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J. Biol. Chem., Vol. 280, Issue 40, 34063-34072, October 7, 2005

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

From the Kirchhoff-Institut für Physik, Molecular Biophysics Group, Ruprecht-Karls-Universität Heidelberg, Im Neuenheimer Feld 227, D-69120 Heidelberg, Germany

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.

Received for publication, July 6, 2005 , and in revised form, August 11, 2005.

^* 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

¹ To whom correspondence should be addressed. Tel.: 49-6221-549270; Fax: 49-6221-549112; E-mail: Karsten.Rippe{at}kip.uni-heidelberg.de.

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