PMID:3170592
| Citation |
Mulders, JW, Hendriks, W, Blankesteijn, WM, Bloemendal, H and de Jong, WW (1988) Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases. J. Biol. Chem. 263:15462-6 |
|---|---|
| Abstract |
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. |
| Links | |
| Keywords |
3-Hydroxyacyl CoA Dehydrogenases/analysis; Amino Acid Sequence; Animals; Base Sequence; Cloning, Molecular; Crystallins/analysis; DNA/analysis; Molecular Sequence Data; Molecular Weight; Rabbits |
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