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 Protacio, R. U.
Right arrow Articles by Widom, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Protacio, R. U.
Right arrow Articles by Widom, J.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, December 2000, p. 8866-8878, Vol. 20, No. 23
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Effects of Histone Tail Domains on the Rate of Transcriptional Elongation through a Nucleosome

R. U. Protacio,1,dagger G. Li,1 P. T. Lowary,1 and J. Widom1,2,*

Department of Biochemistry, Molecular Biology, and Cell Biology,1 and Department of Chemistry,2 Northwestern University, Evanston, Illinois 60208-3500

Received 17 July 2000/Accepted 24 August 2000

The N-terminal tail domains of the core histones play important roles in gene regulation, but the exact mechanisms through which they act are not known. Recent studies suggest that the tail domains may influence the ability of RNA polymerase to elongate through the nucleosomal DNA and, thus, that posttranslational modification of the tail domains may provide a control point for gene regulation through effects on the elongation rate. We take advantage of an experimental system that uses bacteriophage T7 RNA polymerase as a probe for aspects of nucleosome transcription that are dominated by the properties of nucleosomes themselves. With this system, experiments can analyze the synchronous, real-time, single-passage transcription on the nucleosomal template. Here, we use this system to directly test the hypothesis that the tail domains may influence the "elongatability" of nucleosomal DNA and to identify which of the tail domains may contribute to this. The results show that the tail domains strongly influence the rate of elongation and suggest that the effect is dominated by the N-terminal domains of the (H3-H4)2 tetramer. They further imply that tail-mediated octamer transfer is not essential for elongation through the nucleosome. Acetylation of the tail domains leads to effects on elongation that are similar to those arising from complete removal of the tail domains.

* Corresponding author. Mailing address: Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, 2153 Sheridan Rd., Evanston, IL 60208-3500. Phone: (847) 467-1887. Fax: (847) 467-6489. E-mail: j-widom{at}northwestern.edu.

dagger Present address: Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138.

Molecular and Cellular Biology, December 2000, p. 8866-8878, Vol. 20, No. 23
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Maksakova, I. A., Zhang, Y., Mager, D. L. (2009). Preferential Epigenetic Suppression of the Autonomous MusD over the Nonautonomous ETn Mouse Retrotransposons. Mol. Cell. Biol. 29: 2456-2468 [Abstract] [Full Text]  
  • Ferreira, H., Somers, J., Webster, R., Flaus, A., Owen-Hughes, T. (2007). Histone Tails and the H3 {alpha}N Helix Regulate Nucleosome Mobility and Stability. Mol. Cell. Biol. 27: 4037-4048 [Abstract] [Full Text]  
  • Xie, Y., Reeve, J. N. (2004). Transcription by an Archaeal RNA Polymerase Is Slowed but Not Blocked by an Archaeal Nucleosome. J. Bacteriol. 186: 3492-3498 [Abstract] [Full Text]  
  • Kim, J., Jia, L., Tilley, W. D., Coetzee, G. A. (2003). Dynamic methylation of histone H3 at lysine 4 in transcriptional regulation by the androgen receptor. Nucleic Acids Res 31: 6741-6747 [Abstract] [Full Text]  
  • Georges, S. A., Giebler, H. A., Cole, P. A., Luger, K., Laybourn, P. J., Nyborg, J. K. (2003). Tax Recruitment of CBP/p300, via the KIX Domain, Reveals a Potent Requirement for Acetyltransferase Activity That Is Chromatin Dependent and Histone Tail Independent. Mol. Cell. Biol. 23: 3392-3404 [Abstract] [Full Text]  
  • Bernstein, B. E., Humphrey, E. L., Erlich, R. L., Schneider, R., Bouman, P., Liu, J. S., Kouzarides, T., Schreiber, S. L. (2002). Methylation of histone H3 Lys 4 in coding regions of active genes. Proc. Natl. Acad. Sci. USA 99: 8695-8700 [Abstract] [Full Text]  
  • He, G., Margolis, D. M. (2002). Counterregulation of Chromatin Deacetylation and Histone Deacetylase Occupancy at the Integrated Promoter of Human Immunodeficiency Virus Type 1 (HIV-1) by the HIV-1 Repressor YY1 and HIV-1 Activator Tat. Mol. Cell. Biol. 22: 2965-2973 [Abstract] [Full Text]  
  • Winkler, G. S., Kristjuhan, A., Erdjument-Bromage, H., Tempst, P., Svejstrup, J. Q. (2002). Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proc. Natl. Acad. Sci. USA 99: 3517-3522 [Abstract] [Full Text]  
  • Lefebvre, B., Brand, C., Lefebvre, P., Ozato, K. (2002). Chromosomal Integration of Retinoic Acid Response Elements Prevents Cooperative Transcriptional Activation by Retinoic Acid Receptor and Retinoid X Receptor. Mol. Cell. Biol. 22: 1446-1459 [Abstract] [Full Text]  
  • Georges, S. A., Kraus, W. L., Luger, K., Nyborg, J. K., Laybourn, P. J. (2002). p300-Mediated Tax Transactivation from Recombinant Chromatin: Histone Tail Deletion Mimics Coactivator Function. Mol. Cell. Biol. 22: 127-137 [Abstract] [Full Text]  
  • Smith, E. R., Allis, C. D., Lucchesi, J. C. (2001). Linking Global Histone Acetylation to the Transcription Enhancement of X-chromosomal Genes in Drosophila Males. J. Biol. Chem. 276: 31483-31486 [Abstract] [Full Text]  
  • Walter, W., Studitsky, V. M. (2001). Facilitated Transcription through the Nucleosome at High Ionic Strength Occurs via a Histone Octamer Transfer Mechanism. J. Biol. Chem. 276: 29104-29110 [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»