Chromatin superstructure. A study with an immobilized trypsin

S. I. Dimitrov; T. M. Apostolova; V. L. Makarov; I. G. Pashev

doi:10.1016/0014-5793(86)81161-9

Chromatin superstructure. A study with an immobilized trypsin

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

Research output: Contribution to journal › Article

10 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	322-326
Number of pages	5
Journal	FEBS Letters
Volume	200
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(86)81161-9
Publication status	Published - 12 May 1986

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Keywords

Chromatin structure
Flow linear dichroism
Immobilized enzyme
Light scattering
Trypsin

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Cite this

Dimitrov, S. I., Apostolova, T. M., Makarov, V. L., & Pashev, I. G. (1986). Chromatin superstructure. A study with an immobilized trypsin. FEBS Letters, 200(2), 322-326. https://doi.org/10.1016/0014-5793(86)81161-9

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10.1016/0014-5793(86)81161-9