Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (245K) Freely available
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 (36)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kuznetsova, S.
Right arrow Articles by Svinarchuk, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kuznetsova, S.
Right arrow Articles by Svinarchuk, F.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 27, Issue 20 3995-4000, Copyright © 1999 by Oxford University Press


ARTICLES

Gene activation by triplex-forming oligonucleotide coupled to the activating domain of protein VP16

S Kuznetsova, S Ait-Si-Ali, I Nagibneva, F Troalen, JP Le Villain, A Harel- Bellan and F Svinarchuk
Laboratory of Nucleic Acid Chemistry, Lomonosov Moscow State University, Leninskie gory, 119899, Moscow, Russia.

Triplex-forming oligonucleotides (TFOs) are generally designed to inhibit transcription or DNA replication but can be used for more diverse purposes. Here we have designed a chimera peptide-TFO able to activate transcription from a target gene. The designed hybrid molecule contains a triplex-forming sequence, linked through a phosphoroamidate bond to several minimal transcriptional activation domains derived from Herpes simplex virus protein 16 (VP16). We show here that this TFO- peptide chimera (TFO-P) can specifically recognise its DNA target at physiological salt and pH conditions. Bound to the double-stranded target DNA in a promoter region, the TFO-P is able to activate gene expression. Our results suggest that this type of molecule may prove useful in the design of new tools for artificial modulation of gene expression.
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
Nucleic Acids ResHome page
M. Duca, P. Vekhoff, K. Oussedik, L. Halby, and P. B. Arimondo
The triple helix: 50 years later, the outcome
Nucleic Acids Res., September 1, 2008; 36(16): 5123 - 5138.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Z. Lu, S. P. Rowe, B. B. Brennan, S. E. Davis, R. E. Metzler, J. J. Nau, C. Y. Majmudar, A. K. Mapp, and A. Z. Ansari
Unraveling the Mechanism of a Potent Transcriptional Activator
J. Biol. Chem., August 19, 2005; 280(33): 29689 - 29698.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
A. Mortlock, W. Low, and A. Crisanti
Suppression of gene expression by a cell-permeable Tet repressor
Nucleic Acids Res., December 1, 2003; 31(23): e152 - e152.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
T. G. Uil, H. J. Haisma, and M. G. Rots
Therapeutic modulation of endogenous gene function by agents with designed DNA-sequence specificities
Nucleic Acids Res., November 1, 2003; 31(21): 6064 - 6078.
[Abstract] [Full Text] [PDF]


Home page
Hum Mol GenetHome page
M. P. Knauert and P. M. Glazer
Triplex forming oligonucleotides: sequence-specific tools for gene targeting
Hum. Mol. Genet., October 1, 2001; 10(20): 2243 - 2251.
[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.