Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network

Microbiol Mol Biol Rev. 2002 Mar;66(1):64-93; table of contents. doi: 10.1128/MMBR.66.1.64-93.2002.


Alpha-crystallins were originally recognized as proteins contributing to the transparency of the mammalian eye lens. Subsequently, they have been found in many, but not all, members of the Archaea, Bacteria, and Eucarya. Most members of the diverse alpha-crystallin family have four common structural and functional features: (i) a small monomeric molecular mass between 12 and 43 kDa; (ii) the formation of large oligomeric complexes; (iii) the presence of a moderately conserved central region, the so-called alpha-crystallin domain; and (iv) molecular chaperone activity. Since alpha-crystallins are induced by a temperature upshift in many organisms, they are often referred to as small heat shock proteins (sHsps) or, more accurately, alpha-Hsps. Alpha-crystallins are integrated into a highly flexible and synergistic multichaperone network evolved to secure protein quality control in the cell. Their chaperone activity is limited to the binding of unfolding intermediates in order to protect them from irreversible aggregation. Productive release and refolding of captured proteins into the native state requires close cooperation with other cellular chaperones. In addition, alpha-Hsps seem to play an important role in membrane stabilization. The review compiles information on the abundance, sequence conservation, regulation, structure, and function of alpha-Hsps with an emphasis on the microbial members of this chaperone family.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallins* / chemistry
  • Crystallins* / genetics
  • Crystallins* / metabolism
  • Gene Expression Regulation*
  • Heat-Shock Proteins* / chemistry
  • Heat-Shock Proteins* / genetics
  • Heat-Shock Proteins* / metabolism
  • Humans
  • Molecular Chaperones* / chemistry
  • Molecular Chaperones* / genetics
  • Molecular Chaperones* / metabolism
  • Molecular Sequence Data
  • Structure-Activity Relationship


  • Crystallins
  • Heat-Shock Proteins
  • Molecular Chaperones