The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II Journal Article
| Authors: | Ho, C. K.; Sriskanda, V.; McCracken, S.; Bentley, D.; Schwer, B.; Shuman, S. |
| Article Title: | The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II |
| Abstract: | We have conducted a biochemical and genetic analysis of mouse mRNA capping enzyme (Mce1), a bifunctional 597-amino acid protein with RNA triphosphatase and RNA guanylyltransferase activities. The principal conclusions are as follows: (i) the mammalian capping enzyme consists of autonomous and nonoverlapping functional domains; (ii) the guanylyltransferase domain Mce1(211-597) is catalytically active in vitro and functional in vive in yeast in lieu of the endogenous guanylyltransferase Ceg1; (iii) the guanylyltransferase domain per se binds to the phosphorylated RNA polymerase II carboxyl-terminal domain (CTD), whereas the triphosphatase domain, Mce1(1-210), does not bind to the CTD; and (iv) a mutation of the active site cysteine of the mouse triphosphatase elicits a strong growth- suppressive phenotype in yeast, conceivably by sequestering pro-mRNA ends in a nonproductive complex or by blocking access of the endogenous yeast triphosphatase to RNA polymerase II. These findings contribute to an emerging model of mRNA biogenesis wherein RNA processing enzymes are targeted to nascent polymerase II transcripts through contacts with the CTD. The phosphorylation-dependent interaction between guanylyltransferase and the CTD is conserved from yeast to mammals. |
| Keywords: | nonhuman; animals; mice; phosphatase; carboxy terminal sequence; protein protein interaction; transcription, genetic; phosphorylation; enzyme phosphorylation; amino acid sequence; kinetics; saccharomyces cerevisiae; rna, messenger; mammal; nucleotide sequence; peptide fragments; recombinant proteins; mutagenesis, site-directed; binding sites; point mutation; mammals; enzyme binding; guanosine triphosphate; rna polymerase ii; complementary dna; biogenesis; cations, divalent; rna capping; genetic complementation test; nucleotidyltransferases; transferase; protein sorting signals; cloning, organism; priority journal; article |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 273 |
| Issue: | 16 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1998-04-17 |
| Start Page: | 9577 |
| End Page: | 9585 |
| Language: | English |
| DOI: | 10.1074/jbc.273.16.9577 |
| PUBMED: | 9545288 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 12 December 2016 -- Source: Scopus |
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