Flexible DNA binding of the BTB/POZ-domain protein FBI-1

Pessler, F., Hernandez, N. (August 2003) Flexible DNA binding of the BTB/POZ-domain protein FBI-1. Journal of Biological Chemistry, 278 (31). pp. 29327-29335. ISSN 0021-9258

URL: http://www.ncbi.nlm.nih.gov/pubmed/12750370
DOI: 10.1074/jbc.M302980200

Abstract

POZ-domain transcription factors are characterized by the presence of a protein-protein interaction domain called the POZ or BTB domain at their N terminus and zinc fingers at their C terminus. Despite the large number of POZ-domain transcription factors that have been identified to date and the significant insights that have been gained into their cellular functions, relatively little is known about their DNA binding properties. FBI-1 is a BTB/POZ-domain protein that has been shown to modulate HIV-1 Tat trans-activation and to repress transcription of some cellular genes. We have used various viral and cellular FBI-1 binding sites to characterize the interaction of a POZ-domain protein with DNA in detail. We find that FBI-1 binds to inverted sequence repeats downstream of the HIV-1 transcription start site. Remarkably, it binds efficiently to probes carrying these repeats in various orientations and spacings with no particular rotational alignment, indicating that its interaction with DNA is highly flexible. Indeed, FBI-1 binding sites in the adenovirus 2 major late promoter, the c-fos gene, and the c-myc P1 and P2 promoters reveal variously spaced direct, inverted, and everted sequence repeats with the consensus sequence G(A/G)GGG(T/ C)(C/T)(T/C)(C/T)for each repeat.

Item Type: Paper
Uncontrolled Keywords: SHORT TRANSCRIPTS POZ DOMAIN GENE-EXPRESSION COMPLEX-FORMATION INTERACTION MOTIF HIV-1 INDUCER BTB DOMAIN SHORT RNAS FAMILY FLEXIBILITY
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Hernandez lab
Depositing User: Matt Covey
Date: August 2003
Date Deposited: 27 Jun 2013 14:28
Last Modified: 27 Jun 2013 14:28
Related URLs:
URI: http://repository.cshl.edu/id/eprint/27928

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