2014.02.03，Professor Shi Yunyu/Wu Jihui Published a paper entitled 發(fā)表“Crystal Structure of Arginine Methyltransferase 6 from Trypanosoma brucei” in PLoS ONE
時(shí)間：2021-04-12 21:15:01學(xué)院：生命科學(xué)學(xué)院學(xué)校：中國科學(xué)技術(shù)大學(xué)
Author：Wang Chongyuan，Zhu Yuwei，Chen Jiajia，Li Xu，Peng Junhui，Chen Jiaqian,Zou Yang，Chen Jiaqian，Zhang Zhiyong，Jin Hong Yang Fanyuan，Niu Liwen，Wu Jihui，Gong Qingguo，Teng Maikun，Shi Yunyu
Abstract:Arginine methylation plays vital roles in the cellular functions of the protozoanTrypanosoma brucei. The T. bruceiarginine methyltransferase 6 (TbPRMT6) is a type I arginine methyltransferase homologous to human PRMT6. In this study, we report the crystal structures of apo-TbPRMT6 and its complex with the reaction product S-adenosyl-homocysteine (SAH). The structure of apo-TbPRMT6 displays several features that are different from those of type I PRMTs that were structurally characterized previously, including four stretches of insertion, the absence of strandb15, and a distinct dimerization arm. The comparison of the apo-TbPRMT6 and SAH-TbPRMT6 structures revealed the fine rearrangements in the active site upon SAH binding. The isothermal titration calorimetry results demonstrated that SAH binding greatly increases the affinity of TbPRMT6 to a substrate peptide derived from bovine histone H4. The western blotting and mass spectrometry results revealed that TbPRMT6 methylates bovine histone H4 tail at arginine 3 but cannot methylate severalT. bruceihistone tails. In summary, our results highlight the structural differences between TbPRMT6 and other type I PRMTs and reveal that the active site rearrangement upon SAH binding is important for the substrate binding of TbPRMT6.
http://dx.doi.org/10.1371/journal.pone.0087267
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