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Article

Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5.

The Journal of biological chemistry - 31 May 2002

Pei Yi, Shuman Stewart

Abstract excerpt

Elongating RNA polymerase II is targeted by macromolecular assemblies that regulate mRNA synthesis and processing. The capping apparatus is the first of the assemblies to act on the nascent pre-mRNA. Although recruitment of the capping enzymes to the transcription complex is dependent on phosphorylation of the C-terminal domain of the Rpb1 subunit of polymerase II (Pol-II), there may be additional levels of...

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Identifiers

PMID: 11893740
DOI: 10.1074/jbc.M200015200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Interactions between fission yeast mRNA capping enzymes and elongation factor Spt5.PMID 11893740Read ↗

Separable functions of the fission yeast Spt5 carboxyl-terminal domain (CTD) in capping enzyme binding and transcription elongation overlap with those of the RNA polymerase II CTD.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 ↗

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

Functional interaction of Rpb1 and Spt5 C-terminal domains in co-transcriptional histone modification.Semantic proximity Read ↗

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