Molecular Biology and Evolution, Vol 7, 327-339, Copyright © 1990 by Society for Molecular Biology and Evolution
C O'hUigin, L Chan and WH Li
We have cloned and sequenced bovine apoA-I cDNA. Comparison with the apoA-I
sequences of six other vertebrates shows the bovine gene to be most similar
to that of the dog. Estimates of substitution rates show that apoA-I
evolves approximately 25% faster than an average gene in mammalian
lineages. All portions of the coding region evolve at roughly similar
rates, suggesting that global conformation is conserved. However, a region
of the rat protein has evolved rapidly both relative to other portions of
the rat sequence and relative to homologous regions in other mammals. To
extend our analysis to other apolipoproteins, we compared four vertebrate
apoB-100 sequences. Conserved regions were found to include two putative
LDL receptor binding domains, in addition to several regions of
unidentified function. Comparison of the apoA-I sequences and the apoB-100
sequences indicates that the latter evolve approximately 40% faster than
the former and at twice the average rate for mammalian proteins.
ORIGINAL ARTICLE
Cloning and sequencing of bovine apolipoprotein A-I cDNA and molecular evolution of apolipoproteins A-I and B-100
Center for Demographic and Population Genetics, University of Texas, Houston 77225.
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