Homology between the primary structures of the major bovine beta-crystallin chains.

Partial amino acid sequences of six major subunits of bovine beta-crystallin have been determined by automatic liquid-phase Edman degradation and the dansyl-Edman procedure, complemented by amino acid analyses of peptides. The results show that, including the previously established beta Bp sequence [H. P. C. Driessen et al. (1981) Eur. J. Biochem. 121, 83-91], there exist at least seven primary gene products in bovine beta-crystallin, which exhibit 40% or more sequence homology. Two of the gene products are completely identical except for the presence in one of them of 17 additional residues at the N terminus, possibly caused by differential splicing of the same primary RNA transcript. The rate of evolutionary change of the beta chains (4% sequence change per 100 X 10(6) years) is about equally slow as that of alpha-crystallin, and the gene duplications giving rise to the different chains must have occurred very early in vertebrate evolution. The beta chains can be divided into two groups, according to sequence homology and presence of deletions/insertions and C-terminal extension, on which basis a new, rational nomenclature for the beta subunits is introduced. The N-terminal extensions of all beta chains are very different in length and sequence, even between homologous beta chains in different species. Possible explanations for this finding are discussed.