background:
Eukaryotic cells primarily utilize exoribonucleases and decapping enzymes to degrade their mRNA. DcpS is a scavenger pyrophosphatase that hydrolyzes the residual cap structure following 3' to 5' decay of an mRNA. Following mRNA degradation DcpS releases N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. 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. HIT proteins are homodimeric and contain two conserved 100-amino-acid HIT fold domains with independent active sites that are each sufficient to bind and hydrolyze cognate substrates.
Function:
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.
Subunit:
Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1.
Subcellular Location:
Cytoplasm. Nucleus.
Tissue Specificity:
Detected in liver, brain, kidney, testis and prostate.
Similarity:
Belongs to the HIT family.
Database links:
UniProtKB/Swiss-Prot: Q96C86.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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