Arabidopsis serine/threonine/tyrosine protein kinase phosphorylates oil body proteins that regulate oil content in the seeds
Autor: | Ram Rajasekharan, Anitha Vijayakumar, Iyappan Ramachandiran, Visvanathan Ramya |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Arabidopsis lcsh:Medicine Saccharomyces cerevisiae Protein Serine-Threonine Kinases Biochemistry Article 03 medical and health sciences Substrate-level phosphorylation Oil body Gene Expression Regulation Plant Protein Isoforms Protein phosphorylation Amino Acid Sequence Phosphorylation Tyrosine lcsh:Science Protein kinase A Multidisciplinary biology Arabidopsis Proteins Chemistry Gene Expression Profiling Threonine/Tyrosine Protein Kinase lcsh:R Lipid Droplets Lipid Metabolism biology.organism_classification Recombinant Proteins Cell biology 030104 developmental biology Mutation Seeds lcsh:Q Protein Processing Post-Translational |
Zdroj: | Scientific Reports, Vol 8, Iss 1, Pp 1-14 (2018) Scientific Reports |
ISSN: | 2045-2322 |
DOI: | 10.1038/s41598-018-19311-3 |
Popis: | Protein phosphorylation is an important post-translational modification that can regulate the protein function. The current knowledge on the phosphorylation status of plant oil body (OB) proteins is inadequate. This present study identifies the distinct physiological substrates of Arabidopsis serine/threonine/tyrosine protein kinase (STYK) and its role in seed oil accumulation; the role of Arabidopsis OLE1, a major seed OB protein has also been elucidated. In vitro kinase assay followed by mass spectrometry identifies residue that are phosphorylated by STYK. Further, co-expression of OLE1 and STYK in yeast cells increases the cellular lipid levels and reduces the total lipid when OLE1 was replaced with OLE1T166A. Moreover, in vivo experiments with OB isolated from wild-type and styk knock-out lines show the ability of STYK to phosphorylate distinct OB proteins. OLE1T166A mutant and Arabidopsis styk mutant demonstrate the significant reduction of its substrate phosphorylation. styk mutant line significantly reduces the amount of total seed oil as compared to wild-type seeds. Together, our results provide the evidences that Arabidopsis At2G24360 (STYK) is phosphorylating oil body proteins and the phosphorylation regulates the oil content in Arabidopsis seeds. |
Databáze: | OpenAIRE |
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