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FEBS Lett. 2012 Sep 21;586(19):3134-41. doi: 10.1016/j.febslet.2012.08.014. Epub 2012 Aug 19.

Genome-wide biochemical analysis of Arabidopsis protein phosphatase using a wheat cell-free system.

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1
Cell-Free Science and Technology Research Center, Ehime University, Matsuyama, Japan.

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.

PMID:
22968126
DOI:
10.1016/j.febslet.2012.08.014
[Indexed for MEDLINE]
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