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

Jai S. Rohila; Mei Chen; Shuo Chen; Johann Chen; Ronald Cerny; Chris Dardick; Patrick Canlas; Xia Xu; Michael Gribskov; Siddhartha Kanrar; Jian Kang Zhu; Pamela Ronald; Michael E. Fromm

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

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

Jai S. Rohila, Mei Chen, Shuo Chen, Johann Chen, Ronald Cerny, Chris Dardick, Patrick Canlas, Xia Xu, Michael Gribskov, Siddhartha Kanrar, Jian Kang Zhu, Pamela Ronald, Michael E. Fromm

Research output: Contribution to journal › Article › peer-review

129 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	1-13
Number of pages	13
Journal	Plant Journal
Volume	46
Issue number	1
DOIs	https://doi.org/10.1111/j.1365-313X.2006.02671.x
State	Published - Apr 2006

Keywords

Affinity
Oryza sativa
Protein kinase
Proteomics
Tandem affinity purification

ASJC Scopus subject areas

Genetics
Plant Science
Cell Biology

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

Cite this

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title = "Protein-protein interactions of tandem affinity purification-tagged protein kinases in rice",

abstract = "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.",

keywords = "Affinity, Oryza sativa, Protein kinase, Proteomics, Tandem affinity purification",

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AU - Rohila, Jai S.

AU - Chen, Mei

AU - Chen, Shuo

AU - Chen, Johann

AU - Cerny, Ronald

AU - Dardick, Chris

AU - Canlas, Patrick

AU - Xu, Xia

AU - Gribskov, Michael

AU - Kanrar, Siddhartha

AU - Zhu, Jian Kang

AU - Ronald, Pamela

AU - Fromm, Michael E.

PY - 2006/4

Y1 - 2006/4

N2 - 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.

AB - 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.

KW - Affinity

KW - Oryza sativa

KW - Protein kinase

KW - Proteomics

KW - Tandem affinity purification

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

Abstract

Keywords

ASJC Scopus subject areas

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