Alterations in nucleosome core structure in linker histone-depleted chromatin.
We have previously shown that the sequential arrangement of histone-DNA contacts is essentially the same in the nucleosomal core of sea urchin sperm nuclei, where chromatin is highly condensed and repressed, and in nuclei from lily bud sepals or yeast, where chromatin is highly active in transcription and replication and is significantly or completely depleted of histone H1. However, the difference in the strength of some histone-DNA contacts has not been understood or discussed. In this work, we demonstrate that some of these differences are due to a conformational change in the nucleosomal core. We show that the nucleosomal core in linker histone-depleted chromatin is in a different conformational state compared with the nucleosomal core in folded chromatin or in isolated core nucleosomes. This conformational state is characterized by altered strengths in the histone H4 and H2A/H2B contacts with the regions of sharply bent nucleosomal DNA around sites +/-1 and +/-4 and site +/-5, respectively. We demonstrate that this conformation, which we call the "stretched nucleosome," is a general feature of unfolded linker histone-depleted chromatin and may occur during chromatin activation. Our results suggest that this nucleosome structural alteration does not depend on chromatin sources and histone variants studied in this work. In addition, we show that this alteration is reversible and is caused by the stretching of linker DNA during chromatin unfolding.
Usachenko
S I
SI
W. A. Engelhardt Institute of Molecular Biology, Academy of Sciences of Russia, Vavilova, 32, 117984 Moscow B-334, Russia.
Gavin
I M
IM
Bavykin
S G
SG
D000818:Animals; D001665:Binding Sites; D002467:Cell Nucleus / Q000648:ultrastructure*; D002645:Chickens; D002843:Chromatin / Q000648:ultrastructure*; D004247:DNA / Q000737:chemistry* / Q000302:isolation & purification; D004912:Erythrocytes / Q000648:ultrastructure; D006657:Histones / Q000737:chemistry* / Q000302:isolation & purification; D008297:Male; D051379:Mice; D008961:Models, Structural; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000648:ultrastructure*; D010944:Plants; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae; D012617:Sea Urchins; D013094:Spermatozoa / Q000648:ultrastructure
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D004247:DNA