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Family-wide characterization of Matrix Metallo-proteinases from Arabidopsis thaliana reveals their distinct proteolytic activity and cleavage site specificity.
Umeå University, Faculty of Science and Technology, Department of Chemistry. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
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2014 (English)In: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 457, no 2, 335-346 p.Article in journal (Refereed) Published
Abstract [en]

Matrix metalloproteases (MMPs) are a family of zinc-dependent endopeptidases widely distributed throughout all kingdoms of life. In mammals, MMPs play key roles in many physiological and pathological processes including remodeling of the extracellular matrix. In the genome of the annual plant Arabidopsis thaliana five MMP-like proteins (At-MMPs) are encoded, but their function is unknown. Previous work on these enzymes was limited to gene expression analysis, and so far proteolytic activity has been shown only for At1-MMP. We expressed and purified the catalytic domains of all five At-MMPs as His-tagged proteins in E.coli to delineate the biochemical differences and similarities among the Arabidopsis MMP family members. We demonstrate that all five recombinant At-MMPs are active proteases with distinct preferences for different protease substrates. Furthermore, we performed a family-wide characterization of their biochemical properties and highlight similarities and differences in their cleavage site specificities as well as pH- and temperature dependent activities. Detailed analysis of their sequence specificity using Proteomic Identification of protease Cleavage Sites (PICS) revealed profiles similar to human MMPs with the exception of At5-MMP; homology models of the At-MMP catalytic domains supported these results. Our results suggest that each At-MMP may be involved in different proteolytic processes during plant growth and development.

Place, publisher, year, edition, pages
Biochemical Journal , 2014. Vol. 457, no 2, 335-346 p.
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:umu:diva-82582DOI: 10.1042/BJ20130196ISI: 000333718000009PubMedID: 24156403OAI: diva2:661976
Available from: 2013-11-05 Created: 2013-11-05 Last updated: 2014-05-07Bibliographically approved

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Marino, GiadaSchröder, Wolfgang PFunk, Christiane
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Department of ChemistryUmeå Plant Science Centre (UPSC)
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