Effect of high mobility group proteins 14 and 17 on the structural and transcriptional properties of acetylated complete and H2A.H2B-deficient nucleosomal cores.


Journal Article

Acetylation of H2A.H2B-deficient nucleosomal cores, like that of the complete particles, causes a substantial increase in the efficiency of the particles as in vitro transcription templates. Binding of the high mobility group proteins 14 and 17 (HMG 14/17) to chemically acetylated nucleosomal particles, both complete nucleosomal cores and those lacking one of the two H2A.H2B dimers, is accompanied by a small structural stabilization. The affinity of HMG 14/17 for the nucleosomal cores is not affected by acetylation of the particles. With acetylated complete and H2A.H2B-deficient cores, the binding of HMG 14/17 does not cause any significant change in the levels of RNA synthesis, which is compatible with the presence of these proteins in transcriptionally active nucleosomes.

Full Text

Duke Authors

Cited Authors

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

Published Date

  • May 15, 1992

Published In

Volume / Issue

  • 295 / 1

Start / End Page

  • 115 - 119

PubMed ID

  • 1575506

Pubmed Central ID

  • 1575506

International Standard Serial Number (ISSN)

  • 0003-9861

Digital Object Identifier (DOI)

  • 10.1016/0003-9861(92)90495-i


  • eng

Conference Location

  • United States