Prospectus, September 13, 1978

ELECTION DAYS ARE HERE!; Students get refund from hungry Canteen machines; Recipes for college students; CPR saves lives; Advertising Policy; PC band formed; \u27Lost in a masquerade\u27 Benson creates ecstasy; Creative writers receive assistance; Health issues program new WPCD addition; Operetta to begin tomorrow; Shaker photograph exhibition; Student Elections -- Today!; Cadaver lab is added; Apathetic turnout; Poet contest sponsored; Volleyball clinic held Sept. 9; Meeting Sept. 26 for cheerleaders; WPCD\u27s Top 15 For The Week Of Sept. 11; German club to begin activities; Classifieds; Cimmeron review \u27mediocre\u27; Thought food offered for older adults; Student Activities-\u2778; Doehring keeps on truckin\u27; Coach Jim Reed gets many players; Klems wins first Freddy contest; Cooper recruits well; Williams has busy year ahead of him; Fast Freddy Contest; Cross Country Schedulehttps://spark.parkland.edu/prospectus_1978/1012/thumbnail.jp

Structural basis of dcp2 recognition and activation by dcp1

A critical step in mRNA degradation is the removal of the 5' cap structure, which is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of an S. pombe Dcp1p-Dcp2n complex combined with small-angle X-ray scattering analysis (SAXS) reveals that Dcp2p exists in open and closed conformations, with the closed complex being, or closely resembling, the catalytically more active form. This suggests that a conformational change between these open and closed complexes might control decapping. A bipartite RNA-binding channel containing the catalytic site and Box B motif is identified with a bound ATP located in the catalytic pocket in the closed complex, suggesting possible interactions that facilitate substrate binding. Dcp1 stimulates the activity of Dcp2 by promoting and/or stabilizing the closed complex. Notably, the interface of Dcp1 and Dcp2 is not fully conserved, explaining why the Dcp1-Dcp2 interaction in higher eukaryotes requires an additional factor