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

Autor: Océane Gigarel, Sabine Brugière, Jacqueline Martin-Laffon, Marianne Tardif, Morgane Mininno, Stéphane Ravanel, Claude Alban, Sheng Ma, Olivier Bastien
Přispěvatelé: Laboratoire de Physiologie Cellulaire & Végétale [Grenoble] (UGA), Université Grenoble Alpes (UGA), Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Biologie à Grande Échelle (BGE - UMR S1038), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), This work was supported by the Department of Plant Biology and Breeding from the French National Institute for Agricultural Research (AAP BAP2013 INRA_Calvin Cycle-Me) and by the Proteomics French Infrastructure (ANR-10-INBS-08-01)., ANR-10-INBS-08-01/10-INBS-0008,ProFI,Infrastructure Française de Protéomique(2010), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), French National Institute for Agricultural Research (AAP BAP2013 INRA_Calvin Cycle-Me), Physiologie cellulaire et végétale (LPCV), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), ANR-10-INBS-0008,ProFI,Infrastructure Française de Protéomique(2010), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])
Jazyk: angličtina
Rok vydání: 2016
Předmět:
0301 basic medicine
Models
Molecular
Methyltransferase
Chloroplasts
Arabidopsis thaliana
Protein subunit
Ribulose-Bisphosphate Carboxylase
[SDV]Life Sciences [q-bio]
Protein domain
Amino Acid Motifs
Plant Science
Biology
Substrate Specificity
Evolution
Molecular
03 medical and health sciences
Protein Domains
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Amino Acid Sequence
SET-domain protein methyltransferase
green lineage
Site-directed mutagenesis
Rosaceae
Molecular Biology
ComputingMilieux_MISCELLANEOUS
Pisum sativum
Aldehyde-Lyases
Genetics
molecular evolution
chimeric enzyme
Chlamydomonas rheinhardtii
RuBisCO
Carbon fixation
fungi
food and beverages
Fabaceae
Plant
Methylation
Chloroplast
Cucurbitaceae
030104 developmental biology
Biochemistry
biology.protein
Mutagenesis
Site-Directed
methylation
site-directed mutagenesis
Site directed mutagenesis
Zdroj: Molecular Plant
Molecular Plant, Cell Press/Oxford UP, 2016, 9 (4), pp.569-581. ⟨10.1016/j.molp.2016.01.003⟩
Molecular Plant, Cell Press/Oxford UP, 2016
Molecular Plant, 2016, 9 (4), pp.569-581. ⟨10.1016/j.molp.2016.01.003⟩
ISSN: 1674-2052
1752-9867
DOI: 10.1016/j.molp.2016.01.003⟩
Popis: International audience; 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 sativum and Arabidopsis thaliana, whereas the Rubisco large subunit is trimethylated only in the former species. 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.
Databáze: OpenAIRE
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