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A rice kinase-protein interaction map.
- Source :
-
Plant physiology [Plant Physiol] 2009 Mar; Vol. 149 (3), pp. 1478-92. Date of Electronic Publication: 2008 Dec 24. - Publication Year :
- 2009
-
Abstract
- Plants uniquely contain large numbers of protein kinases, and for the vast majority of the 1,429 kinases predicted in the rice (Oryza sativa) genome, little is known of their functions. Genetic approaches often fail to produce observable phenotypes; thus, new strategies are needed to delineate kinase function. We previously developed a cost-effective high-throughput yeast two-hybrid system. Using this system, we have generated a protein interaction map of 116 representative rice kinases and 254 of their interacting proteins. Overall, the resulting interaction map supports a large number of known or predicted kinase-protein interactions from both plants and animals and reveals many new functional insights. Notably, we found a potential widespread role for E3 ubiquitin ligases in pathogen defense signaling mediated by receptor-like kinases, particularly by the kinases that may have evolved from recently expanded kinase subfamilies in rice. We anticipate that the data provided here will serve as a foundation for targeted functional studies in rice and other plants. The application of yeast two-hybrid and TAPtag analyses for large-scale plant protein interaction studies is also discussed.
- Subjects :
- Amino Acid Sequence
Casein Kinase II metabolism
Cyclin-Dependent Kinases metabolism
Mitogen-Activated Protein Kinases metabolism
Models, Biological
Molecular Sequence Data
Phylogeny
Plant Proteins chemistry
Protein Binding
Protein Kinases chemistry
Transcription Factors
Two-Hybrid System Techniques
Ubiquitin-Protein Ligases metabolism
Oryza enzymology
Plant Proteins metabolism
Protein Interaction Mapping methods
Protein Kinases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0032-0889
- Volume :
- 149
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Plant physiology
- Publication Type :
- Academic Journal
- Accession number :
- 19109415
- Full Text :
- https://doi.org/10.1104/pp.108.128298