This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Kan, P.-Y.
Right arrow Articles by Hayes, J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kan, P.-Y.
Right arrow Articles by Hayes, J. J.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, March 2007, p. 2084-2091, Vol. 27, No. 6
0270-7306/07/$08.00+0     doi:10.1128/MCB.02181-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

The H3 Tail Domain Participates in Multiple Interactions during Folding and Self-Association of Nucleosome Arrays{triangledown}

Pu-Yeh Kan,1 Xu Lu,2 Jeffrey C. Hansen,2 and Jeffrey J. Hayes1*

Department of Biochemistry and Biophysics, University of Rochester, Rochester, New York 14642,1 Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-18702

Received 21 November 2006/ Returned for modification 2 January 2007/ Accepted 5 January 2007

The core histone tail domains play a central role in chromatin structure and epigenetic processes controlling gene expression. Although little is known regarding the molecular details of tail interactions, it is likely that they participate in both short-range and long-range interactions between nucleosomes. Previously, we demonstrated that the H3 tail domain participates in internucleosome interactions during MgCl2-dependent condensation of model nucleosome arrays. However, these studies did not distinguish whether these internucleosome interactions represented short-range intra-array or longer-range interarray interactions. To better understand the complex interactions of the H3 tail domain during chromatin condensation, we have developed a new site-directed cross-linking method to identify and quantify interarray interactions mediated by histone tail domains. Interarray cross-linking was undetectable under salt conditions that induced only local folding, but was detected concomitant with salt-dependent interarray oligomerization at higher MgCl2 concentrations. Interestingly, lysine-to-glutamine mutations in the H3 tail domain to mimic acetylation resulted in little or no reduction in interarray cross-linking. In contrast, binding of a linker histone caused a much greater enhancement of interarray interactions for unmodified H3 tails compared to "acetylated" H3 tails. Collectively these results indicate that H3 tail domain performs multiple functions during chromatin condensation via distinct molecular interactions that can be differentially regulated by acetylation or binding of linker histones.

* Corresponding author. Mailing address: Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester NY 14642. Phone: (585) 275-1706. Fax: (585) 275-6007. E-mail: jjhs{at}mail.rochester.edu.

{triangledown} Published ahead of print on 22 January 2007.

Molecular and Cellular Biology, March 2007, p. 2084-2091, Vol. 27, No. 6
0270-7306/07/$08.00+0     doi:10.1128/MCB.02181-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Grigoryev, S. A., Arya, G., Correll, S., Woodcock, C. L., Schlick, T. (2009). Evidence for heteromorphic chromatin fibers from analysis of nucleosome interactions. Proc. Natl. Acad. Sci. USA 106: 13317-13322 [Abstract] [Full Text]  
  • 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]  
  • Wang, Y., Li, M., Stadler, S., Correll, S., Li, P., Wang, D., Hayama, R., Leonelli, L., Han, H., Grigoryev, S. A., Allis, C. D., Coonrod, S. A. (2009). Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. JCB 184: 205-213 [Abstract] [Full Text]  
  • Kan, P.-Y., Caterino, T. L., Hayes, J. J. (2009). The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays. Mol. Cell. Biol. 29: 538-546 [Abstract] [Full Text]  
  • Ujvari, A., Hsieh, F.-K., Luse, S. W., Studitsky, V. M., Luse, D. S. (2008). Histone N-terminal Tails Interfere with Nucleosome Traversal by RNA Polymerase II. J. Biol. Chem. 283: 32236-32243 [Abstract] [Full Text]  
  • McBryant, S. J., Krause, C., Woodcock, C. L., Hansen, J. C. (2008). The Silent Information Regulator 3 Protein, SIR3p, Binds to Chromatin Fibers and Assembles a Hypercondensed Chromatin Architecture in the Presence of Salt. Mol. Cell. Biol. 28: 3563-3572 [Abstract] [Full Text]  
  • Wang, X., Hayes, J. J. (2008). Acetylation Mimics within Individual Core Histone Tail Domains Indicate Distinct Roles in Regulating the Stability of Higher-Order Chromatin Structure. Mol. Cell. Biol. 28: 227-236 [Abstract] [Full Text]  
  • Wang, X., Hayes, J. J. (2007). Site-specific Binding Affinities within the H2B Tail Domain Indicate Specific Effects of Lysine Acetylation. J. Biol. Chem. 282: 32867-32876 [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»