scholarly journals Ternary complex formation over the c-fos serum response element: p62TCF exhibits dual component specificity with contacts to DNA and an extended structure in the DNA-binding domain of p67SRF.

1992 ◽  
Vol 11 (8) ◽  
pp. 3011-3019 ◽  
Author(s):  
P.E. Shaw
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Ternary Complex ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Serum Response Element ◽  
Response Element ◽  
Extended Structure ◽  
Ternary Complex Formation ◽  
Serum Response

scholarly journals MAL and Ternary Complex Factor Use Different Mechanisms To Contact a Common Surface on the Serum Response Factor DNA-Binding Domain

2006 ◽  
Vol 26 (11) ◽  
pp. 4134-4148 ◽  
Author(s):  
Alexia-Ileana Zaromytidou ◽  
Francesc Miralles ◽  
Richard Treisman
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Ternary Complex ◽  
Serum Response Factor ◽  
Dna Bending ◽  
Binding Domain ◽  
Response Factor ◽  
Dna Binding Domain ◽  
Serum Response ◽  
Ternary Complex Factor

ABSTRACT The transcription factor serum response factor (SRF) interacts with its cofactor, MAL/MKL1, a member of the myocardin-related transcription factor (MRTF) family, through its DNA-binding domain. We define a seven-residue sequence within the conserved MAL B1 region essential and sufficient for complex formation. The neighboring Q-box sequence facilitates this interaction. The B1 and Q-box regions also have antagonistic effects on MAL nuclear import, but the residues involved are largely distinct. Both MAL and the ternary complex factor (TCF) family of SRF cofactors interact with a hydrophobic groove and pocket on the SRF DNA-binding domain. Unlike the TCFs, however, interaction of MAL with SRF is impaired by SRF αI-helix mutations that reduce DNA bending in the SRF-DNA complex. A clustered SRF αI-helix mutation strongly impairs MAL-SRF complex formation but does not affect DNA distortion in the MAL-SRF complex. MAL-SRF complex formation is facilitated by DNA binding. DNase I footprinting indicates that in the SRF-MAL complex MAL directly contacts DNA. These contacts, which flank the DNA sequences protected from DNase I by SRF, are required for effective MAL-SRF complex formation in gel mobility shift assays. We propose a model of MAL-SRF complex formation in which MAL interacts with SRF by the addition of a β-strand to the SRF DNA-binding domain β-sheet region, while SRF-induced DNA bending facilitates MAL-DNA contact.

scholarly journals Inhibition of Ets-1 DNA Binding and Ternary Complex Formation between Ets-1, NF-κB, and DNA by a Designed DNA-binding Ligand

1999 ◽  
Vol 274 (18) ◽  
pp. 12765-12773 ◽  
Author(s):  
Liliane A. Dickinson ◽  
John W. Trauger ◽  
Eldon E. Baird ◽  
Peter B. Dervan ◽  
Barbara J. Graves ◽  
...  
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Ternary Complex ◽  
Ternary Complex Formation

scholarly journals Elk-1 Can Recruit SRF to Form a Ternary Complex Upon the Serum Response Element

1996 ◽  
Vol 24 (7) ◽  
pp. 1345-1351 ◽  
Author(s):  
B. V. Latinkic ◽  
M. Zeremski ◽  
L. F. Lau
Keyword(s):  
Ternary Complex ◽  
Serum Response Element ◽  
Response Element ◽  
Serum Response

scholarly journals Involvement of the sigmaN DNA-binding domain in open complex formation

1999 ◽  
Vol 33 (4) ◽  
pp. 873-885 ◽  
Author(s):  
Jose A. Oguiza ◽  
Maria-Trinidad Gallegos ◽  
Matthew K. Chaney ◽  
Wendy V. Cannon ◽  
Martin Buck
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Open Complex Formation

Binding of the estrogen receptor DNA-binding domain to the estrogen response element induces DNA bending

1992 ◽  
Vol 12 (5) ◽  
pp. 2037-2042
Author(s):  
A M Nardulli ◽  
D J Shapiro
Keyword(s):  
Estrogen Receptor ◽  
Dna Binding ◽  
Dna Bending ◽  
Binding Domain ◽  
Estrogen Response Element ◽  
Dna Binding Domain ◽  
Mobility Shift ◽  
Response Element ◽  
Estrogen Response ◽  
Dna Fragment

We have used circular permutation analysis to determine whether binding of purified Xenopus laevis estrogen receptor DNA-binding domain (DBD) to a DNA fragment containing an estrogen response element (ERE) causes the DNA to bend. Gel mobility shift assays showed that DBD-DNA complexes formed with fragments containing more centrally located EREs migrated more slowly than complexes formed with fragments containing EREs near the ends of the DNA. DNA bending standards were used to determine that the degree of bending induced by binding of the DBD to an ERE was approximately 34 degrees. A 1.55-fold increase in the degree of bending was observed when two EREs were present in the DNA fragment. These in vitro studies suggest that interaction of nuclear receptors with their hormone response elements in vivo may result in an altered DNA conformation.

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