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PMID: 4066674 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Specific site of histone H3 phosphorylation related to the maintenance of premature chromosome condensation. Evidence for catalytically induced interchange of the subunits.

The Journal of biological chemistry ·Vol. 260 ·No. 29 ·1985-12-15 ·Pages 15379-81

Ajiro K, Nishimoto T

Abstract

Previously we have found that histone H1 and H3 of tsBN2 cells showing premature chromosome condensation (PCC) at nonpermissive temperature (40.5 degrees C) were phosphorylated extensively as in mitotic cells (Ajiro, K., Nishimoto, T., and Takahashi, T. (1983) J. Biol. Chem. 258, 4534-4538). Under the influence of various chemicals, both the prevention of the PCC induction and the suppression of H3 phosphorylation occurred simultaneously, whereas H1 phosphorylation did not. At the minimum concentration for the inhibition of PCC induction, H1 phosphorylation remained at the control level, but H3 phosphorylation was completely suppressed. Tryptic peptide analysis revealed that the H3 phosphopeptide in PCC was single, and it was observed in the same position as in mitosis. The results suggest that specific site(s) of H3 phosphorylation related to the maintenance of a condensed state of chromatin.

MeSH Terms
Binding Sites Cell Line Chlorides Chromosomes/metabolism Electrophoresis, Polyacrylamide Gel Histones/metabolism Phosphopeptides/analysis Phosphorylation Temperature Trypsin/metabolism Zinc/pharmacology Zinc Compounds
Chemicals
Chlorides Histones Phosphopeptides Zinc Compounds zinc chloride Trypsin Zinc
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ajiro K
Nishimoto T
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1985-12-15
Pages
15379-81
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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