Abstract
We isolated and characterized a stress-inducible gene, designated as Slti114, encoding matrix metalloproteinase (MMP) in soybean. The derived amino acid sequences of Slti114 show the 69 % homology with MMP2 from Glycine max (AAL27029). The size of the full-length cDNA of Slti114 is 1194 bp with open reading frame comprised of 394 amino acids. RNA expression of Slti114 was induced by low temperature or wounding. During early stage, Slti114 RNA level was extremely high, but Slti114 RNA was not detectable just after cotyledons became yellowish. Green fluorescent protein fusion expression system confirmed that Slti114-smGFP and H+-ATPase-RFP were co-localized to the plasma membrane. Purified glutathione-S-transferase (GST)-Slti114 protein was shown to digest myelin basic protein (MBP) in vitro, but not gelatin. This report provides strong evidence that plasma membrane MMP, Slti114 protein may play a critical role during abiotic stress and senescence in plant.
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Abbreviations
- ECM:
-
extracellular matrix
- smGFP:
-
soluble-modified green fluorescent protein
- GST:
-
glutathione-S-transferase
- MBP:
-
myelin basic protein
- MMP:
-
matrix metalloproteinase
- PCD:
-
programmed cell death
- RFP:
-
red fluorescent protein
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Acknowledgements: This research was partially supported by the grant from the BK21 project and by Dong-A University in Korea. We thank Ms. Hyun-Joo Lim (Medical Sciences Research Institute, Dong-A University) for her technical support on GFP confocal microscopy experiment.
The first two authors equally contributed to the paper.
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Cho, C.W., Chung, E., Kim, K. et al. Plasma membrane localization of soybean matrix metalloproteinase differentially induced by senescence and abiotic stress. Biol Plant 53, 461–467 (2009). https://doi.org/10.1007/s10535-009-0086-z
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DOI: https://doi.org/10.1007/s10535-009-0086-z