[Cooperation between heat shock proteins in organizing of proteins spatial structure]

Postepy Hig Med Dosw (Online). 2014 Jun 9;68:793-807. doi: 10.5604/17322693.1108406.
[Article in Polish]

Abstract

Heat shock proteins (Hsps) are a class of proteins with highly conserved amino acid sequences. They are widespread in nature; they are found in archeons, true bacteria and eukaryotic organisms. Hsps from various families, commonly interact to execute essential cellular tasks, such as molecular regulation of newly synthesized protein-folding or restoration of the appropriate conformation of denatured and aggregated proteins. In this review we discuss mechanisms of spatial organization of protein structure mediated by Hsp10, Hsp40, Hsp60, Hsp70, Hsp104 (Hsp100) and Hsp110. Interactions between Hsps of different molecular weights are described.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacteria / metabolism
  • Conserved Sequence
  • Eukaryotic Cells / metabolism
  • HSP110 Heat-Shock Proteins / chemistry
  • HSP110 Heat-Shock Proteins / metabolism
  • HSP40 Heat-Shock Proteins / metabolism
  • HSP70 Heat-Shock Proteins / metabolism
  • HSP90 Heat-Shock Proteins / chemistry
  • HSP90 Heat-Shock Proteins / metabolism
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Chaperones / metabolism
  • Molecular Structure
  • Molecular Weight
  • Protein Folding
  • Substrate Specificity

Substances

  • HSP110 Heat-Shock Proteins
  • HSP40 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • HSP90 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones