RRC ID 52882
Author Sénéchal F, Graff L, Surcouf O, Marcelo P, Rayon C, Bouton S, Mareck A, Mouille G, Stintzi A, Höfte H, Lerouge P, Schaller A, Pelloux J.
Title Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease.
Journal Ann Bot
Abstract BACKGROUND AND AIMS:In Arabidopsis thaliana, the degree of methylesterification (DM) of homogalacturonans (HGs), the main pectic constituent of the cell wall, can be modified by pectin methylesterases (PMEs). In all organisms, two types of protein structure have been reported for PMEs: group 1 and group 2. In group 2 PMEs, the active part (PME domain, Pfam01095) is preceded by an N-terminal extension (PRO part), which shows similarities to PME inhibitors (PMEI domain, Pfam04043). This PRO part mediates retention of unprocessed group 2 PMEs in the Golgi apparatus, thus regulating PME activity through a post-translational mechanism. This study investigated the roles of a subtilisin-type serine protease (SBT) in the processing of a PME isoform.
METHODS:Using a combination of functional genomics, biochemistry and proteomic approaches, the role of a specific SBT in the processing of a group 2 PME was assessed together with its consequences for plant development.
KEY RESULTS:A group 2 PME, AtPME17 (At2g45220), was identified, which was highly co-expressed, both spatially and temporally, with AtSBT3.5 (At1g32940), a subtilisin-type serine protease (subtilase, SBT), during root development. PME activity was modified in roots of knockout mutants for both proteins with consequent effects on root growth. This suggested a role for SBT3.5 in the processing of PME17 in planta. Using transient expression in Nicotiana benthamiana, it was indeed shown that SBT3.5 can process PME17 at a specific single processing motif, releasing a mature isoform in the apoplasm.
CONCLUSIONS:By revealing the potential role of SBT3.5 in the processing of PME17, this study brings new evidence of the complexity of the regulation of PMEs in plants, and highlights the need for identifying specific PME-SBT pairs.
Volume 114(6)
Pages 1161-75
Published 2014-10-1
DOI 10.1093/aob/mcu035
PII mcu035
PMID 24665109
PMC PMC4195543
MeSH Amino Acid Sequence Arabidopsis / enzymology* Arabidopsis / genetics Arabidopsis Proteins / genetics* Arabidopsis Proteins / metabolism Carboxylic Ester Hydrolases / genetics* Carboxylic Ester Hydrolases / metabolism Cell Wall / metabolism Gene Expression Regulation, Plant* Gene Knockout Techniques Isoenzymes Molecular Sequence Data Mutation Organ Specificity Pectins / metabolism Plants, Genetically Modified Promoter Regions, Genetic Protein Processing, Post-Translational* Proteomics Recombinant Fusion Proteins Seedlings / enzymology Seedlings / genetics Subtilisins / genetics* Subtilisins / metabolism Tobacco / enzymology Tobacco / genetics
IF 4.005
Times Cited 31
Arabidopsis / Cultured plant cells, genes pda01681