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30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction |
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| Authors: | Robinson Philip J J An Woojin Routh Andrew Martino Fabrizio Chapman Lynda Roeder Robert G Rhodes Daniela |
| Affiliation: | 1 MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK 2 Stanford Medical School, Department of Structural Biology, Fairchild Building, 299 Campus Drive, Stanford, CA 94305, USA 3 Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA 4 Department of Biochemistry and Molecular Biology, USC/Norris Comprehensive Cancer Center, 1501 San Pablo Street, ZNI 241, MC 2821, Los Angeles, CA 90089-2821, USA 5 Division of Epigenetics, Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058, Basel, Switzerland |
| Abstract: | The mechanism by which chromatin is decondensed to permit access to DNA is largely unknown. Here, using a model nucleosome array reconstituted from recombinant histone octamers, we have defined the relative contribution of the individual histone octamer N-terminal tails as well as the effect of a targeted histone tail acetylation on the compaction state of the 30 nm chromatin fiber. This study goes beyond previous studies as it is based on a nucleosome array that is very long (61 nucleosomes) and contains a stoichiometric concentration of bound linker histone, which is essential for the formation of the 30 nm chromatin fiber. We find that compaction is regulated in two steps: Introduction of H4 acetylated to 30% on K16 inhibits compaction to a greater degree than deletion of the H4 N-terminal tail. Further decompaction is achieved by removal of the linker histone. |
| Keywords: | WT, wild type CE, chicken erythrocyte crDNA, competitor DNA TEA, triethanolamine hydrochloride |
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