期刊
MOLECULAR CELL
卷 41, 期 4, 页码 398-408出版社
CELL PRESS
DOI: 10.1016/j.molcel.2011.01.025
关键词
-
资金
- Wellcome Trust [064414]
- Biotechnology and Biological Sciences Research Council [BB/E022286/1]
- Engineering and Physical Sciences Research Council [EP/F0390341]
- BBSRC [BB/E022286/1] Funding Source: UKRI
- EPSRC [EP/F039034/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E022286/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/F039034/1] Funding Source: researchfish
Histone chaperones physically interact with histones to direct proper assembly and disassembly of nucleosomes regulating diverse nuclear processes such as DNA replication, promoter remodeling, transcription elongation, DNA damage, and histone variant exchange. Currently, the best-characterized chaperone-histone interaction is that between the ubiquitous chaperone Asf1 and a dimer of H3 and H4. Nucleosome assembly proteins (Nap proteins) represent a distinct class of histone chaperone. Using pulsed electron double resonance (PELDOR) measurements and protein crosslinking, we show that two members of this class, Nap1 and Vps75, bind histones in the tetrameric conformation also observed when they are sequestered within the nucleosome. Furthermore, H3 and H4 trapped in their tetrameric state can be used as substrates in nucleosome assembly and chaperone-mediated lysine acetylation. This alternate mode of histone interaction provides a potential means of maintaining the integrity of the histone tetramer during cycles of nucleosome reassembly.
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