5V5F

Crystal structure of RICE1 (PNT2)

5V5F の概要

• エントリーDOI: 10.2210/pdb5v5f/pdb
• 分子名称: At3g11770 (1 entity in total)
• 機能のキーワード: nuclease, mi-rna, transferase
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 68940.51

構造登録者

Li, P. (登録日: 2017-03-14, 公開日: 2017-09-13, 最終更新日: 2024-03-06)

主引用文献

Zhang, Z.,Hu, F.,Sung, M.W.,Shu, C.,Castillo-Gonzalez, C.,Koiwa, H.,Tang, G.,Dickman, M.,Li, P.,Zhang, X.
RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) degrade uridylated cleavage fragments to maintain functional RISC in Arabidopsis thaliana.
Elife, 6:-, 2017

PubMed Abstract: RNA-induced silencing complex (RISC) is composed of miRNAs and AGO proteins. AGOs use miRNAs as guides to slice target mRNAs to produce truncated 5' and 3' RNA fragments. The 5' cleaved RNA fragments are marked with uridylation for degradation. Here, we identified novel cofactors of Arabidopsis AGOs, named RICE1 and RICE2. RICE proteins specifically degraded single-strand (ss) RNAs in vitro; but neither miRNAs nor miRNA*s in vivo. RICE1 exhibited a DnaQ-like exonuclease fold and formed a homohexamer with the active sites located at the interfaces between RICE1 subunits. Notably, ectopic expression of catalytically-inactive RICE1 not only significantly reduced miRNA levels; but also increased 5' cleavage RISC fragments with extended uridine tails. We conclude that RICEs act to degrade uridylated 5' products of AGO cleavage to maintain functional RISC. Our study also suggests a possible link between decay of cleaved target mRNAs and miRNA stability in RISC.

PubMed: 28463111
DOI: 10.7554/eLife.24466

実験手法

X-RAY DIFFRACTION (2.945 Å)