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

Autor: Jai S Rohila, Mei Chen, Shuo Chen, Johann Chen, Ronald L Cerny, Christopher Dardick, Patrick Canlas, Hiroaki Fujii, Michael Gribskov, Siddhartha Kanrar, Lucas Knoflicek, Becky Stevenson, Mingtang Xie, Xia Xu, Xianwu Zheng, Jian-Kang Zhu, Pamela Ronald, Michael E Fromm
Jazyk: angličtina
Rok vydání: 2009
Předmět:
Zdroj: PLoS ONE, Vol 4, Iss 8, p e6685 (2009)
Druh dokumentu: article
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0006685
Popis: 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.
Databáze: Directory of Open Access Journals