Molecular Biology and Evolution, Vol 13, 1039-1043, Copyright © 1996 by Society for Molecular Biology and Evolution
K Fushitani, K Higashiyama, EN Moriyama, K Imai and K Hosokawa
To elucidate phylogenetic relationships among amniotes and the evolution of
alpha globins, hemoglobins were analyzed from the Komodo dragon (Komodo
monitor lizard) Varanus komodoensis, the world's largest extant lizard,
inhabiting Komodo Islands, Indonesia. Four unique globin chains (alpha A,
alpha D, beta B, and beta C) were isolated in an equal molar ratio by high
performance liquid chromatography from the hemolysate. The amino acid
sequences of two alpha chains were determined. The alpha D chain has a
glutamine at E7 as does an alpha chain of a snake, Liophis miliaris, but
the alpha A chain has a histidine at E7 like the majority of hemoglobins.
Phylogenetic analyses of 19 globins including two alpha chains of Komodo
dragon and ones from representative amniotes showed the following results:
(1) The a chains of squamates (snakes and lizards), which have a glutamine
at E7, are clustered with the embryonic alpha globin family, which
typically includes the alpha D chain from birds; (2) birds form a sister
group with other reptiles but not with mammals; (3) the genes for embryonic
and adult types of alpha globins were possibly produced by duplication of
the ancestral alpha gene before ancestral amniotes diverged, indicating
that each of the present amniotes might carry descendants of the two types
of alpha globin genes; (4) squamates first split off from the ancestor of
other reptiles and birds.
ORIGINAL ARTICLE
The amino acid sequences of two alpha chains of hemoglobins from Komodo dragon Varanus komodoensis and phylogenetic relationships of amniotes
Department of Biochemistry, Kawasaki Medical School, Okayama, Japan. kfushita@bcc.kawasaki-m.ac.jp
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