(Q52580421)

3 May 2018

title

Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila. (English)

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3 May 2018

author

Peter B Becker

series ordinal

2

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3 May 2018

author name string

Akhtar A

series ordinal

1

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3 May 2018

publication date

1 February 2000

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3 May 2018

published in

Molecular Cell

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3 May 2018

volume

5

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3 May 2018

issue

2

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3 May 2018

page(s)

367-375

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3 May 2018

NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p

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Construction of an improved host strain for two hybrid screening

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The rox1 and rox2 RNAs are essential components of the compensasome, which mediates dosage compensation in Drosophila

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How flies make one equal two: dosage compensation in Drosophila

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Regulation of the sex-specific binding of the maleless dosage compensation protein to the male X chromosome in Drosophila.

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7 January 2021

Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster.

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mof, a putative acetyl transferase gene related to the Tip60 and MOZ human genes and to the SAS genes of yeast, is required for dosage compensation in Drosophila

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Use of phospho-cellulose paper disks for the assay of histone acetyltransferase

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Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes

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Transcription: gene control by targeted histone acetylation.

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Acetylation of general transcription factors by histone acetyltransferases

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Histone acetyltransferase activity of yeast Gcn5p is required for the activation of target genes in vivo

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7 January 2021

The maleless protein associates with the X chromosome to regulate dosage compensation in drosophila

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7 January 2021

Histone H4 acetylated at lysine 16 and proteins of the Drosophila dosage compensation pathway co-localize on the male X chromosome through mitosis.

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7 January 2021

Histone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin.

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7 January 2021

Mapping Polycomb-repressed domains in the bithorax complex using in vivo formaldehyde cross-linked chromatin

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7 January 2021

The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism

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7 January 2021

PcG complexes and chromatin silencing

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7 January 2021

Yeast SAS silencing genes and human genes associated with AML and HIV-1 Tat interactions are homologous with acetyltransferases

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7 January 2021

Heat shock factor increases the reinitiation rate from potentiated chromatin templates.

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7 January 2021

Dual regulation of the Drosophila hsp26 promoter in vitro.

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ESA1 is a histone acetyltransferase that is essential for growth in yeast

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7 January 2021

The drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation

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7 January 2021

Purified histone acetyltransferase complexes stimulate HIV-1 transcription from preassembled nucleosomal arrays

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7 January 2021

Disruption of higher-order folding by core histone acetylation dramatically enhances transcription of nucleosomal arrays by RNA polymerase III

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7 January 2021

Histone acetylation as an epigenetic determinant of long-term transcriptional competence

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7 January 2021

Histone acetylation in chromatin and chromosomes

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7 January 2021

Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei

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7 January 2021

Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.

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7 January 2021

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

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7 January 2021

Silver staining of proteins in polyacrylamide gels

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7 January 2021

Recruiting TATA-binding protein to a promoter: transcriptional activation without an upstream activator

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7 January 2021

Novel substrate specificity of the histone acetyltransferase activity of HIV-1-Tat interactive protein Tip60

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https://api.crossref.org/works/10.1016%2FS1097-2765%2800%2980431-1

7 January 2021

10.1016/S1097-2765(00)80431-1

Identifiers

DOI

1 reference

3 May 2018

PubMed ID

10882077

1 reference

3 May 2018