1998
DOI: 10.1074/jbc.273.48.32236
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Abstract: The binding of all known linker histones, named H1a through H1e, including H1 0 and H1t, to a model chromatin complex based on a DNA fragment containing the mouse mammary tumor virus long terminal repeat promotor was systematically studied. As for the histone subtype H1b, we found a dissociation constant of 8 -16 nM to a single mononucleosome (210 base pairs), whereas the binding constant of all other subtypes varied between 2 and 4 nM. Most of the H1 histones, namely H1a, H1c, H1d/e, and H1 0 , completely agg… Show more

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Cited by 60 publications
(51 citation statements)
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References 51 publications
(25 reference statements)
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“…It was, therefore, surprising, when a previous study comparing the in vivo binding of histone H1 subtypes H10 and H1c, the murine homolog of histone H1.2, failed to observe a significant difference between the two (38). This has been well documented in vitro, where differences between histone H1 subtypes has been shown for both binding and the capacity to aggregate polynucleosomes into condensed structures (39). This implies functional differences between the different histone H1 subtypes, at least in the context of development of a complex organism.…”
Section: Discussionmentioning
confidence: 90%
“…It was, therefore, surprising, when a previous study comparing the in vivo binding of histone H1 subtypes H10 and H1c, the murine homolog of histone H1.2, failed to observe a significant difference between the two (38). This has been well documented in vitro, where differences between histone H1 subtypes has been shown for both binding and the capacity to aggregate polynucleosomes into condensed structures (39). This implies functional differences between the different histone H1 subtypes, at least in the context of development of a complex organism.…”
Section: Discussionmentioning
confidence: 90%
“…The family of H1 histones consists of 7 subtypes, termed H1.1 to H1.5, H1°, and H1t (27), of which the proteins H1.2 and H1.4 are the predominant subtypes in most human cell lines (14,28). They are very basic proteins that exert their structural roles in interacting with DNA at defined positions (29), thereby organizing higher order structures (30).…”
Section: Discussionmentioning
confidence: 99%
“…Core histone preparation, mononucleosome and polynucleosome reconstitution, and binding assays were performed as reported (28), except that all DNA fragments were labeled by using digoxigenin-11-ddUTP (Roche Diagnostics, Indianapolis) as described (29). A comprehensive description of the methods and materials is available in Supporting Methods and Materials, which is published as supporting information on the PNAS web site, www.pnas.org.…”
Section: Methodsmentioning
confidence: 99%