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PMID: 11707409 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The N-terminus of histone H2B, but not that of histone H3 or its phosphorylation, is essential for chromosome condensation.

The EMBO journal ·Vol. 20 ·No. 22 ·2001-11-15 ·Pages 6383-93

de la Barre AE, Angelov D, Molla A, Dimitrov S

Abstract

We have studied the role of individual histone N-termini and the phosphorylation of histone H3 in chromosome condensation. Nucleosomes, reconstituted with histone octamers containing different combinations of recombinant full-length and tailless histones, were used as competitors for chromosome assembly in Xenopus egg extracts. Nucleosomes reconstituted with intact octamers inhibited chromosome condensation as efficiently as the native ones, while tailless nucleosomes were unable to affect this process. Importantly, the addition to the extract of particles containing only intact histone H2B strongly interfered with chromosome formation while such an effect was not observed with particles lacking the N-terminal tail of H2B. This demonstrates that the inhibition effect observed in the presence of competitor nucleosomes is mainly due to the N-terminus of this histone, which, therefore, is essential for chromosome condensation. Nucleosomes in which all histones but H3 were tailless did not impede chromosome formation. In addition, when competitor nucleosome particles were reconstituted with full-length H2A, H2B and H4 and histone H3 mutated at the phosphorylable serine 10 or serine 28, their inhibiting efficiency was identical to that of the native particles. Hence, the tail of H3, whether intact or phosphorylated, is not important for chromosome condensation. A novel hypothesis, termed 'the ready production label' was suggested to explain the role of histone H3 phosphorylation during cell division.

MeSH Terms
Animals Binding, Competitive Cell Nucleus/metabolism Chromosomes/metabolism Cysteine Endopeptidases/pharmacology Deoxyribonuclease I/metabolism Fluorescent Antibody Technique, Indirect Histones/chemistry Immunoblotting Kinetics Male Microscopy, Fluorescence Mitosis Models, Biological Mutation Nucleosomes/metabolism Ovum Phosphorylation Protein Structure, Tertiary Recombinant Proteins/metabolism Serine/chemistry,metabolism Spermatozoa/metabolism Time Factors Trypsin/pharmacology Xenopus
Chemicals
Histones Nucleosomes Recombinant Proteins Serine Deoxyribonuclease I Trypsin Cysteine Endopeptidases clostripain
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
de la Barre A E
Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U 309, Institut Albert Bonniot, Domaine de la Merci, 38706 La Tronche, Cedex, France.
Angelov D
Molla A
Dimitrov S
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
2001-11-15
Pages
6383-93
Language
English
Region
England
NLM ID
8208664
PMCID
PMC125309
Subset
IM
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