Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex

被引：3

作者：

Duan, Shuyan ^{[1
,2
]}

Gao, Wenqing ^{[1
,2
]}

Chen, Zijun ^{[1
,2
]}

Li, Zhengyang ^{[1
,2
]}

Li, Suhua ^{[1
,2
]}

Gan, Jianhua ^{[1
,2
]}

Chen, Xiangjun ^{[3
]}

Li, Jixi ^{[1
,2
]}

机构：

[1] Fudan Univ, Sch Life Sci, Dept Neurol, State Key Lab Genet Engn, Shanghai 200438, Peoples R China

[2] Fudan Univ, Huashan Hosp, Shanghai 200438, Peoples R China

[3] Fudan Univ, Huashan Hosp, Dept Neurol, Shanghai 200040, Peoples R China

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 2020年 / 122卷

基金：

中国国家自然科学基金;

关键词：

Human archease; Crystal structure; RTCB; SEQUENTIAL; 2'; 3'-CYCLIC PHOSPHODIESTERASE; MESSENGER-RNA; RTCB; PROTEIN; REPAIR; LIGATION; REGENERATION; SPECIFICITY; COMPONENT; MODEL;

D O I：

10.1016/j.biocel.2020.105744

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom to 3.4 angstrom. 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.

引用

页数：8

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