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PMID: 7188348 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Immunochemical localization of the C-terminal hexapeptide of histone H3 at the surface of chromatin subunits.

The EMBO journal ·Vol. 1 ·No. 4 ·1982-00-00 ·Pages 421-5

Muller S, Himmelspach K, Van Regenmortel MH

Abstract

The C-terminal hexapeptide of histone H3 of chicken erythrocytes (residues 130-135) corresponding to the sequence Ile-Arg-Gly-Glu-Arg-Ala ( IRGERA ) was prepared by solid-phase peptide synthesis and, after coupling to bovine serum albumin, was used to elicit antibodies in rabbits. The antigenic activity of the synthetic peptide IRGERA was found to be very similar to that of the natural CN3 fragment (residues 121-135), and it inhibited the H3-anti H3 reaction in complement fixation, solid-phase radioimmunoassay, and enzyme-linked immunosorbent assay. Antibodies induced by IRGERA were found to bind equally well to IRGERA coupled to hemocyanin, to the intact H3 molecule, and to chromatin subunits (nucleosomes and core particles). The results demonstrate that the C-terminal hexapeptide of histone H3 is located at the surface of chromatin subunits and agree with current models proposed for the spatial organization of the chromatin core particle.

MeSH Terms
Amino Acid Sequence Animals Chickens Chromatin/analysis Complement Fixation Tests Enzyme-Linked Immunosorbent Assay Erythrocytes/analysis Histones/analysis Immune Sera Oligopeptides/analysis,chemical synthesis Peptide Fragments/analysis Radioimmunoassay
Chemicals
Chromatin Histones Immune Sera Oligopeptides Peptide Fragments
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Muller S
Himmelspach K
Van Regenmortel M H
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39 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1982-00-00
Pages
421-5
Language
English
Region
England
NLM ID
8208664
PMCID
PMC553062
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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