Linker histones H1 and H5 prevent the mobility of positioned nucleosomes.
We have previously identified a generally occurring short-range mobility of nucleosome cores on DNA in relatively low ionic strength conditions. Here we report that this mobility of histone octamers positioned on constructs of 5S rDNA is suppressed by the binding of histone H1 or H5 to the nucleosome. Histone H5 is the more potent inhibitor of nucleosome mobility, in accordance with its higher affinity for chromatin. We propose that this reversible restraint on chromatin dynamics may play a role in local regulation of processes that require access to the DNA.
Pennings
S
S
Department of Biological Chemistry, School of Medicine, University of California, Davis 95616.
Meersseman
G
G
Bradbury
E M
EM
D000818:Animals; D002645:Chickens; D004275:DNA, Ribosomal / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004912:Erythrocytes / Q000737:chemistry / Q000378:metabolism; D006367:HeLa Cells; D006657:Histones / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D009707:Nucleosomes / Q000737:chemistry / Q000502:physiology*; D011485:Protein Binding; D012341:RNA, Ribosomal, 5S / Q000096:biosynthesis; D012617:Sea Urchins
D004275:DNA, Ribosomal; D006657:Histones; D046911:Macromolecular Substances; D009707:Nucleosomes; D012341:RNA, Ribosomal, 5S