Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain.
mRNA capping is a cotranscriptional event mediated by the association of capping enzyme with the phosphorylated carboxy-terminal domain (CTD) of RNA polymerase II. In the yeast Saccharomyces cerevisiae, capping enzyme is composed of two subunits, the mRNA 5'-triphosphatase (Cet1) and the mRNA guanylyltransferase (Ceg1). Here we map interactions between Ceg1, Cet1, and the CTD. Although the guanylyltransferase subunit can bind alone to the CTD, it cannot be guanylylated unless the triphosphatase subunit is also present. Therefore, the yeast mRNA guanylyltransferase is regulated by allosteric interactions with both the triphosphatase and CTD.
Cho
E J
EJ
Harvard Medical School, Boston, Massachusetts 02115 USA.
Rodriguez
C R
CR
Takagi
T
T
Buratowski
S
S
D017766:Acid Anhydride Hydrolases / Q000235:genetics; D000494:Allosteric Regulation / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics; D015966:Gene Expression Regulation, Fungal / Q000235:genetics; D005800:Genes, Fungal / Q000235:genetics; D009154:Mutation / Q000235:genetics; D009713:Nucleotidyltransferases / Q000235:genetics*; D012319:RNA Polymerase II / Q000235:genetics*; D011994:Recombinant Proteins / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D000098556:mRNA Guanylyltransferases
D005656:Fungal Proteins; D011994:Recombinant Proteins; D009713:Nucleotidyltransferases; D012319:RNA Polymerase II; D000098556:mRNA Guanylyltransferases; D017766:Acid Anhydride Hydrolases; C023090:RNA triphosphatase