Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (208K) 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 (8)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Justice, M. C.
Right arrow Articles by Vershon, A. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Justice, M. C.
Right arrow Articles by Vershon, A. K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 25, Issue 23 4730-4739, Copyright © 1997 by Oxford University Press

ARTICLES

Homeodomain-DNA interactions of the Pho2 protein are promoter-dependent

MC Justice, BP Hogan and AK Vershon
Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08855, USA.

The homeodomain (HD) is a conserved sequence-specific DNA-binding motif found in many eukaryotic transcriptional regulatory proteins. Despite the wealth of in vitro data on the mechanism HD proteins use to bind DNA, comparatively little is known about the roles of individual residues in these domains in vivo . The Saccharomyces cerevisiae Pho2 protein contains a HD that shares significant sequence identity with the Drosophila Engrailed protein. We have used the co-crystal structure of Engrailed as a model to predict how Pho2 might contact DNA and have examined how individual residues of the Pho2 HD contribute to transcriptional activation in vivo and to DNA binding in vitro. Our results demonstrate that Pho2 and Engrailed share many similar DNA- binding characteristics. However, our results also show that some highly conserved residues, which contact the DNA in many HD structures, make relatively small contributions to the DNA-binding affinity and in vivo activity of the Pho2 protein. We also show that the N-terminal arm of the Pho2 HD is a critical component in determining the DNA-binding specificity of the protein and that the requirements for residues in the N-terminal arm are promoter-dependent for Pho2 transcriptional activation and DNA binding.
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. D. Simon, K. Sato, G. A. Weiss, and K. M. Shokat
A phage display selection of engrailed homeodomain mutants and the importance of residue Q50
Nucleic Acids Res., July 9, 2004; 32(12): 3623 - 3631.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
B. M. Owens, Y.-X. Zhu, T.-C. Suen, P.-X. Wang, J. F. Greenblatt, P. E. Goss, and R. G. Hawley
Specific homeodomain-DNA interactions are required for HOX11-mediated transformation
Blood, June 15, 2003; 101(12): 4966 - 4974.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Hannum, O. I. Kulaeva, H. Sun, J. L. Urbanowski, A. Wendus, D. J. Stillman, and R. J. Rolfes
Functional Mapping of Bas2. IDENTIFICATION OF ACTIVATION AND Bas1-INTERACTION DOMAINS
J. Biol. Chem., September 6, 2002; 277(37): 34003 - 34009.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
J. Mead, A. R. Bruning, M. K. Gill, A. M. Steiner, T. B. Acton, and A. K. Vershon
Interactions of the Mcm1 MADS Box Protein with Cofactors That Regulate Mating in Yeast
Mol. Cell. Biol., July 1, 2002; 22(13): 4607 - 4621.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
S. Barbaric, M. Münsterkötter, C. Goding, and W. Hörz
Cooperative Pho2-Pho4 Interactions at the PHO5 Promoter Are Critical for Binding of Pho4 to UASp1 and for Efficient Transactivation by Pho4 at UASp2
Mol. Cell. Biol., May 1, 1998; 18(5): 2629 - 2639.
[Abstract] [Full Text]


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.