tailieunhanh - Báo cáo khoa học: A hydrophilic cation-binding protein of Arabidopsis thaliana, AtPCaP1, is localized to plasma membrane via N-myristoylation and interacts with calmodulin and the phosphatidylinositol phosphates PtdIns(3,4,5)P3 and PtdIns(3,5)P2

A hydrophilic cation-binding protein, PCaP1, was found to be stably bound to the plasma membrane inArabidopsis thaliana. PCaP1 was quanti-fied to account for – of the crude membrane fractions from roots and shoots. | ỊFEBS Journal A hydrophilic cation-binding protein of Arabidopsis thaliana AtPCaPI is localized to plasma membrane via N-myristoylation and interacts with calmodulin and the phosphatidylinositol phosphates PtdIns 3 4 5 P3 and PtdIns 3 5 P2 Nahoko Nagasaki Rie Tomioka and Masayoshi Maeshima Laboratory of CellDynamics Graduate Schoolof BioagriculturalSciences Nagoya University Japan Keywords Arabidopsis calcium myristoylation phosphatidylinositol phosphate plasma membrane Correspondence M. Maeshima Laboratory of CellDynamics Graduate School of Bioagricultural Sciences Nagoya University Nagoya 464-8601 Japan Fax 81 52 789 4096 Tel 81 52 789 4096 E-mail maeshima@ Received 19 October 2007 revised 5 February 2008 accepted 5 March 2008 doi A hydrophilic cation-binding protein PCaPl was found to be stably bound to the plasma membrane in Arabidopsis thaliana. PCaP1 was quantified to account for of the crude membrane fractions from roots and shoots. Its homologous protein was detected in several plant species. We investigated the mechanism of membrane association of PCaPl by transient expression of fusion protein with green fluorescent protein. The amino-terminal sequence of 27 residues of PCaPl had a potential to localize the fusion protein with green fluorescent protein to the plasma membrane and the substitution of Gly at position 2 with Ala resulted in the cytoplasmic localization of PCaPl. When PCaPl was expressed in the in vitro transcription translation system with 3H myristic acid the label was incorporated into PCaPl but not into a mutant PCaPl with Gly2 replaced by Ala. These results indicate that PCaPl tightly binds to the plasma membrane via N-myristoylation at Gly2. We examined the binding capacity with phosphatidylinositol phosphates PtdInsPs and found that PCaPl selectively interacts with phosphatidylinositol 3 5-bisphosphate and phosphatidylinositol 3 4 5-triphosphate. Competition assay with the .

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