The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II (Q28267712)

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S McCracken

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D Bentley

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B Schwer

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S Shuman

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

17 April 1998

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published in

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volume

273

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issue

16

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page(s)

9577-85

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cites work

5′-Capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II

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mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxy-terminal domain

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Mammalian capping enzyme complements mutant Saccharomyces cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II

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Isolation of the mRNA-capping enzyme and ferric-reductase-related genes from Candida albicans

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Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme--guanylate intermediate

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RNA capping enzyme and DNA ligase: a superfamily of covalent nucleotidyl transferases

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Isolation and Characterization of the Yeast mRNA Capping Enzyme β Subunit Gene Encoding RNA 5′-Triphosphatase, Which Is Essential for Cell Viability

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An RNA 5'-triphosphatase related to the protein tyrosine phosphatases

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Phylogeny of mRNA capping enzymes

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Site-directed mutagenesis by overlap extension using the polymerase chain reaction

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Form and function in protein dephosphorylation

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X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes

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Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases

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Domain structure of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli of a subdomain possessing the RNA 5'-triphosphatase and guanylyltransferase activities and a kinetic comparison to the full-size enzyme

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Mutational analysis of mRNA capping enzyme identifies amino acids involved in GTP binding, enzyme-guanylate formation, and GMP transfer to RNA.

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Functional mRNA can be generated by RNA polymerase III.

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Drosophila Cdk8, a kinase partner of cyclin C that interacts with the large subunit of RNA polymerase II.

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The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent cyclin-cyclin-dependent kinase complex

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Transcription elongation factor P-TEFb is required for HIV-1 Tat transactivation in vitro

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P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro

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The general transcription factors of RNA polymerase II

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