DOI: 10.1042/bj2770607. ADP-ribosylation of core histones and their acetylated subspecies

ADP-ribosylation of core histones and their acetylated subspecies

10.1042/bj2770607

Crossref journal-article

Portland Press Ltd.

Biochemical Journal (288)

Abstract

ADP-ribosylation of core histones was investigated in isolated nuclei of Physarum polycephalum. Core histone species differed in the mode of modification. Whereas ADP-ribosylation of H2A and H2B is sensitive to inhibition by 3-methoxybenzamide, as with most other nuclear acceptor proteins, the modification of H3 and H4 is not inhibited. Cleavage experiments with hydroxylamine indicate a carboxylate ester type ADP-ribose-protein bond for H2A and H2B and arginine-linked ADP-ribose residues for H3 and H4. ADP-ribosylation preferentially occurs on acetylated histone subspecies, as shown for H4. These data are substantiated by the use of n-butyrate, which induces hyperacetylation of core histones; the butyrate-induced shift towards more acetylated H4 subspecies is accompanied by an increase of ADP-ribose incorporation into highly acetylated H4 subspecies.

Bibliography

Golderer, G., & GrÃ¶bner, P. (1991). ADP-ribosylation of core histones and their acetylated subspecies. Biochemical Journal, 277(3), 607â610.

Authors 2

G Golderer (first)
P Gröbner (additional)

References 0 Referenced 22

None

Dates

Type	When
Created	10 years ago (Aug. 10, 2015, 5:22 p.m.)
Deposited	3 years, 9 months ago (Nov. 23, 2021, 5:04 p.m.)
Indexed	1 month, 3 weeks ago (July 2, 2025, 3:10 p.m.)
Issued	34 years ago (Aug. 1, 1991)
Published	34 years ago (Aug. 1, 1991)
Published Print	34 years ago (Aug. 1, 1991)

Funders 0

None

BibTeX

@article{Golderer_1991, title={ADP-ribosylation of core histones and their acetylated subspecies}, volume={277}, ISSN={1470-8728}, url={http://dx.doi.org/10.1042/bj2770607}, DOI={10.1042/bj2770607}, number={3}, journal={Biochemical Journal}, publisher={Portland Press Ltd.}, author={Golderer, G and Gröbner, P}, year={1991}, month=aug, pages={607–610} }

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