Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution.
146 bp core particles were assembled from reconstituted hybrid histone octamers where either histone H2A or H2B were replaced by their ubiquitinated counterparts uH2A and uH2B. No difference in the structure of the core particles was evident upon DNase 1 digestion suggesting that ubiquitination of these histones was not a barrier to normal core particle formation.
Department of Biochemistry, University of Cape Town, South Africa.
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Davies
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Lindsey
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002645:Chickens; D003850:Deoxyribonuclease I; D004912:Erythrocytes / Q000378:metabolism / Q000648:ultrastructure; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000737:chemistry*; D013950:Thymus Gland / Q000378:metabolism / Q000648:ultrastructure; D014452:Ubiquitins / Q000737:chemistry*
D000596:Amino Acids; D006657:Histones; D009707:Nucleosomes; D014452:Ubiquitins; D003850:Deoxyribonuclease I