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A gene fusion event in the evolution of aminoacyl‐tRNA synthetases
Author(s) -
Berthonneau Eric,
Mirande Marc
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01343-0
Subject(s) - biology , gene , genetics , phylogenetic tree , transfer rna , aminoacyl trna synthetase , amino acyl trna synthetases , biochemistry , rna
The genes of glutamyl‐ and prolyl‐tRNA synthetases (GluRS and ProRS) are organized differently in the three kingdoms of the tree of life. In bacteria and archaea, distinct genes encode the two proteins. In several organisms from the eukaryotic phylum of coelomate metazoans, the two polypeptides are carried by a single polypeptide chain to form a bifunctional protein. The linker region is made of imperfectly repeated units also recovered as singular or plural elements connected as N‐terminal or C‐terminal polypeptide extensions in various eukaryotic aminoacyl‐tRNA synthetases. Phylogenetic analysis points to the monophyletic origin of this polypeptide motif appended to six different members of the synthetase family, belonging to either of the two classes of aminoacyl‐tRNA synthetases. In particular, the monospecific GluRS and ProRS from Caenorhabditis elegans , an acoelomate metazoan, exhibit this recurrent motif as a C‐terminal or N‐terminal appendage, respectively. Our analysis of the extant motifs suggests a possible series of events responsible for a gene fusion that gave rise to the bifunctional glutamyl‐prolyl‐tRNA synthetase through recombination between genomic sequences encoding the repeated units.