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PMID: 2444434 Published · ppublish English Journal Article

The globular domain of histone H5 is internally located in the 30 nm chromatin fiber: an immunochemical study.

The EMBO journal ·Vol. 6 ·No. 8 ·1987-08-00 ·Pages 2387-92

Dimitrov SI, Russanova VR, Pashev IG

Abstract

The location of the globular domain of histone H5 relative to the axis of the 30 nm chromatin fiber was investigated by following the accessibility of this region of the molecule in chicken erythrocyte chromatin to specific antibodies as a function of chromatin structure. Antibodies to the globular domain of H5 as well as their Fab fragments were found to react with chromatin at ionic strengths ranging from 1-80 mM NaCl, the reaction gradually decreasing upon increase of salt concentration. If, however, Fab fragments were conjugated to ferritin, no reaction of the complex with chromatin was observed at salt concentrations higher than 20 mM. The accessibility of the globular part of H5 in unfolded chromatin to the Fab-ferritin complex was also demonstrated with trypsin-digested chromatin. The experiments were carried out by both solid-phase immunoassay and inhibition experiments. The data obtained are consistent with a structure in which the globular domain of H5 is internally located in the 30 nm chromatin fiber.

MeSH Terms
Animals Antibodies Chickens Chromatin/analysis Enzyme-Linked Immunosorbent Assay Epitopes/analysis Erythrocytes/analysis Histones/blood,immunology Immunoglobulin Fab Fragments
Chemicals
Antibodies Chromatin Epitopes Histones Immunoglobulin Fab Fragments
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Dimitrov S I
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia.
Russanova V R
Pashev I G
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1987-08-00
Pages
2387-92
Language
English
Region
England
NLM ID
8208664
PMCID
PMC553644
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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