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MBE Advance Access published online on September 8, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh258
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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Accepted April 6, 2004

Research Article

A Globin Gene of Ancient Evolutionary Origin in Lower Vertebrates: Evidence for Two Distinct Globin Families in Animals

Anja Roesner 1, Christine Fuchs 2, Thomas Hankeln 2, and Thorsten Burmester 1*

1 Institute of Zoology, Johannes Gutenberg University, D-55099 Mainz, Germany
2 Institute of Molecular Genetics, Johannes-Gutenberg-University, D-55099 Mainz, Germany

* To whom correspondence should be addressed. E-mail: burmeste{at}uni-mainz.de.


  Abstract

Hemoglobin, myoglobin, neuroglobin and cytoglobin are four types of vertebrate globins with distinct tissue-distributions and functions. Here we report the identification of a fifth and novel globin gene from fish and amphibians, which has apparently been lost in the evolution of higher vertebrates (Amniota). Because its function is presently unknown, we tentatively call it globin X (GbX). Globin X sequences were obtained from three fish species, the zebrafish Danio rerio, the goldfish Carassius auratus and the pufferfish Tetraodon nigroviridis, and the clawed frog Silurana tropicalis. Globin X sequences are distinct from vertebrate hemoglobins, myoglobins, neuroglobins and cytoglobins. Globin X displays the highest identity scores with neuroglobin (~26 to 35%), although it is not a neuronal protein, as revealed by RT-PCR experiments on goldfish RNA from various tissues. The distal ligand-binding and the proximal heme-binding histidines (E7 and F8), as well as the conserved phenylalanine CD1 are present in the globin X sequences, but due to extensions at the N- and C-termini the globin X proteins are longer than the typical 8-alpha helical globins and comprise about 200 amino acids. In addition to the conserved globin-introns at helix positions B12.2 and G7.0, the globin X genes contain two introns in E10.2 and H10.0. The intron in E10.2 is shifted by one bp in respect to the vertebrate neuroglobin gene (E11.0), providing possible evidence for an intron sliding event. Phylogenetic analyses confirm an ancient evolutionary relationship of globin X with neuroglobin and suggest the existence of two distinct globin types in the last common ancestor of Protostomia and Deuterostomia.

Keywords: globin; hemoglobin; neuroglobin; gene duplication; intron sliding.
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