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PMID: 1268203 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Histone-histone interactions within chromatin. Crosslinking studies using ultraviolet light.

Biochemistry ·Vol. 15 ·No. 9 ·1976-05-04 ·Pages 2002-7

Martinson HG, Shetlar MD, McCarthy BJ

Abstract

Irradiation of either whole cells or chromatin at 280 nm results in the covalent linkage of histones 2A and 2B, presumably at their mutual binding sites. The reaction is specific and proceeds with high yield (about 80%). Irradiation of reconstituted nucleohistone containing only H2A, H2B and DNA also yields the H2A-H2B dimer. The cross-linking event is sensitive to the conformation of the H2A-H2B pair since the histones must be bound to DNA for maximum cross-linking specificity at low ionic strength. However, the histones must first interact with each other before being deposited on the DNA, since separate addition of the histones to the DNA yields no dimer upon irradiation. If irradiation is conducted at 254 nm rather than 280 nm, DNA-histone cross-linking appears to dominate.

MeSH Terms
Binding Sites Cell Line Chromatin/radiation effects,ultrastructure Electrophoresis, Polyacrylamide Gel Histones/radiation effects Macromolecular Substances Protein Binding Protein Conformation Radiation Effects Spectrophotometry, Ultraviolet Ultraviolet Rays
Chemicals
Chromatin Histones Macromolecular Substances
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Martinson H G
Shetlar M D
McCarthy B J
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1976-05-04
Pages
2002-7
Language
English
Region
United States
NLM ID
0370623
Subset
IM
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