ArticleBMC plant biology2009
A membrane-bound matrix-metalloproteinase from Nicotiana tabacum cv. BY-2 is induced by bacterial pathogens.
Article in BMC plant biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it.
- The front line of defence: a meta-analysis of apoplastic proteases in plant immunity.Journal of experimental botany · 2021Pooled it
- Transcriptome analyses revealPhysiology and molecular biology of plants : an international journal of functional plant biology · 2025Article
- Regulated cleavage and translocation of FERONIA control immunity in Arabidopsis roots.Nature plants · 2024Article
- A novel rubber tree PR-10 protein involved in host-defense response against the white root rot fungus Rigidoporus microporus.BMC plant biology · 2023Article
- Regulation of Arabidopsis Matrix Metalloproteinases by Mitogen-Activated Protein Kinases and Their Function in Leaf Senescence.Frontiers in plant science · 2022Article
- Loss of Arabidopsis matrix metalloproteinase-5 affects root development and root bacterial communities during drought stress.Physiologia plantarum · 2021Article
- Rice matrix metalloproteinase OsMMP1 plays pleiotropic roles in plant development and symplastic-apoplastic transport by modulating cellulose and callose depositions.Scientific reports · 2018Article
- Matrix metalloproteinases operate redundantly in Arabidopsis immunity against necrotrophic and biotrophic fungal pathogens.PloS one · 2017Article
- Cell Death Control by Matrix Metalloproteinases.Plant physiology · 2016Article
- Tomato Sl3-MMP, a member of the Matrix metalloproteinase family, is required for disease resistance against Botrytis cinerea and Pseudomonas syringae pv. tomato DC3000.BMC plant biology · 2015Article
- Extracellular peptidase hunting for improvement of protein production in plant cells and roots.Frontiers in plant science · 2015Article
- Genomic evaluation of oxalate-degrading transgenic soybean in response to Sclerotinia sclerotiorum infection.Molecular plant pathology · 2014Article
- Identification, gene cloning and expression of serine proteases in the extracellular medium of Nicotiana tabacum cells.Plant cell reports · 2012Article
- Development of an optimized tetracycline-inducible expression system to increase the accumulation of interleukin-10 in tobacco BY-2 suspension cells.BMC biotechnology · 2012Article
- Antibody degradation in tobacco plants: a predominantly apoplastic process.BMC biotechnology · 2011Article
- The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases.Molecular microbiology · 2011Article
- Biochemical properties of the matrix metalloproteinase NtMMP1 from Nicotiana tabacum cv. BY-2 suspension cells.Planta · 2010Article
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Authors and funding
6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
backgroundPlant matrix metalloproteinases (MMP) are conserved proteolytic enzymes found in a wide range of monocotyledonous and dicotyledonous plant species. Acting on the plant extracellular matrix, they play crucial roles in many aspects of plant physiology including growth, development and the response to stresses such as pathogen attack.
resultsWe have identified the first tobacco MMP, designated NtMMP1, and have isolated the corresponding cDNA sequence from the tobacco suspension cell line BY-2. The overall domain structure of NtMMP1 is similar to known MMP sequences, although certain features suggest it may be constitutively active rather than dependent on proteolytic processing. The protein appears to be expressed in two forms with different molecular masses, both of which are enzymatically active as determined by casein zymography. Exchanging the catalytic domain of NtMMP1 with green fluorescent protein (GFP) facilitated subcellular localization by confocal laser scanning microscopy, showing the protein is normally inserted into the plasma membrane. The NtMMP1 gene is expressed constitutively at a low level but can be induced by exposure to bacterial pathogens.
conclusionOur biochemical analysis of NtMMP1 together with bioinformatic data on the primary sequence indicate that NtMMP1 is a constitutively-active protease. Given its induction in response to bacterial pathogens and its localization in the plasma membrane, we propose a role in pathogen defense at the cell periphery.
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