The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and diverse family of chaperones

Cell Stress Chaperones. 2001 Jul;6(3):209-18. doi: 10.1379/1466-1268(2001)006<0209:tjdpoa>2.0.co;2.

Abstract

A total of 89 J-domain proteins were identified in the genome of the model flowering plant Arabidopsis thaliana. The deduced amino acid sequences of the J-domain proteins were analyzed for an assortment of structural features and motifs. Based on the results of sequence comparisons and structure and function predictions, 51 distinct families were identified. The families ranged in size from 1 to 6 members. Subcellular localizations of the A thaliana J-domain proteins were predicted; species were found in both the soluble and membrane compartments of all cellular organelles. Based on digital Northern analysis, the J-domain proteins could be separated into groups of low, medium, and moderate expression levels. This genomics-based analysis of the A thaliana J-domain proteins establishes a framework for detailed studies of biological function and specificity. It additionally provides a comprehensive basis for evolutionary comparisons.

MeSH terms

  • Arabidopsis / genetics*
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / genetics*
  • Arabidopsis Proteins / metabolism
  • Databases, Factual
  • Expressed Sequence Tags
  • Genome, Plant
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / classification
  • Heat-Shock Proteins / genetics*
  • Heat-Shock Proteins / metabolism
  • Molecular Chaperones / classification
  • Molecular Chaperones / genetics*
  • Molecular Chaperones / metabolism
  • Phylogeny
  • Protein Structure, Tertiary

Substances

  • ATJ1 protein, Arabidopsis
  • ATJ2 protein, Arabidopsis
  • Arabidopsis Proteins
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones