Periodic recurrence of methionines: fossil of gene fusion?
As we have recently shown, approximately 20% of proteins are made of uniform size units of approximately 123 aa for eukaryotes and approximately 152 aa for prokaryotes. Such regularity may reflect certain past events in protein evolution by fusion (molecular recombination) of a spectrum of standard-size protein-coding DNA segments--the early genes. Consequently, methionines, as start residues, would mark those locations in proteins that correspond to the DNA recombination sites--the borders between the fused genes. This positional preference of the methionines may still survive as a fossil of the early protein sequence organization. In this study we address the question how methionines are distributed in modern protein sequences. This analysis of eukaryotic sequences shows that methionine residues do preferentially appear at the positions corresponding to the multiples of the unit size, as predicted.
Kolker
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Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Trifonov
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EN
D005075:Biological Evolution; D005057:Eukaryotic Cells; D015321:Gene Rearrangement / Q000235:genetics*; D008715:Methionine / Q000235:genetics*; D008957:Models, Genetic; D008970:Molecular Weight; D011506:Proteins / Q000235:genetics*; D013997:Time Factors
D011506:Proteins; D008715:Methionine