A tobacco CBL-interacting protein kinase homolog is involved in phosphorylation of the N-terminal domain of the cucumber mosaic virus polymerase 2a protein
| Autor: | Young Pyo Lee, Young In Park, Hyun Ku Kang, Seung Hwan Yang, Sang Hyon Kim |
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| Rok vydání: | 2012 |
| Předmět: |
Molecular Sequence Data
Biology Mitogen-activated protein kinase kinase Protein Serine-Threonine Kinases Applied Microbiology and Biotechnology Biochemistry Cucumovirus Analytical Chemistry MAP2K7 Enzyme Stability Tobacco c-Raf Amino Acid Sequence Cloning Molecular Phosphorylation Protein kinase A Molecular Biology Sequence Homology Amino Acid Organic Chemistry Cyclin-dependent kinase 2 Cell Membrane General Medicine Autophagy-related protein 13 RNA-Dependent RNA Polymerase Protein kinase R Molecular biology Protein Structure Tertiary Protein Transport biology.protein Cyclin-dependent kinase 9 Biotechnology |
| Zdroj: | Bioscience, biotechnology, and biochemistry. 76(11) |
| ISSN: | 1347-6947 |
| Popis: | The replication and transcription of cucumber mosaic virus (CMV) are catalyzed by multi-protein complex RNA-dependent RNA polymerase (RdRp), which is composed of the viral-encoded 1a and 2a proteins with host factors. We have reported that the N-terminal region of the polymerase 2a protein, composed of 126 amino acids, is required for interaction with the helicase 1a protein, and that the phosphorylation of the region abrogated interaction with the 1a protein, suggesting a mechanism of resistance in host plants against viral infection. Here, we found that three protein 2a kinases, of 60, 55, and 38 kDa, co-purified with the tobacco membrane fraction in an in-gel kinase assay. By yeast two-hybrid library screening using the N-terminal 126 amino acids of 2a as a bait, we identified CBL-interacting protein kinase 12 (NtCIPK12) corresponding to 55 kDa protein 2a kinase. The bacterially expressed protein kinase showed protein 2a kinase (t2aK) activity in vitro. We found that NtCIPK12 stabilized upon CMV infection at the post-translational level, and accumulated more heavily to the membrane than in the cytosol. |
| Databáze: | OpenAIRE |
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