ArticleThe Journal of biological chemistry2008
Mechanistic and kinetic analysis of the DcpS scavenger decapping enzyme.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Analysis of ligand binding mechanism by dimeric receptors using stopped-flow fluorimetry-application to the human decapping scavenger enzyme.European biophysics journal : EBJ · 2025Article
- Structural Fluctuation in Homodimeric Aminoacyl-tRNA Synthetases Induces Half-of-the-Sites Activity.The journal of physical chemistry. B · 2024Article
- Targeted Degradation of mRNA Decapping Enzyme DcpS by a VHL-Recruiting PROTAC.ACS chemical biology · 2022Article
- Effect of the His-Tag Location on Decapping Scavenger Enzymes and Their Hydrolytic Activity toward Cap Analogs.ACS omega · 2020Article
- The yeast scavenger decapping enzyme DcpS and its application for in vitro RNA recapping.Scientific reports · 2019Article
- The Interplay between the RNA Decay and Translation Machinery in Eukaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- An excess of catalytically required motions inhibits the scavenger decapping enzyme.Nature chemical biology · 2015Article
- DcpS is a transcript-specific modulator of RNA in mammalian cells.RNA (New York, N.Y.) · 2015Article
- Structure and Function in Homodimeric Enzymes: Simulations of Cooperative and Independent Functional Motions.PloS one · 2015Article
- Elimination of cap structures generated by mRNA decay involves the new scavenger mRNA decapping enzyme Aph1/FHIT together with DcpS.Nucleic acids research · 2015Article
- Kinetic mechanism of human histidine triad nucleotide binding protein 1.Biochemistry · 2013Article
- Inhibition and avoidance of mRNA degradation by RNA viruses.Current opinion in microbiology · 2012Review
- DcpS as a therapeutic target for spinal muscular atrophy.ACS chemical biology · 2008Article
- Regulation of mRNA decapping.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Decapping is an important process in the control of eukaryotic mRNA degradation. The scavenger decapping enzyme DcpS functions to clear the cell of cap structure following decay of the RNA body by catalyzing the hydrolysis of m(7)GpppN to m(7)Gp and ppN. Structural analysis has revealed that DcpS is a dimeric protein with a domain-swapped amino terminus. The protein dimer contains two cap binding/hydrolysis sites and displays a symmetric structure with both binding sites in the open conformation in the ligand-free state and an asymmetric conformation with one site open and one site closed in the ligand-bound state. The structural data are suggestive of a dynamic decapping mechanism where each monomer could alternate between an open and closed state. Using transient state kinetic studies, we show that both the rate-limiting step and rate of decapping are regulated by cap substrate. A regulatory mechanism is established by the intrinsic domain-swapped structure of the DcpS dimer such that the decapping reaction is very efficient at low cap substrate concentrations yet regulated with excess cap substrate. These data provide biochemical evidence to verify experimentally a dynamic and mutually exclusive cap hydrolysis activity of the two cap binding sites of DcpS and provide key insights into its regulation.
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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.