Table of Contents
International Journal of Evolutionary Biology
Volume 2012, Article ID 843167, 8 pages
http://dx.doi.org/10.1155/2012/843167
Research Article

Where Do Phosphosites Come from and Where Do They Go after Gene Duplication?

Département de Biologie, PROTEO and Institut de Biologie Intégrative et des Systèmes, Université Laval, Pavillon Charles-Eugène-Marchand, 1030, Avenue de la Médecine, Québec, QC, Canada G1V 0A6

Received 21 March 2012; Accepted 3 May 2012

Academic Editor: Frédéric Brunet

Copyright © 2012 Guillaume Diss et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Gene duplication followed by divergence is an important mechanism that leads to molecular innovation. Divergence of paralogous genes can be achieved at functional and regulatory levels. Whereas regulatory divergence at the transcriptional level is well documented, little is known about divergence of posttranslational modifications (PTMs). Protein phosphorylation, one of the most important PTMs, has recently been shown to be an important determinant of the retention of paralogous genes. Here we test whether gains and losses of phosphorylated amino acids after gene duplication may specifically modify the regulation of these duplicated proteins. We show that when phosphosites are lost in one paralog, transitions from phosphorylated serines and threonines are significantly biased toward negatively charged amino acids, which can mimic their phosphorylated status in a constitutive manner. Our analyses support the hypothesis that divergence between paralogs can be generated by a loss of the posttranslational regulatory control on a function rather than by the complete loss of the function itself. Surprisingly, these favoured transitions cannot be reached by single mutational steps, which suggests that the function of a phosphosite needs to be completely abolished before it is restored through substitution by these phosphomimetic residues. We conclude by discussing how gene duplication could facilitate the transitions between phosphorylated and phosphomimetic amino acids.