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United States Department of Agriculture

Agricultural Research Service

Title: Protein-protein interactions of TAP-tagged protein kinases in rice

Authors
item Rohila, Jai - UNIV OF NEBRASKA
item Chen, Mei - UNIV OF NEBRASKA
item Chen, Shuo - UNIV OF NEBRASKA
item Chen, Johann - UNIV OF CALIFORNIA
item Cerny, Ronald - UNIV OF NEBRASKA
item DARDICK, CHRISTOPHER
item Canlas, Patrick - UNIV OF CALIFORNIA
item Xu, Xia - UNIV OF CALIFORNIA
item Gribskov, Michael - PURDUE UNIV
item Kanrar, Siddhartha - UNIV OF CALIFORNIA
item Knoflicek, Lucas - UNIV OF NEBRASKA
item Zhu, Jian-Kang - UNIV OF CALIFORNIA
item Ronald, Pamela - UNIV OF CALIFORNIA
item Stevenson, Rebecca - UNIV OF CALIFORNIA
item Fromm, Michael - UNIV OF NEBRASKA

Submitted to: PLoS One
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: July 21, 2009
Publication Date: N/A

Interpretive Summary: The new science of genetic engineering has tremendous potential to solve agricultural problems that cannot be addressed through traditional plant breeding. However, engineering plants with new or improved agricultural traits, such as better seed/fruit quality, tolerance to drought or resistance to pests, requires knowledge about how individual plant genes function to control these traits. In this report, the results of a large scale study to identify the functions of 88 rice genes are described. Overall, the data reveals insights into the functions of 55 rice genes. While this study was performed in rice, this information can be widely applied to other plants and in many instances, even animals that share similar genes.

Technical Abstract: Eighty-eight rice (Oryza sativa) cDNAs encoding leaf expressed protein kinases (RLePKs) were fused to a Tandem Affinity Purification tag (TAPtag) and expressed in transgenic rice plants. The TAP-tagged RLePKs and interacting proteins were purified from the T1 progeny of the transgenic rice plants and identified by mass spectrometry. Sixty-three percent of the TAP-tagged RLePKs were recovered. Eighty percent of these were found to interact with other rice proteins. A number of these interactions were consistent with known protein complexes found in other species. A comparison of the TAP-tagged data 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.

Last Modified: 8/27/2014
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