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

Authors

Jai S. Rohila, University of Nebraska-LincolnFollow
Mei Chen, University of Nebraska-LincolnFollow
Shuo Chen, University of Nebraska-Lincoln
Johann Chen, University of California Davis
Ronald L. Cerny, University of Nebraska-LincolnFollow
Christopher Dardick, University of California Davis
Patrick Canlas, University of California Davis
Hiroaki Fujii, University of California Riverside
Michael Gribskov, Purdue University
Siddhartha Kanrar, University of California Riverside
Lucas Knoflicek, University of Nebraska-Lincoln
Becky Stevenson, University of California Riverside
Mingtang Xie, University of California Riverside
Xia Xu, University of California Davis
Xianwu Zheng, University of California Riverside
Jing-Kang Zhu, University of California Riverside
Pamela Ronald, University of California Davis
Michael E. Fromm, University of Nebraska-LincolnFollow

Document Type

Article

Date of this Version

2009

Citation

Rohila JS, Chen M, Chen S, Chen J, Cerny RL, et al. (2009) Protein-Protein Interactions of Tandem Affinity Purified Protein Kinases from Rice. PLoS ONE 4(8): e6685. doi:10.1371/journal.pone.0006685

Abstract

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 TAPtagged 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.