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Literature DB >> 10949041

Mediator-nucleosome interaction.

Y Lorch¹, J Beve, C M Gustafsson, L C Myers, R D Kornberg.

Abstract

Mediator, a multiprotein complex involved in the regulation of RNA polymerase II transcription, binds to nucleosomes and acetylates histones. Three lines of evidence identify the Nut1 subunit of Mediator as responsible for the histone acetyltransferase (HAT) activity. An "in-gel" HAT assay reveals a single band of the appropriate size. Sequence alignment shows significant similarity of Nut1 to the GCN5-related N-acetyltransferase superfamily. Finally, recombinant Nut1 exhibits HAT activity in an in-gel assay.

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Year: 2000 PMID： 10949041 DOI： 10.1016/s1097-2765(00)00021-6

Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970

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Cited

28 in total

Mediator-nucleosome interaction.

1. SWI/SNF-dependent chromatin remodeling of RNR3 requires TAF(II)s and the general transcription machinery.

Review 2. Multi-protein complexes in eukaryotic gene transcription.

3. Cooperative activity of cdk8 and GCN5L within Mediator directs tandem phosphoacetylation of histone H3.

4. Chromatin potentiates transcription.

Review 5. Mechanisms of Mediator complex action in transcriptional activation.

6. Mediator influences telomeric silencing and cellular life span.

Review 7. Transcription regulation by the Mediator complex.

8. Histone H3 specific acetyltransferases are essential for cell cycle progression.

9. Role of an ING1 growth regulator in transcriptional activation and targeted histone acetylation by the NuA4 complex.

10. Activation domain-mediator interactions promote transcription preinitiation complex assembly on promoter DNA.