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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Fresco, L. D. Buratowski, S. |
| Description | Author Affiliation: Fresco LD ( Whitehead Institute for Biomedical Research, Cambridge, MA 02142.); |
| Abstract | Nascent mRNA chains are capped at the 5' end by the addition of a guanylyl residue to form a G(5')ppp(5')N ... structure. During the capping reaction, the guanylyltransferase (GTP:mRNA guanylyltransferase, EC 2.7.7.50) is reversibly and covalently guanylylated. In this enzyme-GMP (E-GMP) intermediate, GMP is linked to the epsilon-amino group of a lysine residue via a phosphoamide bond. Lys-70 was identified as the GMP attachment site of the Saccharomyces cerevisiae guanylyltransferase (encoded by the CEG1 gene) by guanylylpeptide sequencing. CEG1 genes with substitutions at Lys-70 were unable to support viability in yeast and produced proteins that were not guanylylated in vitro. The CEG1 active site exhibits sequence similarity to the active sites of viral guanylyltransferases and polynucleotide ligases, suggesting similarity in the mechanisms of nucleotidyl transfer catalyzed by these enzymes. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 14 |
| Volume Number | 91 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1994-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | DNA Ligases Chemistry Nucleotidyltransferases RNA Ligase (ATP) Saccharomyces Cerevisiae Enzymology Genetics Amino Acid Sequence Bacteria Binding Sites Biosynthesis DNA Primers Genes, Fungal Molecular Sequence Data Metabolism Polymerase Chain Reaction Recombinant Proteins Sequence Homology, Amino Acid Viruses Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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