Volume 3 Issue 6
Jun.  2012
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Lifang Niu, Falong Lu, Taolan Zhao, Chunyan Liu, Xiaofeng Cao. The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation[J]. Protein&Cell, 2012, 3(6): 450-459. doi: 10.1007/s13238-012-2935-3
Citation: Lifang Niu, Falong Lu, Taolan Zhao, Chunyan Liu, Xiaofeng Cao. The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation[J]. Protein&Cell, 2012, 3(6): 450-459. doi: 10.1007/s13238-012-2935-3

The enzymatic activity of Arabidopsis protein arginine methyltransferase 10 is essential for flowering time regulation

doi: 10.1007/s13238-012-2935-3
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We would like to thank Aiying Zhang and Qingbao Zhu in Xiaofeng Cao's lab for technical supports. We also thank The Arabidopsis Biological Resource Center at Ohio State for providing SALK T-DNA-insertion lines. This work was supported by the National Basic Research Program of China (Nos. 2011CB915400 and 2009CB941500 to X.C.), the National Natural Science Foundation of China (Grant Nos. 30930048 and 30921061 to X.C., and 90919033 to C.L.), and the Chinese Academy of Sciences (No. KSCX2-EWQ-24-02 to C.L.)

  • Received Date: 2012-04-12
  • Rev Recd Date: 2012-05-21
  • Arabidopsis AtPRMT10 is a plant-specific type I protein arginine methyltransferase that can asymmetrically dimethylate arginine 3 of histone H4 with auto-methylation activity. Mutations of AtPRMT10 derepress FLOWERING LOCUS C (FLC) expression resulting in a late-flowering phenotype. Here, to further investigate the biochemical characteristics of AtPRMT10, we analyzed a series of mutated forms of the AtPRMT10 protein. We demonstrate that the conserved "VLD" residues and "double-E loop" are essential for enzymatic activity of AtPRMT10. In addition, we show that Arg54 and Cys259 of AtPRMT10, two residues unreported in animals, are also important for its enzymatic activity. We find that Arg13 of AtPRMT10 is the auto-methylation site. However, substitution of Arg13 to Lys13 does not affect its enzymatic activity. In vivo complementation assays reveal that plants expressing AtPRMT10 with VLD-AAA, E143Q or E152Q mutations retain high levels of FLC expression and fail to rescue the late-flowering phenotype of atprmt10 plants. Taken together, we conclude that the methyltransferase activity of AtPRMT10 is essential for repressing FLC expression and promoting flowering in Arabidopsis.
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