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Fig. 10 | BMC Plant Biology

Fig. 10

From: Tomato Sl3-MMP, a member of the Matrix metalloproteinase family, is required for disease resistance against Botrytis cinerea and Pseudomonas syringae pv. tomato DC3000

Fig. 10

Mature Sl3-MMP protein had proteolytic activity with different cleavage site specificity. a Purification of recombinant Sl3-MMPm. M, marker for protein molecular weight; lane 1, total cell proteins from non-induced bacteria carrying pGEX-Sl3-MMPm; lane 2, total cell protein from induced bacteria carrying pGEX-Sl3-MMPm; lane 3, purified protein from non-induced bacteria carrying pGEX-Sl3-MMPm; lane 4, purified Sl3-MMP protein. b Proteolytic activity of Sl3-MMPm on MBP in the absence (-) or presence (+) of 1 mM EDTA. Reactions with different component combinations were incubated with 5 μg of MBP at 37 °C and the products were resolved by 16 % SDS-PAGE. Lane 1, a negative control containing MBP only; Lane 2, a negative control with GST tag; Lane 3, a reaction containing Sl3-MMPm and 1 mM EDTA; lane 4, a reaction containing Sl3-MMPm. * indicates the product degraded from MBP by Sl3-MMPm. c Cleavage site specificity of Sl3-MMPm on synthetic quenched peptide substrates. Enzymatic activity of Sl3-MMPm on synthetic quenched peptides QF24, QF35 and QF75 was measured as relative fluorescence in arbitrary units over 90 min at 1 min intervals. Values are the means of triplicate measurements

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