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Molecular and Cellular Biology, January 2009, p. 538-546, Vol. 29, No. 2
0270-7306/09/$08.00+0     doi:10.1128/MCB.01343-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays {triangledown}

Pu-Yeh Kan,1 Tamara L. Caterino,2 and Jeffrey J. Hayes2*

Department of Biochemistry and Biophysics,2 Department of Pathology, University of Rochester, Rochester, New York 146421

Received 22 August 2008/ Returned for modification 29 September 2008/ Accepted 28 October 2008

The condensation of nucleosome arrays into higher-order secondary and tertiary chromatin structures likely involves long-range internucleosomal interactions mediated by the core histone tail domains. We have characterized interarray interactions mediated by the H4 tail domain, known to play a predominant role in the formation of such structures. We find that the N-terminal end of the H4 tail mediates interarray contacts with DNA during self-association of oligonucleosome arrays similar to that found previously for the H3 tail domain. However, a site near the histone fold domain of H4 participates in a distinct set of interactions, contacting both DNA and H2A in condensed structures. Moreover, we also find that H4-H2A interactions occur via an intra- as well as an internucleosomal fashion, supporting an additional intranucleosomal function for the tail. Interestingly, acetylation of the H4 tail has little effect on interarray interactions by itself but overrides the strong stimulation of interarray interactions induced by linker histones. Our results indicate that the H4 tail facilitates secondary and tertiary chromatin structure formation via a complex array of potentially exclusive interactions that are distinct from those of the H3 tail domain.

* Corresponding author. Mailing address: Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642. Fax: (585) 275-6007. E-mail: Jeffrey_Hayes{at}urmc.rochester.edu

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

Molecular and Cellular Biology, January 2009, p. 538-546, Vol. 29, No. 2
0270-7306/09/$08.00+0     doi:10.1128/MCB.01343-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • McBryant, S. J., Klonoski, J., Sorensen, T. C., Norskog, S. S., Williams, S., Resch, M. G., Toombs, J. A. III, Hobdey, S. E., Hansen, J. C. (2009). Determinants of Histone H4 N-terminal Domain Function during Nucleosomal Array Oligomerization: ROLES OF AMINO ACID SEQUENCE, DOMAIN LENGTH, AND CHARGE DENSITY. J. Biol. Chem. 284: 16716-16722 [Abstract] [Full Text]  


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