Molecular Biology and Evolution, Vol 2, 347-358, Copyright © 1985 by Society for Molecular Biology and Evolution
PP Minghetti, SW Law and A Dugaiczyk
We conducted the present study in an attempt to correlate function with the
rate of molecular evolution for serum albumin and alpha- fetoprotein. We
found a high rate of silent substitution (between 5 X 10(-9) and 7 X
10(-9)/site/year) for both the albumin and alpha- fetoprotein genes,
perhaps the highest so far reported for an expressed nuclear gene. The
rates of effective substitution and amino acid changes were also very high,
but in contrast to silent substitutions, they are higher for
alpha-fetoprotein than for albumin by approximately 70%. For
alpha-fetoprotein, the rate of effective substitution (1.5 X
10(-9)/site/year) may be approaching that for nonfunctional pseudogenes
(about 3 X 10(-9)/site/year). Evolutionary divergence was also estimated at
the amino acid level. It was found that the rate of change of
alpha-fetoprotein (55% amino acids replaced in 100 Myr) approaches that of
the fastest-evolving fibrinopeptides (92% amino acids replaced in 100 Myr).
This high rate may indicate that alpha-fetoprotein can tolerate a great
deal of molecular variation without its function being impaired in the
process. Albumin evolves at a slower rate (39% amino acids replaced in 100
Myr), although still faster than either hemoglobin (17% amino acids
replaced in 100 Myr) or cytochrome c (5% amino acids replaced in 100 Myr).
The slower evolutionary rate may indicate that albumin has more refined
functional specifications and hence can tolerate fewer mutational changes.
The latter conclusion remains, however, to be reconciled with the condition
of inherited analbuminemia, where a virtually complete absence of albumin
produces surprisingly few symptoms.
ORIGINAL ARTICLE
The rate of molecular evolution of alpha-fetoprotein approaches that of pseudogenes
Department of Biochemistry, University of California, Riverside 92521.
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