Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships

Using a new template based on an alignment of 145 nonvertebrate globins we examined several recently determined sequences of putative globins and globin-like hemeproteins. We propose that all globins have evolved from a family of ancestral, approx. 17-kDa hemeproteins, which displayed the globin fol...

Full description

Saved in:
Bibliographic Details
Published in:Molecular biology and evolution 1996-02, Vol.13 (2), p.324-333
Main Authors: Moens, L, Vanfleteren, J, Van de Peer, Y, Peeters, K, Kapp, O, Czeluzniak, J, Goodman, M, Blaxter, M, Vinogradov, S
Format: Article
Language:English
Subjects:
Alcaligenes
Amino Acid Sequence
Animals
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Candida
Chlamydomonas
Escherichia
Evolution, Molecular
Fungal Proteins - chemistry
Fungal Proteins - genetics
Gene Transfer, Horizontal
Globins - chemistry
Globins - genetics
Globins - metabolism
Hemeproteins - genetics
Molecular Sequence Data
Origin of Life
Oxidation-Reduction
Oxygen - metabolism
Paramecium
Saccharomyces
Sequence Alignment
Space life sciences
Species Specificity
Structure-Activity Relationship
Templates, Genetic
Tetrahymena
Vitreoscilla
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Using a new template based on an alignment of 145 nonvertebrate globins we examined several recently determined sequences of putative globins and globin-like hemeproteins. We propose that all globins have evolved from a family of ancestral, approx. 17-kDa hemeproteins, which displayed the globin fold and functioned as redox proteins. Once atmospheric O2 became available the acquisition of oxygen-binding properties was initiated, culminating in the various highly specialized functions known as present. During this evolutionary process, we suggest that (1) high oxygen affinity may have been acquired repeatedly and (2) the formation of chimeric proteins containing both a globin and a flavin binding domain was an additional and distinct evolutionary trend. Furthermore, globin-like hemeproteins encompass hemeproteins produced through convergent evolution from nonglobin ancestral proteins to carry out O2-binding functions as well as hemeproteins whose sequences exhibit the loss of some or all of the structural determinants of the globin fold. We also propose that there occurred two cases of horizontal globin gene transfer, one from an ancestor common to the ciliates Paramecium and Tetrahymena and the green alga Chlamydomonas to a cyanobacterium ancestor and the other, from a eukaryote ancestor of the yeasts Saccharomyces and Candida to a bacterial ancestor of the proteobacterial genera Escherichia, Alcaligenes, and Vitreoscilla.
ISSN:0737-4038
1537-1719
DOI:10.1093/oxfordjournals.molbev.a025592