JBC GenomeOne product landing page

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


     

Originally published In Press as doi:10.1074/jbc.M103793200 on August 20, 2001

J. Biol. Chem., Vol. 276, Issue 43, 40127-40132, October 26, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/43/40127    most recent
M103793200v1
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 Hermann, S.
Right arrow Articles by Wright, A. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hermann, S.
Right arrow Articles by Wright, A. P.

How Transcriptional Activators Bind Target Proteins*

Stefan HermannDagger §, Kurt D. Berndt, and Anthony P. WrightDagger

From the Department of Natural Sciences, Södertörns högskola, Box 4101, S-14104 Huddinge, Sweden and the Centers for Dagger  Biotechnology and  Structural Biochemistry, Department of Biosciences, Karolinska Institutet, NOVUM, S-14157 Huddinge, Sweden

The product of the proto-oncogene c-myc influences many cellular processes through the regulation of specific target genes. Through its transactivation domain (TAD), c-Myc protein interacts with several transcription factors, including TATA-binding protein (TBP). We present data that suggest that in contrast to some other transcriptional activators, an extended length of the c-Myc TAD is required for its binding to TBP. Our data also show that this interaction is a multistep process, in which a rapidly forming low affinity complex slowly converts to a more stable form. The initial complex formation results from ionic or polar interactions, whereas the slow conversion to a more stable form is hydrophobic in nature. Based on our results, we suggest two alternative models for activation domain/target protein interactions, which together provide a single universal paradigm for understanding activator-target factor interactions.

* This work was supported by a grant from the Swedish Natural Science Research Council and by the Swedish Cancer Society.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.

§ To whom correspondence should be addressed. Tel.: 46-8-585-88717; Fax: 46-8-585-88510; E-mail: Stefan.Hermann@sh.se.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


This article has been cited by other articles:


Home page
 Eukaryot CellHome page
A. Johnsson, Y. Xue-Franzen, M. Lundin, and A. P. H. Wright
Stress-specific role of fission yeast gcn5 histone acetyltransferase in programming a subset of stress response genes.
Eukaryot. Cell, August 1, 2006; 5(8): 1337 - 1346.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
A. J. Copik, M. S. Webb, A. L. Miller, Y. Wang, R. Kumar, and E. B. Thompson
Activation Function 1 of Glucocorticoid Receptor Binds TATA-Binding Protein in Vitro and in Vivo
Mol. Endocrinol., June 1, 2006; 20(6): 1218 - 1230.
[Abstract] [Full Text] [PDF]

Home page
 J Mol EndocrinolHome page
R A Sporici, J S Hodskins, D M Locasto, L B Meszaros, A L Ferry, A M Weidner, C A Rinehart, J C Bailey, I M Mains, and S E Diamond
Repression of the prolactin promoter: a functional consequence of the heterodimerization between Pit-1 and Pit-1 {beta}
J. Mol. Endocrinol., October 1, 2005; 35(2): 317 - 331.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. E. Ferreira, S. Hermann, P. Prochasson, J. L. Workman, K. D. Berndt, and A. P. H. Wright
Mechanism of Transcription Factor Recruitment by Acidic Activators
J. Biol. Chem., June 10, 2005; 280(23): 21779 - 21784.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. S. Friedman, H. Khanna, P. K. Swain, R. DeNicola, H. Cheng, K. P. Mitton, C. H. Weber, D. Hicks, and A. Swaroop
The Minimal Transactivation Domain of the Basic Motif-Leucine Zipper Transcription Factor NRL Interacts with TATA-binding Protein
J. Biol. Chem., November 5, 2004; 279(45): 47233 - 47241.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Endocrinol.Home page
A. Warnmark, E. Treuter, A. P. H. Wright, and J.-A. Gustafsson
Activation Functions 1 and 2 of Nuclear Receptors: Molecular Strategies for Transcriptional Activation
Mol. Endocrinol., October 1, 2003; 17(10): 1901 - 1909.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
B. He and E. M. Wilson
Electrostatic Modulation in Steroid Receptor Recruitment of LXXLL and FXXLF Motifs
Mol. Cell. Biol., March 15, 2003; 23(6): 2135 - 2150.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. M. Flinn, A. E. Wallberg, S. Hermann, P. A. Grant, J. L. Workman, and A. P. H. Wright
Recruitment of Gcn5-containing Complexes during c-Myc-dependent Gene Activation. STRUCTURE AND FUNCTION ASPECTS
J. Biol. Chem., June 21, 2002; 277(26): 23399 - 23406.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. Warnmark, A. Wikstrom, A. P. H. Wright, J.-A. Gustafsson, and T. Hard
The N-terminal Regions of Estrogen Receptor alpha and beta Are Unstructured in Vitro and Show Different TBP Binding Properties
J. Biol. Chem., November 30, 2001; 276(49): 45939 - 45944.
[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 © 2001 by the American Society for Biochemistry and Molecular Biology.