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Data show that decapping scavenger enzyme DcpS (DcpS) is a nucleocytoplasmic shuttling protein that activates microRNA (miRNA) degradation.
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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.
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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.
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DCPS and more generally RNA catabolism, are critical for neurological development, normal cognition and organismal homeostasis in humans.
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data demonstrate that DcpS in conjunction with Xrn1 has the potential to regulate RNA stability in a transcript-selective manner in mammalian cells
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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.
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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.
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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.
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crystal structures of DcpS in ligand-free form and in a complex with m7GDP
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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
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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.
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biochemical analysis of the dynamic and mutually exclusive cap hydrolysis activity of the two cap binding sites of DcpS
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Data established that DcpS, a key enzyme in mRNA decay, is a new target of DeltaLf transcriptional activity.
