This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hartlepp, K. F.
Right arrow Articles by Becker, P. B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hartlepp, K. F.
Right arrow Articles by Becker, P. B.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2005, p. 9886-9896, Vol. 25, No. 22
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.22.9886-9896.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Histone Fold Subunits of Drosophila CHRAC Facilitate Nucleosome Sliding through Dynamic DNA Interactions{ddagger}

Klaus F. Hartlepp,2 Carlos Fernández-Tornero,1 Anton Eberharter,2 Tim Grüne,1,{dagger} Christoph W. Müller,1 and Peter B. Becker2*

European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, 38042 Grenoble, Cedex 9, France,1 Adolf-Butenandt-Institut, Molekularbiologie, Ludwig-Maximilians-Universität, 80336 München, Germany2

Received 4 May 2005/ Returned for modification 6 July 2005/ Accepted 25 August 2005

The chromatin accessibility complex (CHRAC) is an abundant, evolutionarily conserved nucleosome remodeling machinery able to catalyze histone octamer sliding on DNA. CHRAC differs from the related ACF complex by the presence of two subunits with molecular masses of 14 and 16 kDa, whose structure and function were not known. We determined the structure of Drosophila melanogaster CHRAC14-CHRAC16 by X-ray crystallography at 2.4-Å resolution and found that they dimerize via a variant histone fold in a typical handshake structure. In further analogy to histones, CHRAC14-16 contain unstructured N- and C-terminal tail domains that protrude from the handshake structure. A dimer of CHRAC14-16 can associate with the N terminus of ACF1, thereby completing CHRAC. Low-affinity interactions of CHRAC14-16 with DNA significantly improve the efficiency of nucleosome mobilization by limiting amounts of ACF. Deletion of the negatively charged C terminus of CHRAC16 enhances DNA binding 25-fold but leads to inhibition of nucleosome sliding, in striking analogy to the effect of the DNA chaperone HMGB1 on nucleosome sliding. The presence of a surface compatible with DNA interaction and the geometry of an H2A-H2B heterodimer may provide a transient acceptor site for DNA dislocated from the histone surface and therefore facilitate the nucleosome remodeling process.

* Corresponding author. Mailing address: Adolf-Butenandt-Institut, Molekularbiologie, Schillerstr. 44, 80336 München, Germany. Phone: 49-218075-427. Fax: 49-218075-425. E-mail: pbecker{at}med.uni-muenchen.de.

{ddagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{dagger} Present address: Lehrstuhl für Strukturchemie, Georg-August-Universität, Tammannstr. 4, 37077 Göttingen, Germany.

Molecular and Cellular Biology, November 2005, p. 9886-9896, Vol. 25, No. 22
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.22.9886-9896.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Walker, P., Doenecke, D., Kahle, J. (2009). Importin 13 Mediates Nuclear Import of Histone Fold-containing Chromatin Accessibility Complex Heterodimers. J. Biol. Chem. 284: 11652-11662 [Abstract] [Full Text]  
  • Gatta, R., Mantovani, R. (2008). NF-Y substitutes H2A-H2B on active cell-cycle promoters: recruitment of CoREST-KDM1 and fine-tuning of H3 methylations. Nucleic Acids Res 36: 6592-6607 [Abstract] [Full Text]  
  • Dang, W., Kagalwala, M. N., Bartholomew, B. (2007). The Dpb4 Subunit of ISW2 Is Anchored to Extranucleosomal DNA. J. Biol. Chem. 282: 19418-19425 [Abstract] [Full Text]  
  • Eskeland, R., Eberharter, A., Imhof, A. (2007). HP1 Binding to Chromatin Methylated at H3K9 Is Enhanced by Auxiliary Factors. Mol. Cell. Biol. 27: 453-465 [Abstract] [Full Text]  
  • Tsubota, T., Tajima, R., Ode, K., Kubota, H., Fukuhara, N., Kawabata, T., Maki, S., Maki, H. (2006). Double-stranded DNA Binding, an Unusual Property of DNA Polymerase {epsilon}, Promotes Epigenetic Silencing in Saccharomyces cerevisiae. J. Biol. Chem. 281: 32898-32908 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»