Browse by author
Lookup NU author(s): Dr Amanda Greenall
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
The control of DNA binding by eukaryotic transcription factors represents an important regulatory mechanism. Many transcription factors are controlled by cisacting autoinhibitory modules that are thought to act by blocking promiscuous DNA binding in the absence of appropriate regulatory cues. Here, we have investigated the determinants and regulation of the autoinhibitory mechanism employed by the ETS-domain transcription factor, PEA3. DNA binding is inhibited by a module composed of a combination of two short motifs located on either side of the ETS DNA-binding domain. A second type of protein, Ids, can act in trans to mimic the effect of these cis-acting inhibitory motifs and reduce DNA binding by PEA3. By using a one-hybrid screen, we identified the basic helix-loop-helix-leucine zipper transcription factor USF-1 as an interaction partner for PEA3. PEA3 and USF-1 form DNA complexes in a cooperative manner. Moreover, the formation of ternary PEA3·USF-1· DNA complexes requires parts of the same motifs in PEA3 that form the autoinhibitory module. Thus the binding of USF-1 to PEA3 acts as a switch that modifies the autoinhibitory motifs in PEA3 to first relieve their inhibitory action, and second, promote ternary nucleoprotein complex assembly.
Author(s): Greenall A, Willingham N, Cheung E, Boam DS, Sharrocks AD
Publication type: Article
Publication status: Published
Journal: The Journal of Biological Chemistry
Year: 2001
Volume: 276
Issue: 19
Pages: 16207-16215
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology
URL: http://dx.doi.org/10.1074/jbc.M011582200
DOI: 10.1074/jbc.M011582200
PubMed id: 11278941
Altmetrics provided by Altmetric
