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Molecular and Cellular Biology, January 2009, p. 57-67, Vol. 29, No. 1
0270-7306/09/$08.00+0     doi:10.1128/MCB.00989-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Monomethylation of Lysine 20 on Histone H4 Facilitates Chromatin Maturation{triangledown}

Annette N. D. Scharf,1 Karin Meier,2 Volker Seitz,1,{dagger} Elisabeth Kremmer,3 Alexander Brehm,2 and Axel Imhof1*

Munich Centre of Integrated Protein Science and Adolf-Butenandt Institute, Ludwig Maximilians University of Munich, Schillerstr. 44, 80336 Munich, Germany,1 Institut für Molekularbiologie und Tumorforschung (IMT), Philipps-Universtät Marburg, Emil-Mannkopff-Str. 2, 35033 Marburg, Germany,2 Helmholtz Zentrum München, Institute of Molecular Immunology, Marchioninistraße 25, 81377 Munich, Germany3

Received 23 June 2008/ Returned for modification 6 August 2008/ Accepted 22 October 2008

Histone modifications play an important role in shaping chromatin structure. Here, we describe the use of an in vitro chromatin assembly system from Drosophila embryo extracts to investigate the dynamic changes of histone modifications subsequent to histone deposition. In accordance with what has been observed in vivo, we find a deacetylation of the initially diacetylated isoform of histone H4, which is dependent on chromatin assembly. Immediately after deposition of the histones onto DNA, H4 is monomethylated at K20, which is required for an efficient deacetylation of the H4 molecule. H4K20 methylation-dependent dl(3)MBT association with chromatin and the identification of a dl(3)MBT-dRPD3 complex suggest that a deacetylase is specifically recruited to the monomethylated substrate through interaction with dl(3)MBT. Our data demonstrate that histone modifications are added and removed during chromatin assembly in a highly regulated manner.

* Corresponding author. Mailing address: Histone Modifications Group, Munich Centre of Integrated Protein Science and Adolf-Butenandt Institute, Ludwig Maximilians University of Munich, Schillerstr. 44, 80336 Munich, Germany. Phone: 49 89 218075420. Fax: 49 89 218075440. E-mail: Imhof{at}lmu.de

{triangledown} Published ahead of print on 10 November 2008.

{dagger} Present address: Universitätsklinikum Heidelberg, Klinik für Anaesthesiologie, Im Neuenheimer Feld 110, 69120 Heidelberg, Germany.

Molecular and Cellular Biology, January 2009, p. 57-67, Vol. 29, No. 1
0270-7306/09/$08.00+0     doi:10.1128/MCB.00989-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Scharf, A. N. D., Barth, T. K., Imhof, A. (2009). Establishment of Histone Modifications after Chromatin Assembly. Nucleic Acids Res 37: 5032-5040 [Abstract] [Full Text]  


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