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Molecular Evolution of the Substrate Specificity of Chloroplastic Aldolases/Rubisco Lysine Methyltransferases in Plants

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Molecular Plant 2016年第4期9卷 569-581页

作者： Sheng Ma Jacqueline Martin-Laffon Morgane Mininno Oceane Gigarel Sabine Brugiere Olivier Bastien Marianne Tardift stephane ravanel Claude Alban Universite Grenoble Alpes Laboratoire de Physiologie Cellulaire & Vegetale 38041 Grenoble France CNRS UMR5168 38054 Grenoble France CEA iRTSV Laboratoire de Physiologie Cellulaire & Vegetale 38054 Grenoble France INRA USC1359 38054 Grenoble France Universite Grenoble Alpes 38041 Grenoble France CEA iRTSV Biologie & Grande Echelle 38054 Grenoble France INSERM U1038 38054 Grenoble France

Rubisco and fructose-1,6-bisphosphate aldolases （FBAs） are involved in CO2 fixation in chloroplasts. Both enzymes are trimethylated at a specific lysine residue by the chloroplastic protein methyltransferase LSMT. Genes coding LSMT are present in all plant genomes but the methylation status of the substrates varies in a species-specific manner. For example, chloroplastic FBAs are naturally trimethylated in both Pisum sati- vum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former spe- cies. The in vivo methylation status of aldolases and Rubisco matches the catalytic properties of AtLSMT and PsLSMT, which are able to trimethylate FBAs or FBAs and Rubisco, respectively. Here, we created chimera and site-directed mutants of monofunctional AtLSMT and bifunctional PsLSMT to identify the molecular determinants responsible for substrate specificity. Our results indicate that the His-Ala/Pro- Trp triad located in the central part of LSMT enzymes is the key motif to confer the capacity to trimethylate Rubisco. Two of the critical residues are located on a surface loop outside the methyltransferase catalytic site. We observed a strict correlation between the presence of the triad motif and the in vivo methylation status of Rubisco. The distribution of the motif into a phylogenetic tree further suggests that the ancestral function of LSMT was FBA trimethylation. In a recent event during higher plant evolution, this function evolved in ancestors of Fabaceae, Cucurbitaceae, and Rosaceae to include Rubisco as an additional substrate to the archetypal enzyme. Our study provides insight into mechanisms by which SET-domain protein methyltransferases evolve new substrate specificity.

关键词： SET-domain protein methyltransferase site-directed mutagenesis chimeric enzyme methylation,molecular evolution green lineage

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