R award quantity U01NS041071. The content is solely the responsibility on the authors and will not necessarily represent the official views from the National Institutes of Overall health.AbbreviationsMPTP L-DOPA 5-HT 1-methyl-4-phenyl-1,two,three,6-tetrahydropyridine L-3,4-dihydroxyphenylalanine serotonin
Annals of Botany 114: 1161?175, 2014 doi:ten.1093/aob/mcu035, out there on the net at aob.oxfordjournals.orgPART OF A Specific Situation ON PLANT CELL WALLSArabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.five, a subtilisin-like serine protease??Fabien Senechal1, Lucile Graff2, Ogier Surcouf3, Paulo Marcelo4, Catherine Rayon1, Sophie Bouton1, ?Alain Mareck3, Gregory Mouille5, Annick Stintzi2, Herman Hofte5, Patrice Lerouge3, Andreas Schaller2 ?^ and Jerome Pelloux1,*??EA3900-BIOPI Biologie des Plantes et Innovation, Universite de Picardie, 33 Rue St Leu, F-80039 Amiens, France, 2Universitat ?Hohenheim, Institut fur Physiologie und Biotechnologie der Pflanzen (260), D-70593 Stuttgart, Germany, 3EA4358-Glyco-MEV, ?IFRMP 23, Universite de Rouen, F-76821 Mont-Saint-Aignan, France, 4ICAP, UPJV, 1 ?three Rue des Louvels, F-80037 Amiens, ^ France and 5IJPB, UMR1318 INRA-AgroParisTech, Batiment two, INRA Centre de Versailles-Grignon, Route de St Cyr (RD ten), F-78026 Versailles, France * For correspondence. Email [email protected]: 15 November 2013 Returned for revision: ten January 2014 Accepted: 13 February 2014 Published electronically: 24 MarchBackground and Aims In Arabidopsis thaliana, the degree of methylesterification (DM) of homogalacturonans (HGs), the key pectic constituent with the cell wall, is usually modified by pectin methylesterases (PMEs). In all organisms, two kinds of protein structure have already been reported for PMEs: group 1 and group 2. In group 2 PMEs, the active portion (PME domain, Pfam01095) is preceded by an N-terminal extension (PRO component), which shows similarities to PME inhibitors (PMEI domain, Pfam04043).Formula of 1250997-56-8 This PRO component mediates retention of unprocessed group 2 PMEs in the Golgi apparatus, thus regulating PME activity via a post-translational mechanism.83947-59-5 Order This study investigated the roles of a subtilisin-type serine protease (SBT) in the processing of a PME isoform.PMID:24282960 Solutions Employing a mixture of functional genomics, biochemistry and proteomic approaches, the function of a specific SBT inside the processing of a group two PME was assessed together with its consequences for plant development. Key Outcomes A group 2 PME, AtPME17 (At2g45220), was identified, which was very co-expressed, both spatially and temporally, with AtSBT3.five (At1g32940), a subtilisin-type serine protease (subtilase, SBT), through root improvement. PME activity was modified in roots of knockout mutants for both proteins with consequent effects on root growth. This suggested a part for SBT3.five within the processing of PME17 in planta. Utilizing transient expression in Nicotiana benthamiana, it was indeed shown that SBT3.5 can process PME17 at a distinct single processing motif, releasing a mature isoform in the apoplasm. Conclusions By revealing the potential function of SBT3.5 inside the processing of PME17, this study brings new proof in the complexity in the regulation of PMEs in plants, and highlights the want for identifying precise PME BT pairs. Essential words: Arabidopsis thaliana, co-expression, pectin, pectin methylesterase, PME, subtilase, SBT, post-translational modification, protein processing, gene expression, plant cell walls, subtilisin-like serine protease.
