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 Hirsch, H. A.
Right arrow Articles by Henry, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hirsch, H. A.
Right arrow Articles by Henry, R. W.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, July 2004, p. 5989-5999, Vol. 24, No. 13
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.13.5989-5999.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Distinct Mechanisms for Repression of RNA Polymerase III Transcription by the Retinoblastoma Tumor Suppressor Protein

Heather A. Hirsch,1,{dagger} Gauri W. Jawdekar,2 Kang-Ae Lee,1 Liping Gu,3 and R. William Henry1,3*

Program in Cell and Molecular Biology,1 Department of Microbiology and Molecular Genetics,2 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan 488243

Received 19 February 2004/ Returned for modification 29 March 2004/ Accepted 5 April 2004

The retinoblastoma (RB) protein represses global RNA polymerase III transcription of genes that encode nontranslated RNAs, potentially to control cell growth. However, RNA polymerase III-transcribed genes exhibit diverse promoter structures and factor requirements for transcription, and a universal mechanism explaining global repression is uncertain. We show that RB represses different classes of RNA polymerase III-transcribed genes via distinct mechanisms. Repression of human U6 snRNA (class 3) gene transcription occurs through stable promoter occupancy by RB, whereas repression of adenovirus VAI (class 2) gene transcription occurs in the absence of detectable RB-promoter association. Endogenous RB binds to a human U6 snRNA gene in both normal and cancer cells that maintain functional RB but not in HeLa cells whose RB function is disrupted by the papillomavirus E7 protein. Both U6 promoter association and transcriptional repression require the A/B pocket domain and C region of RB. These regions of RB contribute to U6 promoter targeting through numerous interactions with components of the U6 general transcription machinery, including SNAPC and TFIIIB. Importantly, RB also concurrently occupies a U6 promoter with RNA polymerase III during repression. These observations suggest a novel mechanism for RB function wherein RB can repress U6 transcription at critical steps subsequent to RNA polymerase III recruitment.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, Michigan State University, 409 Biochemistry Building, East Lansing, MI 48824. Phone: (517) 353-3980. Fax: (517) 353-9334. E-mail: henryrw{at}msu.edu.

{dagger} Present address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.

Molecular and Cellular Biology, July 2004, p. 5989-5999, Vol. 24, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.13.5989-5999.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Zhong and, S., Johnson, D. L. (2009). The JNKs differentially regulate RNA polymerase III transcription by coordinately modulating the expression of all TFIIIB subunits. Proc. Natl. Acad. Sci. USA 106: 12682-12687 [Abstract] [Full Text]  
  • Johnson, S. A. S., Dubeau, L., Johnson, D. L. (2008). Enhanced RNA Polymerase III-dependent Transcription Is Required for Oncogenic Transformation. J. Biol. Chem. 283: 19184-19191 [Abstract] [Full Text]  
  • Woiwode, A., Johnson, S. A. S., Zhong, S., Zhang, C., Roeder, R. G., Teichmann, M., Johnson, D. L. (2008). PTEN Represses RNA Polymerase III-Dependent Transcription by Targeting the TFIIIB Complex. Mol. Cell. Biol. 28: 4204-4214 [Abstract] [Full Text]  
  • Lageix, S., Catrice, O., Deragon, J.-M., Gronenborn, B., Pelissier, T., Ramirez, B. C. (2007). The Nanovirus-Encoded Clink Protein Affects Plant Cell Cycle Regulation through Interaction with the Retinoblastoma-Related Protein. J. Virol. 81: 4177-4185 [Abstract] [Full Text]  
  • Ullah, Z., Buckley, M. S., Arnosti, D. N., Henry, R. W. (2007). Retinoblastoma Protein Regulation by the COP9 Signalosome. Mol. Biol. Cell 18: 1179-1186 [Abstract] [Full Text]  
  • Cavellan, E., Asp, P., Percipalle, P., Farrants, A.-K. O. (2006). The WSTF-SNF2h Chromatin Remodeling Complex Interacts with Several Nuclear Proteins in Transcription. J. Biol. Chem. 281: 16264-16271 [Abstract] [Full Text]  
  • Ernens, I., Goodfellow, S. J., Innes, F., Kenneth, N. S., Derblay, L. E., White, R. J., Scott, P. H. (2006). Hypoxic stress suppresses RNA polymerase III recruitment and tRNA gene transcription in cardiomyocytes. Nucleic Acids Res 34: 286-294 [Abstract] [Full Text]  
  • Fairley, J. A., Kantidakis, T., Kenneth, N. S., Intine, R. V., Maraia, R. J., White, R. J. (2005). Human La is found at RNA polymerase III-transcribed genes in vivo. Proc. Natl. Acad. Sci. USA 102: 18350-18355 [Abstract] [Full Text]  
  • Gu, L., Esselman, W. J., Henry, R. W. (2005). Cooperation between Small Nuclear RNA-activating Protein Complex (SNAPC) and TATA-box-binding Protein Antagonizes Protein Kinase CK2 Inhibition of DNA Binding by SNAPC. J. Biol. Chem. 280: 27697-27704 [Abstract] [Full Text]  
  • Gridasova, A. A., Henry, R. W. (2005). The p53 Tumor Suppressor Protein Represses Human snRNA Gene Transcription by RNA Polymerases II and III Independently of Sequence-Specific DNA Binding. Mol. Cell. Biol. 25: 3247-3260 [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»