Evidence map›Paper›PMID 11564863›Full record

ArticleMolecular and cellular biology2001

Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo.

E Martinez, V B Palhan, A Tjernberg, E S Lymar, A M Gamper, T K Kundu, B T Chait, R G Roeder

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In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers.

0numbers the graph read from it
0cells of the map it votes in
212citing papers in PubMed
7.9field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

212 citing papers in PubMed, 374 citations in OpenAlex.

  1. Review
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  9. GCN5L: a critical target in energy metabolism pathways.Frontiers in cell and developmental biology · 2025
    Review
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  11. Article
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  20. Research progress and therapeutic prospect of PHF5A acting as a new target for malignant tumors.Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2022
    Review

152 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 3 countries.

E MartinezLaboratories of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021, USA.
V B Palhan
A Tjernberg
E S Lymar
A M Gamper
T K Kundu
B T Chait
R G Roeder
Laboratoire de Biochimie · FRIONICS Mass Spectrometry (Canada) · CARockefeller University · US

Funding

YNG1 PHD BINDING TO H3 3METHYL AT K4 PROMOTES TRANSCRIPTION AT TARGETED ORFSP41RR000862 · NCRR · ROCKEFELLER UNIVERSITY · PI DARNELL, JAMES E · 1985 to 2011
$16.1M
MOLECULAR BASIS OF CELL GROWTH AND TRANSFORMATIONR35CA042567 · NCI · ROCKEFELLER UNIVERSITY · PI ROEDER, ROBERT G · 1986 to 1999
–
NCI NIH HHS CA42567NCRR NIH HHS P41 RR000862NCRR NIH HHS RR00862
6 · The paper itself

Abstract

GCN5 is a histone acetyltransferase (HAT) originally identified in Saccharomyces cerevisiae and required for transcription of specific genes within chromatin as part of the SAGA (SPT-ADA-GCN5 acetylase) coactivator complex. Mammalian cells have two distinct GCN5 homologs (PCAF and GCN5L) that have been found in three different SAGA-like complexes (PCAF complex, TFTC [TATA-binding-protein-free TAF(II)-containing complex], and STAGA [SPT3-TAF(II)31-GCN5L acetylase]). The composition and roles of these mammalian HAT complexes are still poorly characterized. Here, we present the purification and characterization of the human STAGA complex. We show that STAGA contains homologs of most yeast SAGA components, including two novel human proteins with histone-like folds and sequence relationships to yeast SPT7 and ADA1. Furthermore, we demonstrate that STAGA has acetyl coenzyme A-dependent transcriptional coactivator functions from a chromatin-assembled template in vitro and associates in HeLa cells with spliceosome-associated protein 130 (SAP130) and DDB1, two structurally related proteins. SAP130 is a component of the splicing factor SF3b that associates with U2 snRNP and is recruited to prespliceosomal complexes. DDB1 (p127) is a UV-damaged-DNA-binding protein that is involved, as part of a complex with DDB2 (p48), in nucleotide excision repair and the hereditary disease xeroderma pigmentosum. Our results thus suggest cellular roles of STAGA in chromatin modification, transcription, and transcription-coupled processes through direct physical interactions with sequence-specific transcription activators and with components of the splicing and DNA repair machineries.

Indexed as

DNA DamageRNA-Binding ProteinsRNA SplicingTranscriptional ActivationTranscription, GeneticAcetylationAdaptor Proteins, Signal TransducingAmino Acid SequenceBlotting, WesternCell LineCell NucleusChromatinDNA-Binding ProteinsElectrophoresis, Polyacrylamide GelHeLa CellsHumansAdaptor Proteins, Signal TransducingChromatinDDB1 protein, humanDdb1 protein, mouseDDB2 protein, humanDNA-Binding ProteinsNuclear ProteinsNucleosomesPhosphoproteinsRibonucleoprotein, U2 Small NuclearRNA-Binding ProteinsRNA PrecursorsRNA Splicing FactorsSF3B3 protein, humantransformation-transcription domain-associated protein

Identifiers

PMID11564863
PMCPMC99856
OpenAlexW2115674719

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.