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  • Title: Genome-wide biochemical analysis of Arabidopsis protein phosphatase using a wheat cell-free system.
    Author: Takahashi H, Ozawa A, Nemoto K, Nozawa A, Seki M, Shinozaki K, Takeda H, Endo Y, Sawasaki T.
    Journal: FEBS Lett; 2012 Sep 21; 586(19):3134-41. PubMed ID: 22968126.
    Abstract:
    Plant genome possesses over 100 protein phosphatase (PPase) genes that are key regulators of signal transduction via phosphorylation/dephosphorylation event. Here we report a comprehensive functional analysis of protein serine/threonine, dual-specificity and tyrosine phosphatases using recombinant PPases produced by wheat cell-free protein synthesis system. Eighty-two recombinant PPases were successfully produced using Arabidopsis full-length cDNA as templates. In vitro PPase assay was performed using phosphorylated myelin basic protein as substrate. Among the AtPPases examined, 26 serine/threonine, three dual-specificity and one tyrosine PPases exhibited catalytic activity, including 20 serine/threonine and one dual-specificity PPases that showed in vitro activities for the first time. Our study demonstrates genome-wide biochemical analysis of AtPPases using wheat cell-free system, and provides new information and insights on enzyme activities.
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