Core histone N-termini play an essential role in mitotic chromosome condensation.
We have studied the role of core histone tails in the assembly of mitotic chromosomes using Xenopus egg extracts. Incubation of sperm nuclei in the extracts led to the formation of mitotic chromosomes, a process we found to be correlated with phosphorylation of the N-terminal tail of histone H3 at Ser10. When the extracts were supplemented with H1-depleted oligosomes, they were not able to assemble chromosomes. Selective elimination of oligosome histone tails by trypsin digestion resulted in a dramatic decrease in their ability to inhibit chromosome condensation. The chromosome assembly was also inhibited by each of the histone tails with differing efficiency. In addition, we found that nucleosomes were recruiting through the flexible histone tails some chromosome assembly factors, different from topoisomerase II and 13S condensin. These findings demonstrate that histone tails play an essential role in chromosome assembly. We also present evidence that the nucleosomes, through physical association, were able to deplete the extracts from the kinase phosphorylating histone H3 at Ser10, suggesting that this kinase could be important for chromosome condensation.
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Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, équipe Mécanismes d'Assemblage du Matériel Génétique, INSERM U 309, Institut Albert Bonniot, Domaine de la Merci, 38706 La Tronche, Cedex, France.
Gerson
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Gout
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Creaven
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Allis
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Dimitrov
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D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D006690:Bisbenzimidazole; D002457:Cell Extracts; D002875:Chromosomes / Q000737:chemistry*; D004247:DNA / Q000378:metabolism; D004250:DNA Topoisomerases, Type II / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000235:genetics; D008297:Male; D008856:Microscopy, Fluorescence; D008938:Mitosis; D046912:Multiprotein Complexes; D009154:Mutation; D009687:Nuclear Proteins / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism; D009865:Oocytes; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013094:Spermatozoa; D014357:Trypsin / Q000378:metabolism; D014981:Xenopus
D002457:Cell Extracts; D004268:DNA-Binding Proteins; D006657:Histones; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D009707:Nucleosomes; D011993:Recombinant Fusion Proteins; C108312:condensin complexes; D004247:DNA; D011494:Protein Kinases; D014357:Trypsin; D000251:Adenosine Triphosphatases; D004250:DNA Topoisomerases, Type II; D006690:Bisbenzimidazole