MBE Advance Access published online on February 12, 2004
Molecular Biology and Evolution, doi:10.1093/molbev/msh082
Molecular Biology and Evolution © Society for Molecular Biology and Evolution 2004; all rights reserved
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1 Laboratoire de Génétique et Développement des Mammifères, Institut Jacques Monod, 2, place Jussieu, 75251 Paris, Cedex 05, France
* To whom correspondence should be addressed. E-mail: houzelstein{at}ijm.jussieu.fr.
Galectins form a family of structurally related carbohydrate binding proteins (lectins) that have been identified in a large variety of metazoan phyla. They are involved in many biological processes such as morphogenesis, control of cell death, immunological response and cancer. To elucidate the evolutionary history of galectins and galectin-like proteins in chordates, we have exploited three independent lines of evidence: (i) location of galectin encoding genes (LGALS) in the human genome; (ii) exon-intron organisation of galectin encoding genes; and (iii) sequence comparison of carbohydrate recognition domains (CRDs) of chordate galectins. Our results suggest that a duplication of a mono-CRD galectin gene gave rise to an original bi-CRD galectin gene, before or early in chordate evolution. The N-terminal and C-terminal CRDs of this original galectin subsequently diverged into two different subtypes, defined by exon-intron structure (F4-CRD and F3-CRD). We show that all vertebrate mono-CRD galectins known to date belong to either the F3- or F4-subtype. A sequence of duplication and divergence events of the different galectins in chordates is proposed. Key Words:
galectin, Lgals, vertebrate, chordate, evolution
© 2004 Society for Molecular Biology and Evolution
Original Articles
Phylogenetic Analysis of the Vertebrate Galectin Family
2 Laboratoire de Structure et dynamique des Génomes, Institut Jacques Monod, 2, place Jussieu, 75251 Paris, Cedex 05, France
3 Department of Biochemistry, Glycobiology Institute, University of Oxford, South Parks Road, Oxford 0X1 3QU, United Kingdom
4 Departments of Psychiatry and Anatomy, University of California, San Francisco, LPPI, Box F-0984, 401 Parnassus Ave., San Francisco, CA 94143-0984, USA
5 Department of Bioorganic Chemistry, Lund University, Lund SE-22100, Sweden
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