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

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

来源：PLos One, 2009, 4(8): e6685.

DOI：10.1371/journal.pone.0006685

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.

• 出版日期2009-8-19