The nucleotide sequence of the mRNA encoding a tadpole beta-globin polypeptide of Xenopus laevis.
We have determined the nucleotide sequence of a cloned cDNA derived from the mRNA encoding an abundant Xenopus laevis tadpole beta-globin polypeptide. The cloned sequence contains the entire coding region of the mRNA as well as most of its 5'- and 3' -noncoding regions. The complete amino acid sequence of the protein has been deduced. Comparison of this sequence with that of the major adult beta-globin polypeptide of X. laevis shows that the two gene products are highly diverged from each other, the tadpole sequence actually displaying a somewhat greater homology to the human beta-like globin sequences than to the adult frog sequence. An unusual feature of the predicted tadpole beta-globin polypeptide is the presence of a phenylalanine residue at its carboxyl terminus. All known amphibian, avian, and mammalian beta-globin polypeptides have a COOH-terminal histidine residue, and this amino acid is known to play a major role in the alkaline Bohr effect. This observation suggests that, as has been found for two fish hemoglobins which also have a COOH-terminal phenylalanine residue, the tadpole hemoglobin of X. laevis will display a much reduced alkaline Bohr effect.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000032:analysis*; D005914:Globins / Q000235:genetics*; D006801:Humans; D007814:Larva; D012333:RNA, Messenger / Q000235:genetics*; D011898:Ranidae; D013045:Species Specificity; D014981:Xenopus
D012333:RNA, Messenger; D005914:Globins; D004247:DNA