Interaction of RNA polymerase II with acetylated nucleosomal core particles.


Journal Article

Chemical acetylation of nucleosomal cores is accompanied by an increase in their efficiency as in vitro transcription templates. Low amounts of acetic anhydride cause preferential modification of the amino-terminal tails of core histones. Modification of these domains, which causes moderate structural effects, is apparently correlated with the observed stimulation of RNA synthesis. In contrast, extensive modification of the globular regions of core histones, which is accompanied by a large structural relaxation of the particle, causes little additional effect on transcription. Acetylation of the amino-terminal domains of histones might stimulate transcription by changing the interaction of the histone tails with components of the transcriptional machinery.

Full Text

Duke Authors

Cited Authors

  • Piñeiro, M; González, PJ; Hernández, F; Palacián, E

Published Date

  • May 31, 1991

Published In

Volume / Issue

  • 177 / 1

Start / End Page

  • 370 - 376

PubMed ID

  • 1710452

Pubmed Central ID

  • 1710452

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/0006-291x(91)91993-m


  • eng

Conference Location

  • United States