Libertini L J, Ausió J, van Holde K E, Small E W
Department of Biochemistry and Biophysics, Oregon State University, Corvallis 97331.
Biophys J. 1988 Apr;53(4):477-87. doi: 10.1016/S0006-3495(88)83126-6.
Effects of histone hyperacetylation on transitions of HeLa cell nucleosome core particles were studied. The transitions examined were induced by low salt concentrations, pH, temperature, and nondissociating high salt. Effects of salt dissociation were also examined. The low-salt transition was found to shift to higher ionic strength by approximately three fold for hyperacetylated particles, a change which may be due simply to the increased overall negative charge on the particles caused by acetylation of lysine residues. Some differences were also seen in the way in which core particles refold after exposure to very low salt (which induces a nonreversible change in the particles). Otherwise no significant effects of hyperacetylation were observed.
研究了组蛋白高度乙酰化对HeLa细胞核小体核心颗粒转变的影响。所检测的转变是由低盐浓度、pH值、温度和非解离性高盐诱导的。还检测了盐解离的影响。发现对于高度乙酰化的颗粒，低盐转变向更高离子强度移动了约三倍，这种变化可能仅仅是由于赖氨酸残基乙酰化导致颗粒上整体负电荷增加所致。在核心颗粒暴露于极低盐（这会诱导颗粒发生不可逆变化）后重新折叠的方式上也观察到了一些差异。否则，未观察到高度乙酰化的显著影响。
