Sandbox ceg1p Steven Paris
From Proteopedia
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== Function of Ceg1p and the Cet1-Ceg1 mRNA Capping Complex == | == 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). | + | 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). |
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== Structure of Ceg1p and Interactions with Cet1p in the Capping Apparatus == | == Structure of Ceg1p and Interactions with Cet1p in the Capping Apparatus == | ||
Revision as of 01:54, 14 October 2014
Ceg1p mRNA Guanylyltransferase
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
