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NAP1 Modulates Binding of Linker Histone H1 to Chromatin and Induces an Extended Chromatin Fiber Conformation

Kepert, J. Felix and Mazurkiewicz, Jacek and Heuvelman, Gerrit L. and Fejes Tóth, Katalin and Rippe, Karsten (2005) NAP1 Modulates Binding of Linker Histone H1 to Chromatin and Induces an Extended Chromatin Fiber Conformation. Journal of Biological Chemistry, 280 (40). pp. 34063-34072. ISSN 0021-9258. doi:10.1074/jbc.m507322200.

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NAP1 (nucleosome assembly protein 1) is a histone chaperone that has been described to bind predominantly to the histone H2A·H2B dimer in the cell during shuttling of histones into the nucleus, nucleosome assembly/remodeling, and transcription. Here it was examined how NAP1 interacts with chromatin fibers isolated from HeLa cells. NAP1 induced a reversible change toward an extended fiber conformation as demonstrated by sedimentation velocity ultracentrifugation experiments. This transition was due to the removal of the linker histone H1. The H2A·H2B dimer remained stably bound to the native fiber fragments and to fibers devoid of linker histone H1. This was in contrast to mononucleosome substrates, which displayed a NAP1-induced removal of a single H2A·H2B dimer from the core particle. The effect of NAP1 on the chromatin fiber structure was examined by scanning/atomic force microscopy. A quantitative image analysis of ∼36,000 nucleosomes revealed an increase of the average internucleosomal distance from 22.3 ± 0.4 to 27.6 ± 0.6 nm, whereas the overall fiber structure was preserved. This change reflects the disintegration of the chromatosome due to binding of H1 to NAP1 as chromatin fibers stripped from H1 showed an average nucleosome distance of 27.4 ± 0.8 nm. The findings suggest a possible role of NAP1 in chromatin remodeling processes involved in transcription and replication by modulating the local linker histone content.

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Fejes Tóth, Katalin0000-0001-6558-2636
Additional Information:© 2005 The American Society for Biochemistry and Molecular Biology, Inc. Received July 6, 2005; Revision received August 11, 2005; First Published on August 16, 2005. We thank Peter Lichter, Malte Wachsmuth, Gernot Längst, Olaf Thürigen, Claudio Rivetti, and Lutz Ehrhardt for help and discussions and Karolin Luger and Tom Owen-Hughes for providing plasmid vectors. The insightful comments of the anonymous reviewer of a previous manuscript version are gratefully acknowledged. This work was supported by the Volkswagen Foundation Program “Junior Research Groups at German Universities” and Deutsche Forschungsgemeinschaft Research Training Group “Molecular Imaging Methods for the Analysis of Gene and Protein Expression” Grant GRK 886/1. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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Volkswagen FoundationUNSPECIFIED
Deutsche Forschungsgemeinschaft (DFG)GRK 886/1
Issue or Number:40
Record Number:CaltechAUTHORS:20200421-085839554
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:102689
Deposited By: Tony Diaz
Deposited On:21 Apr 2020 16:09
Last Modified:16 Nov 2021 18:14

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