Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice

被引：108

作者：

Rohila, JS

Chen, M

Chen, S

Chen, J

Cerny, R

Dardick, C

Canlas, P

Xu, X

Gribskov, M

Kanrar, S

Zhu, JK

Ronald, P

Fromm, ME ^{[1
]}

机构：

[1] Univ Nebraska, Plant Sci Initiat, Lincoln, NE 68588 USA

[2] Univ Calif Davis, Dept Plant Pathol, Davis, CA 95616 USA

[3] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA

[4] Purdue Univ, Dept Biol Sci, W Lafayette, IN 47907 USA

[5] Univ Calif Riverside, Riverside, CA 92521 USA

来源：

PLANT JOURNAL | 2006年 / 46卷 / 01期

关键词：

Oryza sativa; tandem affinity purification; affinity; protein kinase; proteomics;

D O I：

10.1111/j.1365-313X.2006.02671.x

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Forty- one rice cDNAs encoding protein kinases were fused to the tandem affinity purification ( TAP) tag and expressed in transgenic rice plants. The TAP- tagged kinases and interacting proteins were purified from the T1 progeny of the transgenic rice plants and identified by mass spectrometry. Ninety- five percent of the TAP-tagged kinases were recovered. Fifty- six percent of the TAP- tagged kinases were found to interact with other rice proteins. A number of these interactions were consistent with known protein complexes found in other species, validating the TAP- tag method in rice plants. Phosphorylation sites were identified on four of the kinases that interacted with either 14- 3- 3 proteins or cyclins.

引用

页码：1 / 13

页数：13

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