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富含赖氨酸的组蛋白H1(F1)在真核生物染色质中的作用及作用模式研究。染色质及H1 - DNA复合物中的组蛋白H1。

Studies on the role and mode of operation of the very-lysine-rich histone H1 (F1) in eukaryote chromatin. Histone H1 in chromatin and in H1 - DNA complexes.

作者信息

Bradbury E M, Danby S E, Rattle H W, Giancotti V

出版信息

Eur J Biochem. 1975 Sep 1;57(1):97-105. doi: 10.1111/j.1432-1033.1975.tb02280.x.

Abstract

The nuclear magnetic resonance (NMR) spectrum of chromatin at ionic strengths below about 0.5 M may be attributed solely to its histone H1 component. The effect of various ions and urea on the complex has been investigated using NMR and confirm that the contraction of the complex on increase of ionic strength is largely due to electrostatic interactions. A detailed study of the H1 - DNA complex has also been undertaken. The behaviour of H1 in the two cases is virtually identical, implying that in chromatin the H1 is complexed with the DNA rather than with the other histones. Microcalorimetric measurements reveal that the binding of H1 to DNA is athermic or involves a heat of reaction which is very small indeed.

摘要

在离子强度低于约0.5M时,染色质的核磁共振(NMR)谱可能仅归因于其组蛋白H1成分。已使用NMR研究了各种离子和尿素对该复合物的影响,并证实随着离子强度增加复合物的收缩主要是由于静电相互作用。还对H1-DNA复合物进行了详细研究。在这两种情况下H1的行为几乎相同,这意味着在染色质中H1与DNA而非其他组蛋白形成复合物。微量量热法测量表明,H1与DNA的结合是无热的,或者涉及的反应热确实非常小。

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