Linker histones H1 and H5 prevent the mobility of positioned nucleosomes

Journal Article · Tue Oct 25 04:00:00 EDT 1994 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

DOI:https://doi.org/10.1073/pnas.91.22.10275· OSTI ID:6701355

Pennings, S; Meersseman, G ^[1]; Bradbury, E M ^[2]

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1. Univ. of California, Davis, CA (United States)
2. Univ. of California, Davis, CA (United States) Los Alamos National Lab., NM (United States)

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. 42 refs., 2 figs.

• DOE Contract Number: FG03-88ER60673
• OSTI ID: 6701355
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 91:22; ISSN PNASA6; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
CHROMATIN
COMPARATIVE EVALUATIONS
DNA
EVALUATION
HISTONES
INHIBITION
MOBILITY
NUCLEIC ACIDS
NUCLEOSOMES
ORGANIC COMPOUNDS