TY - JOUR
T1 - The amino acid sequences of two α chains of hemoglobins from Komodo dragon Varanus komodoensis and phylogenetic relationships of amniotes
AU - Fushtiani, Kenzo
AU - Higashiyama, Kayo
AU - Moriyama, Etsuko N.
AU - Imai, Kiyohiro
AU - Hosokawa, Keiichi
PY - 1996/9
Y1 - 1996/9
N2 - To elucidate phylogenetic relationships among amniotes and the evolution of α 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 (α(A), α(D), β(B), and β(C)) were isolated in an equal molar ratio by high performance liquid chromatography from the hemolysate. The amino acid sequences of two α chains were determined. The α(D) chain has a glutamine at E7 as does an α chain of a snake, Liophis miliaris, but the α(A) chain has a histidine at E7 like the majority of hemoglobins. Phylogenetic analyses of 19 globins including two α 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 α globin family, which typically includes the α(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 α globins were possibly produced by duplication of the ancestral α gene before ancestral amniotes diverged, indicating that each of the present amniotes might carry descendants of the two types of α globin genes; (4) squamates first split off from the ancestor of other reptiles and birds.
AB - To elucidate phylogenetic relationships among amniotes and the evolution of α 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 (α(A), α(D), β(B), and β(C)) were isolated in an equal molar ratio by high performance liquid chromatography from the hemolysate. The amino acid sequences of two α chains were determined. The α(D) chain has a glutamine at E7 as does an α chain of a snake, Liophis miliaris, but the α(A) chain has a histidine at E7 like the majority of hemoglobins. Phylogenetic analyses of 19 globins including two α 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 α globin family, which typically includes the α(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 α globins were possibly produced by duplication of the ancestral α gene before ancestral amniotes diverged, indicating that each of the present amniotes might carry descendants of the two types of α globin genes; (4) squamates first split off from the ancestor of other reptiles and birds.
KW - Komodo dragon
KW - amino acid sequence
KW - amniote
KW - hemoglobin
KW - phylogenetic analysis
KW - reptile
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U2 - 10.1093/oxfordjournals.molbev.a025654
DO - 10.1093/oxfordjournals.molbev.a025654
M3 - Article
C2 - 8752011
AN - SCOPUS:0029844788
VL - 13
SP - 1039
EP - 1043
JO - Molecular Biology and Evolution
JF - Molecular Biology and Evolution
SN - 0737-4038
IS - 7
ER -