We have recently identified an Arabidopsis thaliana cDNA encoding a putative protein Ser/Thr phosphatase PP7, not closely related to any protein phosphatases in animals or fungi. Here, we describe the characterization of PP7 expressed in a bacterial system. The recombinant protein was inactive unless the longest insert in its catalytic domain was cleaved, suggesting that this insert is an autoinhibitory region. PP7 was resistant to okadaic acid, calyculin and fumonisin B1, and was stimulated by Mn2+ or Fe2+, while Ni2+ and Zn2+ were inhibitory. Polylysine stimulated PP7 activity towards p-nitrophenylphosphate but inhibited activity towards the most efficient protein substrate, myelin basic protein. A tentative model of the control of PP7 activity is proposed.
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