Subcellular localization and nucleosome specificity of yeast histone acetyltransferases

We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present...

Full description

Saved in:
Bibliographic Details
Published inBiochemistry (Easton) Vol. 30; no. 15; pp. 3728 - 3732
Main Authors Lopez-Rodas, Gerardo, Tordera, Vicente, Mateo Sanchez del Pino, M, Franco, Luis
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 16.04.1991
Subjects
Online AccessGet full text

Cover

Loading…
More Information
Summary:We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate both H3 and H4 in nucleosomes. The fourth enzyme, which is located in the cytoplasm, does not accept nucleosomes as substrate, and it represents a canonical type B, H4-specific histone acetyltransferase. Finally, histone deacetylase activity is preferentially found in the nucleus.
Bibliography:ark:/67375/TPS-MWX7NX7B-C
istex:10852E6FB8F38703602E44077B0CE61A053328CF
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00229a020