JBC Focus on PI3-Kinase with Echelon

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


A more recent version of this article appeared on November 15, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/47/45619    most recent
M206829200v1
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 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 Hou, S. Y.
Right arrow Articles by Chiang, C.-M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hou, S. Y.
Right arrow Articles by Chiang, C.-M.
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?

Papers In Press, published online ahead of print September 17, 2002
J. Biol. Chem, 10.1074/jbc.M206829200
Submitted on July 9, 2002
Revised on August 28, 2002
Accepted on September 17, 2002

Transcriptional activity among high- and low-risk human papillomavirus E2 proteins correlates with E2-DNA binding

Samuel Y. Hou, Shwu-Yuan Wu, and Cheng-Ming Chiang

Biochemistry Dept., Case Western Reserve University, School of Medicine, W409, Cleveland, OH 44106-4935

Corresponding Author: c-chiang{at}biochemistry.cwru.edu

The full-length E2 protein, encoded by human papillomaviruses (HPVs), is a sequence-specific transcription factor found in all HPVs, including cancer-causing high-risk HPV types 16 and 18, and wart-inducing low-risk HPV types 6 and 11. To investigate whether E2 proteins encoded by high-risk HPVs may function differentially from E2 proteins encoded by low-risk HPVs and animal papillomaviruses, we conducted comparative DNA-binding and transcription studies using electrophoretic mobility shift assays and cell-free transcription systems reconstituted with purified general transcription factors, cofactor, RNA polymerase II and with E2 proteins encoded by HPV-16, HPV-18, HPV-11 and bovine papillomavirus type 1 (BPV-1). We found that although different types of E2 proteins all exhibited transactivation and repression activities, depending on the sequence context of the E2-binding sites, HPV-16 E2 shows stronger transcription activity and greater DNA-binding affinity than those displayed by the other E2 proteins. Surprisingly, HPV-18 E2 behaves more similarly to BPV-1 E2 than HPV-16 E2 in their functional properties. Our studies thus categorize HPV-18 E2 and BPV-1 E2 in the same protein family, a finding consistent with the available E2 structural data which separate the closely related HPV-16 and HPV-18 E2 proteins but classify together the more divergent BPV-1 and HPV-18 E2 proteins.


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
J. Virol.Home page
E. E. Hernandez-Ramon, J. E. Burns, W. Zhang, H. F. Walker, S. Allen, A. A. Antson, and N. J. Maitland
Dimerization of the Human Papillomavirus Type 16 E2 N Terminus Results in DNA Looping within the Upstream Regulatory Region
J. Virol., May 15, 2008; 82(10): 4853 - 4861.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
I. E. Sanchez, M. Dellarole, K. Gaston, and G. de Prat Gay
Comprehensive comparison of the interaction of the E2 master regulator with its cognate target DNA sites in 73 human papillomavirus types by sequence statistics
Nucleic Acids Res., February 11, 2008; 36(3): 756 - 769.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S.-Y. Wu and C.-M. Chiang
The Double Bromodomain-containing Chromatin Adaptor Brd4 and Transcriptional Regulation
J. Biol. Chem., May 4, 2007; 282(18): 13141 - 13145.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
E. Hooley, V. Fairweather, A. R. Clarke, K. Gaston, and R. Leo Brady
The recognition of local DNA conformation by the human papillomavirus type 6 E2 protein
Nucleic Acids Res., September 1, 2006; 34(14): 3897 - 3908.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
S.-Y. Wu, A-Y. Lee, S. Y. Hou, J. K. Kemper, H. Erdjument-Bromage, P. Tempst, and C.-M. Chiang
Brd4 links chromatin targeting to HPV transcriptional silencing
Genes & Dev., September 1, 2006; 20(17): 2383 - 2396.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
T. Mino, T. Hatono, N. Matsumoto, T. Mori, Y. Mineta, Y. Aoyama, and T. Sera
Inhibition of DNA replication of human papillomavirus by artificial zinc finger proteins.
J. Virol., June 1, 2006; 80(11): 5405 - 5412.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
J. L. Parish, A. Kowalczyk, H.-T. Chen, G. E. Roeder, R. Sessions, M. Buckle, and K. Gaston
E2 Proteins from High- and Low-Risk Human Papillomavirus Types Differ in Their Ability To Bind p53 and Induce Apoptotic Cell Death
J. Virol., May 1, 2006; 80(9): 4580 - 4590.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
S.-Y. Wu, T. Zhou, and C.-M. Chiang
Human Mediator Enhances Activator-Facilitated Recruitment of RNA Polymerase II and Promoter Recognition by TATA-Binding Protein (TBP) Independently of TBP-Associated Factors
Mol. Cell. Biol., September 1, 2003; 23(17): 6229 - 6242.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.