Skip Navigation

This Article
Right arrow Print PDF (5994K)
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (17)
Right arrowRequest Permissions
Citing Articles
Right arrowScopus Links
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Kuprash, D. V.
Right arrow Articles by Nedospasov, S. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kuprash, D. V.
Right arrow Articles by Nedospasov, S. A.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1995, Vol. 23, No. 3 427-433
© 1995


MOLECULAR BIOLOGY

Homodimer of p50 (NF{kappa}B1) does not introduce a substantial directed bend into DNA according to three different experimental assays

Dmitry V. Kuprash1,2,3, Nancy R. Rice3 and Sergei A. Nedospasov1,2,*

1Laboratory of Cytokine Molecular Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences Moscow 117984, Russia 2Biological Carcinogenesis and Development Program, Program Resources, Inc./DynCorp., Laboratory of Molecular Immunoregulation, Biological Response Modifiers Program, National Cancer Institute—Frederick Cancer Research and Development Center Frederick, MD 21702-1201, USA 3ABL-Basic Research Program, National Cancer Institute—Frederick Cancer Research and Development Center Frederick, MD 21702-1201, USA

*To whom correspondence should be addressed at: BCDP, PRI/DynCorp, National Cancer Institute, Frederick Cancer Research and Development Center, Building 560, Room 31-70, Frederick, MD 21702-1201, USA

Received October 12, 1994. Revised November 23, 1994. Accepted November 23, 1994.

Transcription factors can distort the conformation of the DNA double helix upon binding to their target sites. Previously, studies utilizing circular permutation—electrophoretlc mobility shift assay suggested that the homodimer of p50 (NF{kappa}B1), canonical NF-{kappa}B (p65-p50), as well as several non-canonical NF-{kappa}B/Rel complexes, may induce substantial DNA bending at the binding site. Here we have applied three additional experimental approaches, helical phasing analysis, mlniclrcle binding and cyclization kinetics, and conclude that the homodimer of p50 introduces virtually no directed bend into the consensus {kappa}B sequences GGGACTTTCC or GGGAATTCCC.


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. Pharmacol.Home page
C. E. Ruby, M. Leid, and N. I. Kerkvliet
2,3,7,8-Tetrachlorodibenzo-p-dioxin Suppresses Tumor Necrosis Factor-alpha and Anti-CD40-Induced Activation of NF-kappa B/Rel in Dendritic Cells: p50 Homodimer Activation Is Not Affected
Mol. Pharmacol., September 1, 2002; 62(3): 722 - 728.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
L. A. Hanakahi and N. Maizels
Transcriptional activation by LR1 at the E{micro} enhancer and switch region sites
Nucleic Acids Res., July 15, 2000; 28(14): 2651 - 2657.
[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.