Effect of DNA length and H4 acetylation on the thermal stability of reconstituted nucleosome particles

被引:14
作者
Siino, JS [1 ]
Yau, PM
Imai, BS
Gatewood, JM
Bradbury, EM
机构
[1] Univ Calif Davis, Dept Microbiol, Davis, CA 95616 USA
[2] Los Alamos Natl Lab, Biosci Div, Los Alamos, NM 87545 USA
[3] SeiraD Inc, Santa Fe, NM 87507 USA
[4] Rockefeller Univ, Prot Resource Ctr, New York, NY 10021 USA
[5] Univ Illinois, Dept Cell & Struct Biol, Urbana, IL 61801 USA
[6] Univ Calif Davis, Sch Med, Dept Biol Chem, Davis, CA 95616 USA
关键词
nucleosome; acetylation; thermal denaturation;
D O I
10.1016/S0006-291X(03)00277-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To examine the factors involved with nucleosome stability, we reconstituted nonacetylated particles containing various lengths (192, 162, and 152 base pairs) of DNA onto the Lytechinus variegatus nucleosome positioning sequence in the absence of linker histone. We characterized the particles and examined their thermal stability. DNA of less than chromatosome length (168 base pairs) produces particles with altered denaturation profiles, possibly caused by histone rearrangement in those core-like particles. We also examined the effects of tetra-acetylation of histone H4 on the thermal stability of reconstituted nucleosome particles. Tetra-acetylation of H4 reduces the nucleosome thermal stability by 0.8degreesC as compared with nonacetylated particles. This difference is close to values published comparing bulk nonacetylated nucleosomes and core particles to ones enriched for core histone acetylation, suggesting that H4 acetylation has a dominant effect on nucleosome particle energetics. (C) 2003 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:885 / 891
页数:7
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