Linker Histones H1 and H5 Prevent the Mobility of Positioned Nucleosomes

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 91; no. 22; pp. 10275 - 10279
• Main Authors: Pennings, Sari, Meersseman, Geert, Bradbury, E. Morton
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 25.10.1994; National Acad Sciences; National Academy of Sciences
• Subjects: Animals; BASIC BIOLOGICAL SCIENCES; Biochemistry; Cellular biology; Chickens; CHROMATIN; COMPARATIVE EVALUATIONS; Deoxyribonucleic acid; Dimers; DNA; DNA, Ribosomal - chemistry; DNA, Ribosomal - isolation & purification; DNA, Ribosomal - metabolism; Electrophoresis; Erythrocytes - chemistry; Erythrocytes - metabolism; EVALUATION; Gels; HeLa Cells; HISTONES; Histones - chemistry; Histones - isolation & purification; Histones - metabolism; Humans; INHIBITION; Macromolecular Substances; MOBILITY; NUCLEIC ACIDS; Nucleoproteins; NUCLEOSOMES; Nucleosomes - chemistry; Nucleosomes - physiology; ORGANIC COMPOUNDS 550200 > Biochemistry; Protein Binding; Proteins; Ribosomal DNA; RNA, Ribosomal, 5S - biosynthesis; Sea Urchins
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.91.22.10275

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.