Role of histones H1 and H3 in the maintenance of chromatin in a compact conformation: Study with an immobilized enzyme

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....

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Bibliographic Details
Published in:FEBS letters 1983-07, Vol.157 (2), p.317-321
Main Authors: Marion, Christian, Roux, Bernard, Coulet, Pierre R.
Format: Article
Language:English
Subjects:
Animals
Chromatin - ultrastructure
Chromatin structure
Circular Dichroism
Enzymatic collagen membrane
Enzymes, Immobilized - metabolism
Histone H1
Histone H3
Histones - physiology
Immobilized enzyme
Rats
Trypsin - metabolism
Trypsin digestion
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Summary: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(83)80568-7