Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases

J Biol Chem. 1988 Oct 25;263(30):15462-6.


It has recently been discovered that several lens proteins in birds and lower vertebrates are active enzymes or enzyme-related proteins (Wistow, G., Mulders, J. W. M., and de Jong, W. W. (1987) Nature 326, 622-624; Wistow, G., and Piatigorsky, J. (1987) Science 236, 1554-1556). We report here a novel lens protein, designated as lambda-crystallin, that occurs in rabbit and hare. It constitutes 7-8% of the total lens protein and has a subunit molecular mass of 35 kDa. Sequencing of cDNA clones encoding rabbit lambda-crystallin revealed 30% homology (at the amino acid sequence level) with L-3-hydroxyacyl-CoA dehydrogenase from pig mitochondria and 26% homology with enoyl-CoA hydratase-3-hydroxyacyl-CoA dehydrogenase from rat peroxisomes. Also, the presence of a putative beta-alpha-beta nucleotide-binding fold and low levels of non-lens expression are indicative of some enzymatic function for lambda-crystallin (or highly related sequences) in non-lens tissues. lambda-Crystallin thus represents the first example of an enzyme-related crystallin in lenses from mammalian species. The recruitment of enzymes as lens structural proteins apparently is an evolutionary strategy which has been applied independently in different lineages.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Hydroxyacyl CoA Dehydrogenases / analysis*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Crystallins / analysis*
  • DNA / analysis
  • Molecular Sequence Data
  • Molecular Weight
  • Rabbits


  • Crystallins
  • DNA
  • 3-Hydroxyacyl CoA Dehydrogenases

Associated data

  • GENBANK/M22743