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Article

Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain.

Genes & development - 15 Nov 1998

Cho E J, Rodriguez C R, Takagi T, Buratowski S

Abstract excerpt

mRNA capping is a cotranscriptional event mediated by the association of capping enzyme with the phosphorylated carboxy-terminal domain (CTD) of RNA polymerase II. In the yeast Saccharomyces cerevisiae, capping enzyme is composed of two subunits, the mRNA 5'-triphosphatase (Cet1) and the mRNA guanylyltransferase (Ceg1). Here we map interactions between Ceg1, Cet1, and the CTD. Although the guanylyltransferase...

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Identifiers

PMID: 9832501
DOI: 10.1101/gad.12.22.3482
PMCID: PMC317247

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Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxy-terminal domain.PMID 9832501Read ↗

The mRNA capping enzyme of Saccharomyces cerevisiae has dual specificity to interact with CTD of RNA Polymerase II.Semantic proximity Read ↗

Structural insights to how mammalian capping enzyme reads the CTD code.Semantic proximity Read ↗

An essential function of Saccharomyces cerevisiae RNA triphosphatase Cet1 is to stabilize RNA guanylyltransferase Ceg1 against thermal inactivation.Semantic proximity Read ↗

The length, phosphorylation state, and primary structure of the RNA polymerase II carboxyl-terminal domain dictate interactions with mRNA capping enzymes.Semantic proximity Read ↗

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

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