Dcp1 Background Information Analysis of mRNA decay in Saccharomyces cerevisiae has shown that removal of the 5' cap structure is a key step in the turnover of many yeast mRNAs, and that this decapping is carried out by Dcp1 (1,2). Dcp1 is required for the normal decay of many unstable and stable yeast mRNAs, as well as mRNAs that are decapped independently of deadenylation (3). Dcp1 recognizes the mRNA substrate by interactions with both the cap and the RNA moiety (4). The Dcp1 is also a phosphoprotein, suggesting its activity may be regulated by post-transcriptional modification (4). The eukaryotic initiation factor complex eIF4F, which in yeast contains the core components eIF4E and eIF4G, uses the cap as a binding site, serving as an initial point of assembly for the translation apparatus (5). Dcp1 then interacts physically and functionally with the eIF4F translation initiation complex (5).
