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• W2003727007 startingPage "591" @default.
• W2003727007 abstract "Peptides derived from calf thymus H1 and rat liver H1, comprising only the globular and COOH-terminal domains of the intact molecule and therefore lacking NH2-terminal domains, have been shown by reconstitution to be as effective as the complete H1 molecule in inducing higher-order-chromatin structure. As the globular domain of H1 alone cannot induce chromatin folding, our results demonstrate that this function is primarily controlled by the COOH-terminal domain of the molecule. Surprisingly, these peptides do not locate correctly with respect to the nucleosome. This is demonstrated by their failure to confer upon reconstitutes the ability to protect DNA fragments of chromatosome length when digested with micrococcal nuclease. The precise placement of the H1 molecule (globular domain) with respect to the nucleosome is shown to be influenced by the tail domains of both H1 and the core histones." @default.
• W2003727007 created "2016-06-24" @default.
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• W2003727007 date "1986-02-01" @default.
• W2003727007 modified "2023-10-10" @default.
• W2003727007 title "Roles of H1 domains in determining higher order chromatin structure and H1 location" @default.
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• W2003727007 doi "https://doi.org/10.1016/0022-2836(86)90337-2" @default.
• W2003727007 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3458926" @default.
• W2003727007 hasPublicationYear "1986" @default.
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