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The major pathway of eukaryotic mRNA decay involves deadenylation-dependent decapping followed by 5' to 3'exonucleolytic degradation. Human decapping enzyme 2 (hDcp2) is an mRNA decapping enzyme which contains intrinsic decapping activity. In nonsense-mediated decay, the human decapping complex, made up of hDcp1 and hDcp2, may be recruited to mRNAs containing premature termination codons by nonsense-mediated decay factor (Upf) proteins. The decapping activator complex (Lsm1p-7p) is also involved in the recruitment of the decapping complex, indicated by data showing that Lsm1p-7p enhances the co-immunoprecipitation of the complex with mRNA. Dcp2 specifically hydrolyzes methylated capped RNA to release m7GDP, thereby aiding in mRNA degradation. Both Dcp1 and Dcp2 co-localize in the cytoplasm, which is consistent with their role in mRNA decay
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