Genome-wide biochemical analysis of Arabidopsis protein phosphatase using a wheat cell-free system
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- 作者：Hirotaka Takahashi ; Akihiko Ozawa ; Keiichirou Nemoto ; Akira Nozawa ; Motoaki Seki ; Kazuo Shinozaki ; Hiroyuki Takeda ; Yaeta Endo ; Tatsuya Sawasaki
- 关键词：PPase ; protein phosphatase ; Tyr ; tyrosine ; Ser ; serine ; Thr ; threonine ; PPPs ; serine/threonine-specific protein phosphatases ; PPMs ; metal ion-dependent phosphoprotein phosphatases ; PTPs ; tyrosine-specific phosphatases ; DSPs ; dual-specificity phosphatases
- 刊名：FEBS Letters
- 出版年：2012
- 出版时间：21 September, 2012
- 年：2012
- 卷：586
- 期：19
- 页码：3134-3141
- 全文大小：1207 K
文摘
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.
Structured summary of protein interactions
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