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Necessary for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Additionally we are shipping Decapping Enzyme, Scavenger Antibodies (47) and Decapping Enzyme, Scavenger Proteins (9) and many more products for this protein.
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Data show that decapping scavenger enzyme DcpS (DcpS) is a nucleocytoplasmic shuttling protein that activates microRNA (miRNA) degradation.
In DcpS, conformational change is dominated by an anti-symmetric cooperative motion, causing one active site to close as the other opens; however a symmetric motion is also significant.
In vitro decapping assays showed that altered EDC3 is unable to enhance DCP2 decapping at low concentrations and even inhibits DCP2 decapping at high concentration.
DCPS and more generally RNA catabolism, are critical for neurological development, normal cognition and organismal homeostasis in humans.
data demonstrate that DcpS in conjunction with Xrn1 has the potential to regulate RNA stability in a transcript-selective manner in mammalian cells
The central histidine within the DcpS HIT motif is critical for decapping activity and defines the HIT motif as a new mRNA decapping domain, making DcpS the first member of the HIT family of proteins with a defined biological function.
m7GDP breakdown by DcpS should prevent misincorporation of methylated nucleotides in nucleic acids and could generate a unique indicator allowing the cell to monitor mRNA decay.
Structural and biochemical analysis suggests an autoregulatory mechanism whereby premature decapping mRNA is prevented by blocking the conformational changes that are required to form a closed productive active site capable of cap hydrolysis.
crystal structures of DcpS in ligand-free form and in a complex with m7GDP
Furthermore, we show that a novel human histidine triad protein DCS-1, which is expressed together with NR1 in many tissues, can significantly reduce menadione-induced cytotoxicity in these cells
These studies demonstrate that the significance of DcpS extends beyond its well-characterized role in mRNA decay and involves a broader range of functions in RNA processing including nuclear pre-mRNA splicing.
biochemical analysis of the dynamic and mutually exclusive cap hydrolysis activity of the two cap binding sites of DcpS
Data established that DcpS, a key enzyme in mRNA decay, is a new target of DeltaLf transcriptional activity.
Amino acid sequence and xray crystallograpy structure given
Necessary for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA fragments shorter than 10 nucleotides that are produced by 3'->5' exosome-mediated mRNA decay. Releases m7GMP. Can also degrade m7GDP to m7GMP. Has no activity towards mRNA molecules longer than 25 nucleotides.
decapping enzyme, scavenger
, decapping scavenger enzyme
, heat shock-like protein 1
, hint-related 7meGMP-directed hydrolase
, histidine triad nucleotide-binding protein 5
, histidine triad protein member 5
, homolog of C. elegans 7meGMP-directed hydrolase dcs-1
, m7GpppX diphosphatase
, mRNA decapping enzyme
, scavenger mRNA-decapping enzyme DcpS