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dc.contributor.authorBharath, M M S-
dc.contributor.authorChandra, Nagasuma R-
dc.contributor.authorRao, M R S-
dc.date.accessioned2012-02-14T11:28:35Z-
dc.date.available2012-02-14T11:28:35Z-
dc.date.issued2003-07-15-
dc.identifier0305-1048en_US
dc.identifier.citationNucleic Acids Research 31(14), 4264-4274 (2003)en_US
dc.identifier.urihttp://hdl.handle.net/10572/417-
dc.description.abstractIn an effort to understand the role of the linker histone in chromatin folding, its structure and location in the nucleosome has been studied by molecular modeling methods. The structure of the globular domain of the rat histone H1d, a highly conserved part of the linker histone, built by homology modeling methods, revealed a three-helical bundle fold that could be described as a helix-turn-helix variant with its characteristic properties of binding to DNA at the major groove. Using the information of its preferential binding to four-way Holliday junction (HJ) DNA, a model of the domain complexed to HJ was built, which was subsequently used to position the globular domain onto the nucleosome. The model revealed that the primary binding site of the domain interacts with the extra 20 bp of DNA of the entering duplex at the major groove while the secondary binding site interacts with the minor groove of the central gyre of the DNA superhelix of the nucleosomal core. The positioning of the globular domain served as an anchor to locate the C-terminal domain onto the nucleosome to obtain the structure of the chromatosome particle. The resulting structure had a stem-like appearance, resembling that observed by electron microscopic studies. The C-terminal domain which adopts a high mobility group (HMG)-box-like fold, has the ability to bend DNA, causing DNA condensation or compaction. It was observed that the three S/TPKK motifs in the C-terminal domain interact with the exiting duplex, thus defining the path of linker DNA in the chromatin fiber. This study has provided an insight into the probable individual roles of globular and the C-terminal domains of histone H1 in chromatin organization.en_US
dc.description.urihttp://dx.doi.org/10.1093/nar/gkg481en_US
dc.language.isoenen_US
dc.publisherOxford University Pressen_US
dc.rights© 2003 Oxford University Pressen_US
dc.subjectHigher-Order Structureen_US
dc.subjectGlobular Domainen_US
dc.subjectHolliday Junctionen_US
dc.subjectLinker Dnaen_US
dc.subjectHistone H1en_US
dc.subjectCrystal-Structureen_US
dc.subjectCryoelectron Microscopyen_US
dc.subjectNucleosome Bindingen_US
dc.subjectH5en_US
dc.subjectIdentificationen_US
dc.titleMolecular modeling of the chromatosome particleen_US
dc.typeArticleen_US
Appears in Collections:Research Papers (M.R.S. Rao)

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