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Protein-protein interactions of tandem affinity purified protein kinases from rice.

  • Author(s): 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
  • et al.
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 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.

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