Phylogenetic analysis of invertebrate lysozymes and the evolution of lysozyme function.
We isolated and sequenced the cDNAs coding for lysozymes of six bivalve species. Alignment and phylogenetic analysis showed that, together with recently described bivalve lysozymes, the leech destabilase, and a number of putative proteins from extensive genomic and cDNA analyses, they belong to the invertebrate type of lysozymes (i type), first described by Jollès and Jollès (1975). We determined the genomic structure of the gene encoding the lysozyme of Mytilus edulis, the common mussel. We provide evidence that the central exon of this gene is homologous to the second exon of the chicken lysozyme gene, belonging to the c type. We propose that the origin of this domain can be traced back in evolution to the origin of bilaterian animals. Phylogenetic analysis suggests that i-type proteins form a monophyletic family.
Bachali
Sana
S
UMR 7622, "Biologie du Développement," CNRS et Université P. et M. Curie, Paris, France.
Jager
Muriel
M
Hassanin
Alexandre
A
Schoentgen
Françoise
F
Jollès
Pierre
P
Fiala-Medioni
Aline
A
Deutsch
Jean S
JS
D000595:Amino Acid Sequence; D000818:Animals; D018076:DNA, Complementary; D019143:Evolution, Molecular; D007448:Invertebrates / Q000235:genetics*; D007768:Lactalbumin / Q000235:genetics; D008969:Molecular Sequence Data; D009113:Muramidase / Q000502:physiology*; D010802:Phylogeny; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D007768:Lactalbumin; D009113:Muramidase