Chromatin superstructure: A study with an immobilized trypsin

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 in...

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Bibliographic Details
Published in:FEBS letters 1986-05, Vol.200 (2), p.322-326
Main Authors: Dimitrov, S.I., Apostolova, T.M., Makarov, V.L., Pashev, I.G.
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Chickens
Chromatin - analysis
Chromatin structure
Chromatin. Chromosome
Enzymes, Immobilized - pharmacology
Female
Flow linear dichroism
Fundamental and applied biological sciences. Psychology
Histones - metabolism
Immobilized enzyme
Light
Light scattering
Molecular and cellular biology
Molecular genetics
Scattering, Radiation
Trypsin
Trypsin - pharmacology
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(86)81161-9