期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 278, 期 3, 页码 1504-1510出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M209355200
关键词
-
资金
- NCI NIH HHS [CA42567] Funding Source: Medline
The nature of histone acetylation events in active chromatin is an important issue in transcriptional regulation. We have systematically analyzed the ability of p300, either alone or in response to an interacting activator, to acetylate specific recombinant histones in the context of free histones, histone octamers, or nucleosomal arrays. Our results indicate that p300 has an intrinsic ability to acetylate all core histones but that the level and specificity of histone acetylation is indeed context-dependent. Thus, H3 and H4 are preferentially acetylated in free octamers, whereas all histones are nearly equally acetylated, in an activator-dependent manner, in chromatin. Moreover, H3 and H4 show H2A and H2B tail-independent acetylation in chromatin, whereas maximal H2A and 11213 acetylation in this context is dependent upon H3 and H4 tails (but not their acetylation). In further support of an apparent intrinsic preference of p300 for the H3 and 114 tails, as well as an important role for direct interactions of p300 with unacetylated H3 and H4 tails in both acetylation and transcription, we have shown that p300 selectively acetylates isolated 113 and H4 tails, that p300 strongly and selectively binds to free unacetylated H3 and H4 tails, and that p300-mediated acetylation of nucleosomal histones and transcriptional activation are selectively inhibited by isolated (unacetylated) H3 and H4 tails.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据