The presence of a p53 binding site in the promoter of the isolated genes raises questions about the possible implication of hsp90s in the molluscan leukemia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Clone Cells
  • Cytoplasm / metabolism*
  • Expressed Sequence Tags
  • Genome / genetics
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / genetics*
  • HSP90 Heat-Shock Proteins / isolation & purification*
  • Molecular Sequence Data
  • Mytilus / genetics*
  • Peptides / chemistry
  • Promoter Regions, Genetic / genetics*
  • Sequence Homology, Amino Acid
  • Transcription, Genetic
  • Tumor Suppressor Protein p53 / metabolism*

Substances

  • HSP90 Heat-Shock Proteins
  • Peptides
  • Tumor Suppressor Protein p53