Function of Ceg1p and the Cet1-Ceg1 mRNA Capping Complex
Ceg1p is an mRNA guanylyltransferase in Saccharomyces cerevisiae that forms a heterotetramer with the RNA triphosphatase cet1p which is called the mRNA capping apparatus. This complex is recruited by RNA polymerase II (RNAP-II) and performs the first two steps in the 5’-guanisine capping mechanism of mRNA. Cet1p hydrolyzes the 5’-triphosphate end of the mRNA, then Ceg1p attaches a guanine monophosphate (GMP) to the 5’-diphosphate end (1). This 5’ capping is necessary for cells to live in yeast among other organisms. The interactions between Cet1p and Ceg1p are extremely important for inducing capping activity. These interactions both stimulate Ceg1p GMP transfer and help localize the complex in the nucleus where RNAP-II can recruit it (2).
Structure of Ceg1p and Interactions with Cet1p in the Capping Apparatus
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
