The insertion of palindromic repeats in the evolution of proteins.
The current theory of protein evolution is that all contemporary proteins are derived from an ancestral subset. However, each new sequenced genome exhibits many genes with no detectable homologues in other species, leading to the paradoxical picture of a universal ancestor with more genes than any of its progeny. Standard explanations indicate that fast evolving genes might disappear into the 'twilight zone' of sequence similarity. Regardless of the size of the original ancestral subset, its origin and the potential mechanisms of its subsequent enlargement are rarely addressed. Sequencing of Rickettsia conorii genome recently led to the discovery of three families of repeat-mobile elements frequently inserted into the middle of protein coding genes. Although not yet identified in other species of bacteria, this discovery has provided the first clear evidence for the de novo creation of long protein segments (up to 50 amino acid residues) by repeat insertion. Based on previous results and theories on the coding potential of palindromic elements, we speculate that their insertion and mobility might have played a significant role in the early stages of protein evolution.
Claverie
Jean-Michel
JM
Information Génétique et Structurale, CNRS-AVENTIS UMR 1889, Institut de Biologie Structurale et Microbiologie, Marseille, France. jean-michel.claverie@igs.cnrs-mrs.fr
Ogata
Hiroyuki
H
D000595:Amino Acid Sequence; D001483:Base Sequence; D004247:DNA / Q000235:genetics*; D019143:Evolution, Molecular; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016366:Open Reading Frames / Q000235:genetics; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000235:genetics*; D012091:Repetitive Sequences, Nucleic Acid; D020114:Rickettsia conorii / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D011506:Proteins; D004247:DNA