Chromatin superstructure

FEBS Letters

Pashev, I.G.¹  Dimitrov, S.I.¹  Makarov, V.L.²  Apostolova, T.M.¹ 

[1] Institute of Molecular Biology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria;Institute of Molecular Biology, USSR Academy of Sciences, Moscow, USSR

关键词: Chromatin structure;    Immobilized enzyme;    Trypsin;    Light scattering;    Flow linear dichroism;    LD;    linear dichroism;   

DOI  :  10.1016/0014-5793(86)81161-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hen erythrocyte chromatin was treated with trypsin immobilized on collagen membranes and the unfolding of chromatin fiber was followed by light scattering at 90° and flow linear dichroism. Chromatin was found almost completely decondensed when the bulk of H1 and H5 was digested while H3 was still intact. Further digestion leading to degradation of both H3 and the rest of H1 and H5 accounted for no more than 10–15% of the total effect. When chromatin with trypsin-cleaved H1 and H5 was titrated with increasing amounts of spermidine it folded similarly to the control sample. This finding suggests that charge neutralization appears a likely mechanism for maintaining the structure of the 30 nm chromatin fiber by the C-terminal domain of H1 and H5.

【 授权许可】

Unknown