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Structural basis for Gemin5 decamer-mediated mRNA binding

Authors :
Qiong Guo
Shidong Zhao
Rosario Francisco-Velilla
Jiahai Zhang
Azman Embarc-Buh
Salvador Abellan
Mengqi Lv
Peiping Tang
Qingguo Gong
Huaizong Shen
Linfeng Sun
Xuebiao Yao
Jinrong Min
Yunyu Shi
Encarnacion Martínez-Salas
Kaiming Zhang
Chao Xu
Source :
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Publication Year :
2022
Publisher :
Nature Portfolio, 2022.

Abstract

Structural biology, complemented by biochemistry experiments and RNA-binding assays show that the Gemin5 C-terminal region adopts a decamer architecture. Gemin5 decamerization is essential for its role in regulating mRNA translation.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
13
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.1415af1fefb643b1be8b200fb6c9501e
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-022-32883-z