6Y3Z

Crystal structure of the Pby1 ATP-grasp enzyme bound to the S. cerevisiae mRNA decapping complex (Dcp1-Dcp2-Edc3)

6Y3Z の概要

• エントリーDOI: 10.2210/pdb6y3z/pdb
• 分子名称: m7GpppN-mRNA hydrolase, mRNA-decapping enzyme subunit 1, Enhancer of mRNA-decapping protein 3, ... (5 entities in total)
• 機能のキーワード: rna decay enzyme, hydrolase
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 117021.31

構造登録者

Graille, M. (登録日: 2020-02-19, 公開日: 2020-04-29, 最終更新日: 2024-01-24)

主引用文献

Charenton, C.,Gaudon-Plesse, C.,Back, R.,Ulryck, N.,Cosson, L.,Seraphin, B.,Graille, M.
Pby1 is a direct partner of the Dcp2 decapping enzyme.
Nucleic Acids Res., 48:6353-6366, 2020

PubMed Abstract: Most eukaryotic mRNAs harbor a characteristic 5' m7GpppN cap that promotes pre-mRNA splicing, mRNA nucleocytoplasmic transport and translation while also protecting mRNAs from exonucleolytic attacks. mRNA caps are eliminated by Dcp2 during mRNA decay, allowing 5'-3' exonucleases to degrade mRNA bodies. However, the Dcp2 decapping enzyme is poorly active on its own and requires binding to stable or transient protein partners to sever the cap of target mRNAs. Here, we analyse the role of one of these partners, the yeast Pby1 factor, which is known to co-localize into P-bodies together with decapping factors. We report that Pby1 uses its C-terminal domain to directly bind to the decapping enzyme. We solved the structure of this Pby1 domain alone and bound to the Dcp1-Dcp2-Edc3 decapping complex. Structure-based mutant analyses reveal that Pby1 binding to the decapping enzyme is required for its recruitment into P-bodies. Moreover, Pby1 binding to the decapping enzyme stimulates growth in conditions in which decapping activation is compromised. Our results point towards a direct connection of Pby1 with decapping and P-body formation, both stemming from its interaction with the Dcp1-Dcp2 holoenzyme.

PubMed: 32396195
DOI: 10.1093/nar/gkaa337

実験手法

X-RAY DIFFRACTION (3.49 Å)