ArticleProceedings of the National Academy of Sciences of the United States of America2012
Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 35 citations in OpenAlex.
- Non-redundant roles for the human mRNA decapping cofactor paralogs DCP1a and DCP1b.Life science alliance · 2024Article
- Eukaryotic mRNA decapping factors: molecular mechanisms and activity.The FEBS journal · 2023Review
- Assessing the applicability ofJournal of biomolecular NMR · 2023Article
- Decapping factor Dcp2 controls mRNA abundance and translation to adjust metabolism and filamentation to nutrient availability.bioRxiv : the preprint server for biology · 2023Article
- RNase H-based analysis of synthetic mRNA 5' cap incorporation.RNA (New York, N.Y.) · 2022Article
- Dcp2 C-terminaleLife · 2022Article
- Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022Review
- Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation.Nature chemical biology · 2021Article
- Dcp2: an mRNA decapping enzyme that adopts many different shapes and forms.Current opinion in structural biology · 2019Review
- The Translation Inhibitor Rocaglamide Targets a Bimolecular Cavity between eIF4A and Polypurine RNA.Molecular cell · 2019Article
- Structural and molecular mechanisms for the control of eukaryotic 5'-3' mRNA decay.Nature structural & molecular biology · 2018Review
- mRNA decapping: finding the right structures.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Control of mRNA decapping by autoinhibition.Nucleic acids research · 2018Article
- Structure of the activated Edc1-Dcp1-Dcp2-Edc3 mRNA decapping complex with substrate analog poised for catalysis.Nature communications · 2018Article
- Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of the active form of Dcp1-Dcp2 decapping enzyme bound to mNature structural & molecular biology · 2016Article
- Structural basis of mRNA-cap recognition by Dcp1-Dcp2.Nature structural & molecular biology · 2016Article
- The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface.RNA (New York, N.Y.) · 2016Article
- Sequences flanking the core-binding site modulate glucocorticoid receptor structure and activity.Nature communications · 2016Article
- Structure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformation.Nature structural & molecular biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Conformational dynamics in bilobed enzymes can be used to regulate their activity. One such enzyme, the eukaryotic decapping enzyme Dcp2, controls the half-life of mRNA by cleaving the 5' cap structure, which exposes a monophosphate that is efficiently degraded by exonucleases. Decapping by Dcp2 is thought to be controlled by an open-to-closed transition involving formation of a composite active site with two domains sandwiching substrate, but many details of this process are not understood. Here, using NMR spectroscopy and enzyme kinetics, we show that Trp43 of Schizosaccharomyces pombe Dcp2 is a conserved gatekeeper of this open-to-closed transition. We find that Dcp2 samples multiple conformations in solution on the millisecond-microsecond timescale. Mutation of the gatekeeper tryptophan abolishes the dynamic behavior of Dcp2 and attenuates coactivation by a yeast enhancer of decapping (Edc1). Our results determine the dynamics of the open-to-closed transition in Dcp2, suggest a structural pathway for coactivation, predict that Dcp1 directly contacts the catalytic domain of Dcp2, and show that coactivation of decapping by Dcp2 is linked to formation of the composite active site.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.