Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex.
Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex.
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人类古酶的晶体结构,它是 tRNA 剪接连接酶复合物的关键辅助因子。
DOI:
10.1016/j.biocel.2020.105744
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发表时间:
2020-03
期刊:
影响因子:
--
通讯作者:
Li Jixi
中科院分区:
文献类型:
--
作者:
Duan Shuyan;Gao Wenqing;Chen Zijun;Li Zhengyang;Li Suhua;Gan Jianhua;Chen Xiangjun;Li Jixi
The human archease, hereafter named HArch, is identified as a key cofactor of the tRNA-splicing ligase complex, and a potential therapeutic target for treating nervous system injuries. However, little is known about the structural basis of HArch in tRNA maturation, mRNA splicing, and RNA repair. Here we report the crystal structures of HArch and its two mutants D51A and D178A with resolutions ranging from 1.96 Å to 3.4 Å. HArch is composed of an extended N-terminal protrusion domain (NTD) and one compacted C-terminal domain (CTD). Unlike previously reported homologous proteins, the NTD of the first subunit interacts with the CTD of the second one, and this interaction might be important for maintaining protein stability. Moreover, HArch interacts and colocalizes with RNA ligase RTCB in cells. Our current study reveals the atomic structure of HArch and may help us understand its function in mRNA splicing.
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发表时间:
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影响因子:
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作者:
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发表时间:
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影响因子:
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