ArticleThe Biochemical journal2003
Ara12 subtilisin-like protease from Arabidopsis thaliana: purification, substrate specificity and tissue localization.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 68 citations in OpenAlex.
- Clathrin-Mediated Endocytosis Delivers Proteolytically Active Phytaspases Into Plant Cells.Frontiers in plant science · 2019Article
- Subtilisin-like proteases in plant defence: the past, the present and beyond.Molecular plant pathology · 2018Review
- Genetic mapping of anthocyanin accumulation-related genes in pepper fruits using a combination of SLAF-seq and BSA.PloS one · 2018Article
- A Novel Function for Arabidopsis CYCLASE1 in Programmed Cell Death Revealed by Isobaric Tags for Relative and Absolute Quantitation (iTRAQ) Analysis of Extracellular Matrix Proteins.Molecular & cellular proteomics : MCP · 2015Article
- Extracellular peptidase hunting for improvement of protein production in plant cells and roots.Frontiers in plant science · 2015Article
- Genome-wide and molecular evolution analysis of the subtilase gene family in Vitis vinifera.BMC genomics · 2014Article
- Arabidopsis PECTIN METHYLESTERASE17 is co-expressed with and processed by SBT3.5, a subtilisin-like serine protease.Annals of botany · 2014Article
- Flying saucer1 is a transmembrane RING E3 ubiquitin ligase that regulates the degree of pectin methylesterification in Arabidopsis seed mucilage.The Plant cell · 2013Article
- Horizontal transfer of a subtilisin gene from plants into an ancestor of the plant pathogenic fungal genus Colletotrichum.PloS one · 2013Article
- Identification, gene cloning and expression of serine proteases in the extracellular medium of Nicotiana tabacum cells.Plant cell reports · 2012Article
- Border sequences of Medicago truncatula CLE36 are specifically cleaved by endoproteases common to the extracellular fluids of Medicago and soybean.Journal of experimental botany · 2011Article
- Functional analysis of the cucumisin propeptide as a potent inhibitor of its mature enzyme.The Journal of biological chemistry · 2010Article
- Article
- The protease-associated domain and C-terminal extension are required for zymogen processing, sorting within the secretory pathway, and activity of tomato subtilase 3 (SlSBT3).The Journal of biological chemistry · 2009Article
- Diversity of serine hydrolase activities of unchallenged and botrytis-infected Arabidopsis thaliana.Molecular & cellular proteomics : MCP · 2009Article
- Plants can use protein as a nitrogen source without assistance from other organisms.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- The two main endoproteases present in dark-induced senescent wheat leaves are distinct subtilisin-like proteases.Planta · 2006Article
- Inferring hypotheses on functional relationships of genes: Analysis of the Arabidopsis thaliana subtilase gene family.PLoS computational biology · 2005Article
- Review
- Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa.The Plant cell · 2004Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A C-terminal portion of Ara12 subtilisin-like protease (residues 542-757) was expressed in Escherichia coli cells as a fusion protein bound to maltose binding protein. Polyclonal antisera raised against the expressed protein were used to examine the tissue specificity and subcellular localization of Ara12. The protease was found predominantly in the silique and stem of plants, but was hardly detectable in leaf and not seen in root tissue. The distribution observed using immunological techniques is different from that seen by an RNA analysis study, which demonstrated similar mRNA abundance in the stem and leaves. Using immunogold labelling, Ara12 was shown to have an extracellular localization and was found in the intercellular spaces in stem tissue. Ara12 protease was purified to homogeneity from Arabidopsis thaliana cell suspension cultures by anion exchange and hydrophobic interaction chromatography. Proteolytic activity of Ara12 was inhibited by a number of serine protease inhibitors, but was almost unaffected by inhibitors of other catalytic classes of proteases. Optimal proteolytic activity was displayed under acidic conditions (pH 5.0). Ara12 activity was relatively thermostable and was stimulated in the presence of Ca2+ ions. Substrate specificity studies were conducted using a series of internally quenched fluorogenic peptide substrates. At the P1 position of substrates, hydrophobic residues, such as Phe and Ala, were preferred to Arg, whilst at the P1' position, Asp, Leu and Ala were most favoured. Possible functions of Ara12 are discussed in the light of the involvement of a number of plant subtilisin-like proteases in morphogenesis.
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