Discover Community Create You

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

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

The Journal of biological chemistry - 28 Sept 2001

Hausmann S, Ho C K, Schwer B, Shuman S

Abstract excerpt

Saccharomyces cerevisiae RNA triphosphatase (Cet1) and RNA guanylyltransferase (Ceg1) interact in vivo and in vitro to form a bifunctional mRNA capping enzyme complex. Here we show that the guanylyltransferase activity of Ceg1 is highly thermolabile in vitro (98% loss of activity after treatment for 10 min at 35 degrees C) and that binding to recombinant Cet1 protein, or a synthetic peptide Cet1(232-265),...

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 Alanine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Candida albicans

Share to Catalysis

Share to Chromatography, Affinity

Share to Hot Temperature

Share to Nucleotidyltransferases

Share to Schizosaccharomyces

Source

Identifiers

PMID: 11463793
DOI: 10.1074/jbc.M105856200

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

An essential function of Saccharomyces cerevisiae RNA triphosphatase Cet1 is to stabilize RNA guanylyltransferase Ceg1 against thermal inactivation.PMID 11463793Read ↗

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 ↗

Importance of homodimerization for the in vivo function of yeast RNA triphosphatase.Semantic proximity Read ↗

Isolation of temperature-sensitive mutants for mRNA capping enzyme in Saccharomyces cerevisiae.Semantic proximity Read ↗

Conditional inactivation of mRNA capping enzyme affects yeast pre-mRNA splicing in vivo.Semantic proximity Read ↗

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

Single allele knock-out of Candida albicans CGT1 leads to unexpected resistance to hygromycin B and elevated temperature.Semantic proximity Read ↗

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

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

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

Accelerated mRNA decay in conditional mutants of yeast mRNA capping enzyme.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 ↗

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