Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Importance of homodimerization for the in vivo function of yeast RNA triphosphatase.

The Journal of biological chemistry - 4 May 2001

Lehman K, Ho C K, Shuman S

Abstract excerpt

Saccharomyces cerevisiae RNA triphosphatase Cet1 is an essential component of the yeast mRNA capping apparatus. The active site of Cet1 resides within a topologically closed hydrophilic beta-barrel (the triphosphate tunnel) that is supported by a globular hydrophobic core. The homodimeric quatern...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acid Anhydride Hydrolases
Share to Dimerization
Share to Gene Dosage

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Enzymologic

Share to Mutagenesis

Share to Nucleotidyltransferases

Share to Protein Conformation

Share to Recombinant Fusion Proteins

Source

Identifiers

PMID: 11279098
DOI: 10.1074/jbc.M100588200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11279098-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Importance of homodimerization for the in vivo function of yeast RNA triphosphatase.PMID 11279098Read ↗

Functional groups required for the stability of yeast RNA triphosphatase in vitro and in vivo.Semantic proximity Read ↗

A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus.Semantic proximity Read ↗

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

Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus.Semantic proximity Read ↗

The domain order of mammalian capping enzyme can be inverted and baculovirus phosphatase can function in cap formation in vivo.Semantic proximity Read ↗

Characterization of Candida albicans RNA triphosphatase and mutational analysis of its active site.Semantic proximity Read ↗

A yeast-based genetic system for functional analysis of viral mRNA capping enzymes.Semantic proximity Read ↗

Structure of an mRNA capping enzyme bound to the phosphorylated carboxy-terminal domain of RNA polymerase II.Semantic proximity Read ↗

Characterization of a temperature-sensitive mutation that impairs the function of yeast tRNA nucleotidyltransferase.Semantic proximity Read ↗

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

Characterization of a trifunctional mimivirus mRNA capping enzyme and crystal structure of the RNA triphosphatase domain.Semantic proximity Read ↗

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 ↗

⌁Select a neighboring publication to make it the new centre.