JBC Oz Biosciences

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lehman, A. L.
Right arrow Articles by Dahmus, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lehman, A. L.
Right arrow Articles by Dahmus, M. E.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 20, 14923-14932, May 19, 2000

The Sensitivity of RNA Polymerase II in Elongation Complexes to C-terminal Domain Phosphatase*

Alan L. Lehman and Michael E. DahmusDagger

From the Section of Molecular and Cellular Biology, Division of Biological Sciences, University of California, Davis, California 95616

The phosphorylation state of the carboxyl-terminal domain (CTD) of the largest RNA polymerase (RNAP) II subunit plays an important role in the regulation of transcript elongation. This report examines the sensitivity of RNAP II to dephosphorylation by CTD phosphatase (CTDP) and addresses factors that regulate its sensitivity. The CTDP sensitivity of RNAP IIO in paused elongation complexes on a dC-tailed template does not significantly differ from that of free RNAP IIO. RNAP IIO contained in elongation complexes that initiate transcription from the adenovirus-2 major late promoter in the presence of a nuclear extract is relatively resistant to dephosphorylation. Complexes treated with 1% Sarkosyl remain elongation-competent but demonstrate a 5-fold increase in CTDP sensitivity. Furthermore, the sensitivity of RNAP IIO in both control and Sarkosyl-treated elongation complexes is dependent on their position relative to the start site of transcription. Elongation complexes 11-24 nucleotides downstream are more sensitive to dephosphorylation than complexes 50-150 nucleotides downstream. The incubation of Sarkosyl-treated elongation complexes with nuclear extract restores the original resistance to dephosphorylation. These results suggest that a conformational change occurs in RNAP II as it clears the promoter, which results in an increased resistance to dephosphorylation. Furthermore, the sensitivity to dephosphorylation can be modulated by a factor(s) present in the nuclear extract.

* This work was supported by National Institutes of Health Grant GM-33300 (to M. E. D.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 530-752-3551; Fax: 530-752-3085; E-mail: medahmus@ucdavis.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Proc. Natl. Acad. Sci. USAHome page
M.-H. Suh, P. Ye, M. Zhang, S. Hausmann, S. Shuman, A. L. Gnatt, and J. Fu
Fcp1 directly recognizes the C-terminal domain (CTD) and interacts with a site on RNA polymerase II distinct from the CTD
PNAS, November 29, 2005; 102(48): 17314 - 17319.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
A. Meinhart, T. Kamenski, S. Hoeppner, S. Baumli, and P. Cramer
A structural perspective of CTD function
Genes & Dev., June 15, 2005; 19(12): 1401 - 1415.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. E. Kong, M. S. Kobor, N. J. Krogan, B. P. Somesh, T. M. M. Sogaard, J. F. Greenblatt, and J. Q. Svejstrup
Interaction of Fcp1 Phosphatase with Elongating RNA Polymerase II Holoenzyme, Enzymatic Mechanism of Action, and Genetic Interaction with Elongator
J. Biol. Chem., February 11, 2005; 280(6): 4299 - 4306.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Tremeau-Bravard, T. Riedl, J.-M. Egly, and M. E. Dahmus
Fate of RNA Polymerase II Stalled at a Cisplatin Lesion
J. Biol. Chem., February 27, 2004; 279(9): 7751 - 7759.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
E. M. Friedl, W. S. Lane, H. Erdjument-Bromage, P. Tempst, and D. Reinberg
The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation
PNAS, March 4, 2003; 100(5): 2328 - 2333.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. S. Lin, M.-F. Dubois, and M. E. Dahmus
TFIIF-associating Carboxyl-terminal Domain Phosphatase Dephosphorylates Phosphoserines 2 and 5 of RNA Polymerase II
J. Biol. Chem., November 22, 2002; 277(48): 45949 - 45956.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Palancade, M.-F. Dubois, and O. Bensaude
FCP1 Phosphorylation by Casein Kinase 2 Enhances Binding to TFIIF and RNA Polymerase II Carboxyl-terminal Domain Phosphatase Activity
J. Biol. Chem., September 20, 2002; 277(39): 36061 - 36067.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Hausmann and S. Shuman
Characterization of the CTD Phosphatase Fcp1 from Fission Yeast. PREFERENTIAL DEPHOSPHORYLATION OF SERINE 2 VERSUS SERINE 5
J. Biol. Chem., June 7, 2002; 277(24): 21213 - 21220.
[Abstract] [Full Text] [PDF]

Home page
 Genes Dev.Home page
E.-J. Cho, M. S. Kobor, M. Kim, J. Greenblatt, and S. Buratowski
Opposing effects of Ctk1 kinase and Fcp1 phosphatase at Ser 2 of the RNA polymerase II C-terminal domain
Genes & Dev., December 15, 2001; 15(24): 3319 - 3329.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
B. Palancade, M. F. Dubois, M. E. Dahmus, and O. Bensaude
Transcription-Independent RNA Polymerase II Dephosphorylation by the FCP1 Carboxy-Terminal Domain Phosphatase in Xenopus laevis Early Embryos
Mol. Cell. Biol., October 1, 2001; 21(19): 6359 - 6368.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
M. S. Kobor, L. D. Simon, J. Omichinski, G. Zhong, J. Archambault, and J. Greenblatt
A Motif Shared by TFIIF and TFIIB Mediates Their Interaction with the RNA Polymerase II Carboxy-Terminal Domain Phosphatase Fcp1p in Saccharomyces cerevisiae
Mol. Cell. Biol., October 15, 2000; 20(20): 7438 - 7449.
[Abstract] [Full Text]

Home page
 Genes Dev.Home page
R. M. Nissen and K. R. Yamamoto
The glucocorticoid receptor inhibits NFkappa B by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain
Genes & Dev., September 15, 2000; 14(18): 2314 - 2329.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
N. F. Marshall and M. E. Dahmus
C-terminal Domain Phosphatase Sensitivity of RNA Polymerase II in Early Elongation Complexes on the HIV-1 and Adenovirus 2 Major Late Templates
J. Biol. Chem., October 13, 2000; 275(42): 32430 - 32437.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. A. Hawkes, G. Otero, G. S. Winkler, N. Marshall, M. E. Dahmus, D. Krappmann, C. Scheidereit, C. L. Thomas, G. Schiavo, H. Erdjument-Bromage, et al.
Purification and Characterization of the Human Elongator Complex
J. Biol. Chem., January 18, 2002; 277(4): 3047 - 3052.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.