Molecular Biology and Evolution, Vol 2, 484-493, Copyright © 1985 by Society for Molecular Biology and Evolution
WW de Jong, A Zweers, M Versteeg, HC Dessauer and M Goodman
The amino acid sequences of the eye lens protein alpha-crystallin A from
many mammalian and avian species, two frog species, and a dogfish have
provided detailed information about the molecular evolution of this protein
and allowed some useful inferences about phylogenetic relationships among
these species. We now have isolated and sequenced the alpha-crystallins of
the American alligator and the common tegu lizard. The reptilian alpha A
chains appear to have evolved as slowly as those of other vertebrates,
i.e., at two to three amino acid replacements per 100 residues in 100 Myr.
The lack of charged replacements and the general types and distribution of
replacements also are similar to those in other vertebrate alpha A chains.
Maximum- parsimony analyses of the total data set of 67 vertebrate alpha A
sequences support the monophyletic origin of alligator, tegu, and birds and
favor the grouping of crocodilians and birds as surviving sister groups in
the subclass Archosauria.
ORIGINAL ARTICLE
alpha-Crystallin A sequences of Alligator mississippiensis and the lizard Tupinambis teguixin: molecular evolution and reptilian phylogeny
Department of Biochemistry, University of Nijmegen, The Netherlands.
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