4A53

Structural basis of the Dcp1:Dcp2 mRNA decapping complex activation by Edc3 and Scd6

4A53 の概要

• エントリーDOI: 10.2210/pdb4a53/pdb
• 関連するPDBエントリー: 4A54
• NMR情報: BMRB: 18041
• 分子名称: EDC3 (1 entity in total)
• 機能のキーワード: rna binding protein
• 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: 14016.72

構造登録者

Fromm, S.A.,Truffault, V.,Kamenz, J.,Braun, J.E.,Hoffmann, N.A.,Izaurralde, E.,Sprangers, R. (登録日: 2011-10-24, 公開日: 2012-02-01, 最終更新日: 2024-06-19)

主引用文献

Fromm, S.A.,Truffault, V.,Kamenz, J.,Braun, J.E.,Hoffmann, N.A.,Izaurralde, E.,Sprangers, R.
The Structural Basis of Edc3- and Scd6-Mediated Activation of the Dcp1:Dcp2 Mrna Decapping Complex.
Embo J., 31:279-, 2011

PubMed Abstract: The Dcp1:Dcp2 decapping complex catalyses the removal of the mRNA 5' cap structure. Activator proteins, including Edc3 (enhancer of decapping 3), modulate its activity. Here, we solved the structure of the yeast Edc3 LSm domain in complex with a short helical leucine-rich motif (HLM) from Dcp2. The motif interacts with the monomeric Edc3 LSm domain in an unprecedented manner and recognizes a noncanonical binding surface. Based on the structure, we identified additional HLMs in the disordered C-terminal extension of Dcp2 that can interact with Edc3. Moreover, the LSm domain of the Edc3-related protein Scd6 competes with Edc3 for the interaction with these HLMs. We show that both Edc3 and Scd6 stimulate decapping in vitro, presumably by preventing the Dcp1:Dcp2 complex from adopting an inactive conformation. In addition, we show that the C-terminal HLMs in Dcp2 are necessary for the localization of the Dcp1:Dcp2 decapping complex to P-bodies in vivo. Unexpectedly, in contrast to yeast, in metazoans the HLM is found in Dcp1, suggesting that details underlying the regulation of mRNA decapping changed throughout evolution.

PubMed: 22085934
DOI: 10.1038/EMBOJ.2011.408

実験手法

SOLUTION NMR