Protein-Protein Interactions of Tandem Affinity Purified Protein Kinases from Rice

被引：30

作者：

Rohila, Jai S.

Chen, Mei

Chen, Shuo

Chen, Johann

Cerny, Ronald L.

Dardick, Christopher

Canlas, Patrick

Fujii, Hiroaki

Gribskov, Michael

Kanrar, Siddhartha

Knoflicek, Lucas

Stevenson, Becky

Xie, Mingtang

Xu, Xia

Zheng, Xianwu

Zhu, Jian-Kang

Ronald, Pamela

Fromm, Michael E.

机构：

[1] Plant Science Initiative, University of Nebraska, Lincoln, NE

[2] Department of Chemistry, University of Nebraska, Lincoln, NE

[3] Department of Plant Pathology, University of California Davis, Davis,CA

[4] Department of Biological Sciences, Purdue University, West Lafayette, IN

[5] Department of Botany and Plant Sciences, University of California, Riverside, Riverside, CA

[6] Department of Biology and Microbiology, South Dakota State University, Brookings, SD

[7] Appalachian Fruit Research Station, USDA-ARS, Kearneysville, WV

来源：

PLOS ONE | 2009年 / 4卷 / 08期

关键词：

D O I：

10.1371/journal.pone.0006685

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Eighty-eight rice (Oryza sativa) cDNAs encoding rice leaf expressed protein kinases (PKs) were fused to a Tandem Affinity Purification tag (TAP-tag) and expressed in transgenic rice plants. The TAP-tagged PKs and interacting proteins were purified from the T1 progeny of the transgenic rice plants and identified by tandem mass spectrometry. Forty-five TAP-tagged PKs were recovered in this study and thirteen of these were found to interact with other rice proteins with a high probability score. In vivo phosphorylated sites were found for three of the PKs. A comparison of the TAP-tagged data from a combined analysis of 129 TAP-tagged rice protein kinases with a concurrent screen using yeast two hybrid methods identified an evolutionarily new rice protein that interacts with the well conserved cell division cycle 2 (CDC2) protein complex.

引用

页数：8

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