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

page(s)

367-375

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3 May 2018

issue

2

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

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

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

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PcG complexes and chromatin silencing

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

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

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Histone acetylation in chromatin and chromosomes

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

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

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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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Silver staining of proteins in polyacrylamide gels

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

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

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10.1016/S1097-2765(00)80431-1

Identifiers

DOI

1 reference

3 May 2018

PubMed ID

10882077

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3 May 2018