A phylogenomic profile of globins.
BACKGROUND
Globins occur in all three kingdoms of life: they can be classified into single-domain globins and chimeric globins. The latter comprise the flavohemoglobins with a C-terminal FAD-binding domain and the gene-regulating globin coupled sensors, with variable C-terminal domains. The single-domain globins encompass sequences related to chimeric globins and "truncated" hemoglobins with a 2-over-2 instead of the canonical 3-over-3 alpha-helical fold.


RESULTS
A census of globins in 26 archaeal, 245 bacterial and 49 eukaryote genomes was carried out. Only approximately 25% of archaea have globins, including globin coupled sensors, related single domain globins and 2-over-2 globins. From one to seven globins per genome were found in approximately 65% of the bacterial genomes: the presence and number of globins are positively correlated with genome size. Globins appear to be mostly absent in Bacteroidetes/Chlorobi, Chlamydia, Lactobacillales, Mollicutes, Rickettsiales, Pastorellales and Spirochaetes. Single domain globins occur in metazoans and flavohemoglobins are found in fungi, diplomonads and mycetozoans. Although red algae have single domain globins, including 2-over-2 globins, the green algae and ciliates have only 2-over-2 globins. Plants have symbiotic and nonsymbiotic single domain hemoglobins and 2-over-2 hemoglobins. Over 90% of eukaryotes have globins: the nematode Caenorhabditis has the most putative globins, approximately 33. No globins occur in the parasitic, unicellular eukaryotes such as Encephalitozoon, Entamoeba, Plasmodium and Trypanosoma.


CONCLUSIONS
Although Bacteria have all three types of globins, Archaeado not have flavohemoglobins and Eukaryotes lack globin coupled sensors. Since the hemoglobins in organisms other than animals are enzymes or sensors, it is likely that the evolution of an oxygen transport function accompanied the emergence of multicellular animals.
Vinogradov
Serge N
SN
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, Detroit, MI 48201, USA. svinogra@med.wayne.edu
Hoogewijs
David
D
Bailly
Xavier
X
Arredondo-Peter
Raúl
R
Gough
Julian
J
Dewilde
Sylvia
S
Moens
Luc
L
Vanfleteren
Jacques R
JR
D000595:Amino Acid Sequence; D000818:Animals; D019143:Evolution, Molecular; D019766:Genes, Archaeal; D005798:Genes, Bacterial; D005800:Genes, Fungal; D017238:Genes, Helminth; D017344:Genes, Insect; D017343:Genes, Plant; D016678:Genome; D005914:Globins / Q000145:classification / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D054793:Truncated Hemoglobins; D014714:Vertebrates / Q000235:genetics
D054793:Truncated Hemoglobins; D005914:Globins