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 Howe, L.
Right arrow Articles by Ausió, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Howe, L.
Right arrow Articles by Ausió, J.

 Previous Article  |  Next Article 

Mol Cell Biol, March 1998, p. 1156-1162, Vol. 18, No. 3
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Nucleosome Translational Position, Not Histone Acetylation, Determines TFIIIA Binding to Nucleosomal Xenopus laevis 5S rRNA Genes

LeAnn Howe and Juan Ausió*

Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia V8W 3P6, Canada

Received 21 October 1997/Returned for modification 5 December 1997/Accepted 9 December 1997

We sought to study the binding constraints placed on the nine-zinc-finger protein transcription factor IIIA (TFIIIA) by a histone octamer. To this end, five overlapping fragments of the Xenopus laevis oocyte and somatic 5S rRNA genes were reconstituted into nucleosomes, and it was subsequently shown that nucleosome translational positioning is a major determinant of the binding of TFIIIA to the 5S rRNA genes. Furthermore, it was found that histone acetylation cannot override the TFIIIA binding constraints imposed by unfavorable translational positions.

* Corresponding author. Mailing address: Department of Biochemistry and Microbiology, University of Victoria, P.O. Box 3055, Victoria, British Columbia V8W 3P6, Canada. Phone: (250) 721-8863. Fax: (250) 721-8855. E-mail: jausio{at}uvic.ca.




This article has been cited by other articles:

  • Mertens, C., Roeder, R. G. (2008). Different Functional Modes of p300 in Activation of RNA Polymerase III Transcription from Chromatin Templates. Mol. Cell. Biol. 28: 5764-5776 [Abstract] [Full Text]  
  • Ishibashi, T., So, K., Cupples, C. G., Ausio, J. (2008). MBD4-Mediated Glycosylase Activity on a Chromatin Template Is Enhanced by Acetylation. Mol. Cell. Biol. 28: 4734-4744 [Abstract] [Full Text]  
  • Prasad, A., Wallace, S. S., Pederson, D. S. (2007). Initiation of Base Excision Repair of Oxidative Lesions in Nucleosomes by the Human, Bifunctional DNA Glycosylase NTH1. Mol. Cell. Biol. 27: 8442-8453 [Abstract] [Full Text]  
  • Shivaswamy, S., Kassavetis, G. A., Bhargava, P. (2004). High-Level Activation of Transcription of the Yeast U6 snRNA Gene in Chromatin by the Basal RNA Polymerase III Transcription Factor TFIIIC. Mol. Cell. Biol. 24: 3596-3606 [Abstract] [Full Text]  
  • Ghose, R., Malik, M., Huber, P. W. (2004). Restricted Specificity of Xenopus TFIIIA for Transcription of Somatic 5S rRNA Genes. Mol. Cell. Biol. 24: 2467-2477 [Abstract] [Full Text]  
  • Vitolo, J. M., Thiriet, C., Hayes, J. J. (2000). The H3-H4 N-Terminal Tail Domains Are the Primary Mediators of Transcription Factor IIIA Access to 5S DNA within a Nucleosome. Mol. Cell. Biol. 20: 2167-2175 [Abstract] [Full Text]  
  • Kundu, T. K., Wang, Z., Roeder, R. G. (1999). Human TFIIIC Relieves Chromatin-Mediated Repression of RNA Polymerase III Transcription and Contains an Intrinsic Histone Acetyltransferase Activity. Mol. Cell. Biol. 19: 1605-1615 [Abstract] [Full Text]  
  • Mutskov, V., Gerber, D., Angelov, D., Ausio, J., Workman, J., Dimitrov, S. (1998). Persistent Interactions of Core Histone Tails with Nucleosomal DNA following Acetylation and Transcription Factor Binding. Mol. Cell. Biol. 18: 6293-6304 [Abstract] [Full Text]  
  • Thiriet, C., Hayes, J. J. (1998). Functionally Relevant Histone-DNA Interactions Extend Beyond the Classically Defined Nucleosome Core Region. J. Biol. Chem. 273: 21352-21358 [Abstract] [Full Text]  
  • Tse, C., Sera, T., Wolffe, A. P., Hansen, J. C. (1998). Disruption of Higher-Order Folding by Core Histone Acetylation Dramatically Enhances Transcription of Nucleosomal Arrays by RNA Polymerase III. Mol. Cell. Biol. 18: 4629-4638 [Abstract] [Full Text]  
  • WADE, P.A., JONES, P.L., VERMAAK, D., VEENSTRA, G.J.C., IMHOF, A., SERA, T., TSE, C., GE, H., SHI, Y.-B., HANSEN, J.C., WOLFFE, A.P. (1998). Histone Deacetylase Directs the Dominant Silencing of Transcription in Chromatin: Association with MeCP2 and the Mi-2 Chromodomain SWI/SNF ATPase. Cold Spring Harb Symp Quant Biol 63: 435-446 [Abstract]  
  • Wang, X., Moore, S. C., Laszckzak, M., Ausio, J. (2000). Acetylation Increases the alpha -Helical Content of the Histone Tails of the Nucleosome. J. Biol. Chem. 275: 35013-35020 [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»