ArticleAnnals of botany2014
Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease.
Article in Annals of botany, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
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Who cites it
47 citing papers in PubMed, 1 synthesis or guideline pooled it, 113 citations in OpenAlex.
- The front line of defence: a meta-analysis of apoplastic proteases in plant immunity.Journal of experimental botany · 2021Pooled it
- Pectin under stress: Pectin methylesterases at the core of cell wall remodeling, integrity sensing, and signaling in plants.Plant communications · 2026Review
- Advances in the functional research of pectin methylesterases in Arabidopsis thaliana.BMC plant biology · 2026Review
- CmbZIP11 regulatesHorticulture research · 2026Article
- Four guidelines to identify bona fide protease-substrate pairs.Journal of experimental botany · 2025Review
- PECTIN METHYLESTERASE51 Affects Stomatal Dimensions, Rosette Area, and Root Length inPlant direct · 2025Article
- Subtilisin-like protease 4 regulates cold tolerance through cell wall modification in rice.Scientific reports · 2025Article
- Kallfu and Wenutram: two Chilean flaxseed varieties with contrasting mucilage production, composition, and structure.Frontiers in plant science · 2025Article
- Proteolysis in plant immunity.The Plant cell · 2024Review
- Pull the fuzes: Processing protein precursors to generate apoplastic danger signals for triggering plant immunity.Plant communications · 2024Review
- Pectin Remodeling and Involvement of AtPME3 in the Parasitic Plant-Plant Interaction,Plants (Basel, Switzerland) · 2024Article
- The proteome of Nicotiana benthamiana is shaped by extensive protein processing.The New phytologist · 2024Article
- Pectin methylesterification state and cell wall mechanical properties contribute to neighbor proximity-induced hypocotyl growth in Arabidopsis.Plant direct · 2024Article
- Subtilases: a major prospect to the genome editing in horticultural crops.Frontiers in plant science · 2024Review
- Auxin as an architect of the pectin matrix.Journal of experimental botany · 2023Review
- Subtilase-mediated biogenesis of the expanded family of SERINE RICH ENDOGENOUS PEPTIDES.Nature plants · 2023Article
- Maintenance of Methyl-Esterified Pectin Level in Pollen Mother-Cell Stages Is Required for Microspore Development.Plants (Basel, Switzerland) · 2023Article
- Genome-Wide Investigation and Co-Expression Network Analysis of SBT Family Gene inInternational journal of molecular sciences · 2023Article
- Genetic architecture of the response ofFrontiers in plant science · 2023Article
- Chromosome groups 5, 6 and 7 harbor major quantitative trait loci controlling root traits in bread wheat (Frontiers in plant science · 2023Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND AND
aimsIn 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.
methodsUsing 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
resultsA 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.
conclusionsBy 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.
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