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Open Access Research article

A membrane-bound matrix-metalloproteinase from Nicotiana tabacum cv. BY-2 is induced by bacterial pathogens

Andreas Schiermeyer1*, Hanna Hartenstein2, Manoj K Mandal2, Burkhard Otte2, Verena Wahner3 and Stefan Schillberg1

Author Affiliations

1 Fraunhofer Institute for Molecular Biology and Applied Ecology (IME), Department Plant Biotechnology, Forckenbeckstrasse 6, 52074 Aachen, Germany

2 RWTH Aachen University, Institute for Molecular Biotechnology, Worringerweg 1, 52074 Aachen, Germany

3 Aachen University for Applied Sciences, Campus Juelich, Ginsterweg 1, 52428 Juelich, Germany

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BMC Plant Biology 2009, 9:83  doi:10.1186/1471-2229-9-83

Published: 29 June 2009

Abstract

Background

Plant 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.

Results

We 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.

Conclusion

Our 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.