Role of histones H1 and H3 in the maintenance of chromatin in a compact conformation

FEBS Letters

Coulet, Pierre R.¹  Marion, Christian²  Roux, Bernard² 

[1] Laboratoire de Biologie et de Technologie des Membranes du CNRS, Université Claude Bernard, Lyon I, 43, Bd. du 11 Novembre 1918, 69622 Villeurbanne Cedex, France;Laboratoire de Physico-chimie Biologique Villeurbanne Cedex, France

关键词: Chromatin structure;    Histone H1;    Histone H3;    Trypsin digestion;    Immobilized enzyme;    Enzymatic collagen membrane;    PMSF;    phenylmethylsulfonyl fluoride;    EDTA;    ethylenediamine tetraacetic acid;    TAME;    p-toluene sulfonyl-L-arginine methyl ester;    CD;    circular dichroism;   

DOI  :  10.1016/0014-5793(83)80568-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Chromatin polynucleosomes have been digested with trypsin immobilized on collagen membranes. This method allows the mild removal of the most accessible histone fragments simply by dipping the enzymatic membrane into the chromatin solution, without modification of its ionic and chemical composition. These results demonstrate that the removal of H1 does not affect the higher-order structure of chromatin and that only the elimination of the terminal regions of H3 leads to the unfolding of H1-depleted fibres. This observation suggests that structural changes reported in many previous works were not due to only the removal of H1 but to a concomitant unbinding from DNA of the N-terminal domain of H3.

【 授权许可】

Unknown