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

Overlapping roles for the histone acetyltransferase activities of SAGA and elongator in vivo.

The EMBO journal - 15 Jun 2000

Wittschieben B O, Fellows J, Du W, Stillman D J, Svejstrup J Q

Abstract excerpt

Elp3 and Gcn5 are histone acetyltransferases (HATs) that function in transcription as subunits of Elongator and SAGA/ADA, respectively. Here we show that mutations that impair the in vitro HAT activity of Elp3 confer typical elp phenotypes such as temperature sensitivity. Combining an elp3Delta mutation with histone H3 or H4 tail mutations confers lethality or sickness, supporting a role for Elongator in...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Acetyltransferases
Share to Chromatin

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Histone Acetyltransferases

Share to Histone Deacetylases

Share to Protein Kinases

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 10856249
DOI: 10.1093/emboj/19.12.3060
PMCID: PMC203375

Genes

ADA

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Overlapping roles for the histone acetyltransferase activities of SAGA and elongator in vivo.PMID 10856249Read ↗

Functional organization of the yeast SAGA complex: distinct components involved in structural integrity, nucleosome acetylation, and TATA-binding protein interaction.Semantic proximity Read ↗

Function and regulation of the Spt-Ada-Gcn5-Acetyltransferase (SAGA) deubiquitinase module.Semantic proximity Read ↗

SUPT3H-less SAGA coactivator can assemble and function without significantly perturbing RNA polymerase II transcription in mammalian cellsSemantic proximity Read ↗

Expression profiling of S. pombe acetyltransferase mutants identifies redundant pathways of gene regulation.Semantic proximity Read ↗

A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme.Semantic proximity Read ↗

Multi-tasking on chromatin with the SAGA coactivator complexes.Semantic proximity Read ↗

The ADA complex is a distinct histone acetyltransferase complex in Saccharomyces cerevisiae.Semantic proximity Read ↗

Critical residues for histone acetylation by Gcn5, functioning in Ada and SAGA complexes, are also required for transcriptional function in vivo.Semantic proximity Read ↗

The novel SLIK histone acetyltransferase complex functions in the yeast retrograde response pathway.Semantic proximity Read ↗

The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex.Semantic proximity Read ↗

The Transcriptional Adaptor Protein ADA3a Modulates Flowering of Arabidopsis thaliana.Semantic proximity Read ↗

The elongator complex interacts with PCNA and modulates transcriptional silencing and sensitivity to DNA damage agents.Semantic proximity Read ↗

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