Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (233K) Freely available
Right arrow Supplementary Material
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (24)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Mondal, N.
Right arrow Articles by Parvin, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Mondal, N.
Right arrow Articles by Parvin, J. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2003, Vol. 31, No. 17 5016-5024
© 2003 Oxford University Press

Elongation by RNA polymerase II on chromatin templates requires topoisomerase activity

Neelima Mondal, Ye Zhang, Zophonias Jonsson, Suman Kumar Dhar, Madhu Kannapiran and Jeffrey D. Parvin*

Department of Pathology, Brigham and Women’s Hospital, Harvard Medical School, Boston, MA 02115, USA

*To whom correspondence should be addressed. Tel: +1 617 278 0818; Fax: +1 617 732 7449; Email: jparvin{at}rics.bwh.harvard.edu

Transcription on chromatin by RNA polymerase II (pol II) is repressed as compared with transcription on histone-free DNA. In this study, we show that human topoisomerase I (topo I) and yeast topoisomerase II (topo II), each of which relax both positive and negative superhelical tension, reverse the transcriptional repression by chromatin. In the presence of bacterial topo I, which can relax only negative superhelical tension, the transcription is repressed on chromatin templates. The data together show that the relaxation of positive superhelical tension by these enzymes was the key property required for RNA synthesis from chromatin templates. In the absence of topoisomerase, transcriptional repression on chromatin depended on RNA length. The synthesis of transcripts of 100 nt or shorter was unaffected by chromatin, but repression was apparent when the RNA transcript was 200 nt or longer. These findings suggest that transcription on chromatin templates results in the accumulation of positive superhelical tension by the elongating polymerase, which in turn inhibits further elongation in the absence of topoisomerase activity.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
M. Dovey, E. E. Patton, T. Bowman, T. North, W. Goessling, Y. Zhou, and L. I. Zon
Topoisomerase II{alpha} Is Required for Embryonic Development and Liver Regeneration in Zebrafish
Mol. Cell. Biol., July 1, 2009; 29(13): 3746 - 3753.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
C.-H. Su, Y.-J. Shann, and M.-T. Hsu
p53 Chromatin Epigenetic Domain Organization and p53 Transcription
Mol. Cell. Biol., January 1, 2009; 29(1): 93 - 103.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
S.-W. Park, A. M. Parrott, D. T. Fritz, Y. Park, M. B. Mathews, and C.-G. Lee
Regulation of the catalytic function of topoisomerase II alpha through association with RNA
Nucleic Acids Res., November 1, 2008; 36(19): 6080 - 6090.
[Abstract] [Full Text] [PDF]

Home page
 Br. J. Radiol.Home page
J R Jenkins
A proteomic approach to identifying new drug targets (potentiating topoisomerase II poisons)
Br. J. Radiol., October 1, 2008; 81(Special_Issue_1): S69 - S77.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Malanga, A. Czubaty, A. Girstun, K. Staron, and F. R. Althaus
Poly(ADP-ribose) Binds to the Splicing Factor ASF/SF2 and Regulates Its Phosphorylation by DNA Topoisomerase I
J. Biol. Chem., July 18, 2008; 283(29): 19991 - 19998.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
R. F. Frohlich, C. Veigaard, F. F. Andersen, A. K. McClendon, A. C. Gentry, A. H. Andersen, N. Osheroff, T. Stevnsner, and B. R. Knudsen
Tryptophane-205 of human topoisomerase I is essential for camptothecin inhibition of negative but not positive supercoil removal
Nucleic Acids Res., September 25, 2007; 35(18): 6170 - 6180.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
W. G. Muller, D. Rieder, T. S. Karpova, S. John, Z. Trajanoski, and J. G. McNally
Organization of chromatin and histone modifications at a transcription site
J. Cell Biol., July 30, 2007; 177(6): 957 - 967.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. A. Horwitz, S. Sankaran, and J. D. Parvin
Direct Stimulation of Transcription Initiation by BRCA1 Requires Both Its Amino and Carboxyl Termini
J. Biol. Chem., March 31, 2006; 281(13): 8317 - 8320.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Mialon, M. Sankinen, H. Soderstrom, T. T. Junttila, T. Holmstrom, R. Koivusalo, A. C. Papageorgiou, R. S. Johnson, S. Hietanen, K. Elenius, et al.
DNA Topoisomerase I Is a Cofactor for c-Jun in the Regulation of Epidermal Growth Factor Receptor Expression and Cancer Cell Proliferation
Mol. Cell. Biol., June 15, 2005; 25(12): 5040 - 5051.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Zhang, K. Griffin, N. Mondal, and J. D. Parvin
Phosphorylation of Histone H2A Inhibits Transcription on Chromatin Templates
J. Biol. Chem., May 21, 2004; 279(21): 21866 - 21872.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.