Evidence map›Paper›PMID 11940655›Full record

ArticleMolecular and cellular biology2002

Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro.

Hiroshi Asahara, Sophie Tartare-Deckert, Takeya Nakagawa, Tsuyoshi Ikehara, Fumiko Hirose, Tony Hunter, Takashi Ito, Marc Montminy

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In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

39 citing papers in PubMed, 84 citations in OpenAlex.

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  18. Nucleosome eviction and activated transcription require p300 acetylation of histone H3 lysine 14.Proceedings of the National Academy of Sciences of the United States of America · 2010
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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 4 institutions in 2 countries.

Hiroshi AsaharaPeptide Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037, USA.
Sophie Tartare-Deckert
Takeya Nakagawa
Tsuyoshi Ikehara
Fumiko Hirose
Tony Hunter
Takashi Ito
Marc Montminy
Saitama Medical University · JPSalk Institute for Biological Studies · USAichi Cancer Center · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In a yeast two-hybrid screen to identify proteins that bind to the KIX domain of the coactivator p300, we obtained cDNAs encoding nucleosome assembly protein 1 (NAP-1), a 60-kDa histone H2A-H2B shuttling protein that promotes histone deposition. p300 associates preferentially with the H2A-H2B-bound form of NAP-1 rather than with the unbound form of NAP-1. Formation of NAP-1-p300 complexes was found to increase during S phase, suggesting a potential role for p300 in chromatin assembly. In micrococcal nuclease and supercoiling assays, addition of p300 promoted efficient chromatin assembly in vitro in conjunction with NAP-1 and ATP-utilizing chromatin assembly and remodeling factor; this effect was dependent in part on the intrinsic histone acetyltransferase activity of p300. Surprisingly, NAP-1 potently inhibited acetylation of core histones by p300, suggesting that efficient assembly requires acetylation of either NAP-1 or p300 itself. As p300 acted cooperatively with NAP-1 in stimulating transcription from a chromatin template in vitro, our results suggest a dual role of NAP-1-p300 complexes in promoting chromatin assembly and transcriptional activation.

Indexed as

Transcriptional ActivationAnimalsBlotting, WesternCell Cycle ProteinsCell NucleusChromatinDNADrosophilaDrosophila ProteinsElectrophoresis, Polyacrylamide GelHeLa CellsHumansNuclear ProteinsNucleosome Assembly Protein 1NucleosomesProtein BindingCell Cycle ProteinsChromatinDNADrosophila ProteinsNAP1L1 protein, humanNap1 protein, DrosophilaNuclear ProteinsNucleosome Assembly Protein 1NucleosomesProteinsRecombinant ProteinsTrans-Activators

Identifiers

PMID11940655
PMCPMC133748
OpenAlexW2106161842

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.