2L6M

Structure of C-terminal dsRBD of the Fission Yeast DICER (Dcr1)

2L6M の概要

• エントリーDOI: 10.2210/pdb2l6m/pdb
• NMR情報: BMRB: 17315
• 分子名称: Protein Dicer, ZINC ION (2 entities in total)
• 機能のキーワード: dsrbd, dicer, hydrolase
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14043.67

構造登録者

Barraud, P.,Allain, F.H.-T. (登録日: 2010-11-23, 公開日: 2011-08-24, 最終更新日: 2024-05-15)

主引用文献

Barraud, P.,Emmerth, S.,Shimada, Y.,Hotz, H.R.,Allain, F.H.,Buhler, M.
An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer.
Embo J., 30:4223-4235, 2011

PubMed Abstract: Dicer proteins function in RNA interference (RNAi) pathways by generating small RNAs (sRNAs). Here, we report the solution structure of the C-terminal domain of Schizosaccharomyces pombe Dicer (Dcr1). The structure reveals an unusual double-stranded RNA binding domain (dsRBD) fold embedding a novel zinc-binding motif that is conserved among dicers in yeast. Although the C-terminal domain of Dcr1 still binds nucleic acids, this property is dispensable for proper functioning of Dcr1. In contrast, disruption of zinc coordination renders Dcr1 mainly cytoplasmic and leads to remarkable changes in gene expression and loss of heterochromatin assembly. In summary, our results reveal novel insights into the mechanism of nuclear retention of Dcr1 and raise the possibility that this new class of dsRBDs might generally function in nucleocytoplasmic trafficking and not substrate binding. The C-terminal domain of Dcr1 constitutes a novel regulatory module that might represent a potential target for therapeutic intervention with fungal diseases.

PubMed: 21847092
DOI: 10.1038/emboj.2011.300

実験手法

SOLUTION NMR