POU proteins bend DNA via the POU-specific domain.
POU proteins constitute a family of ubiquitous as well as cell type-specific transcription factors that share the conserved POU DNA binding domain. This domain consists of two distinct subdomains, a POU-specific domain and a POU homeodomain, that are both required for high affinity sequence-specific DNA binding. In a circular permutation assay, several POU proteins, including Oct-1, Oct-2A, Oct-6 and Pit-1, demonstrated a position dependent mobility of the protein-DNA complexes, suggesting induction of DNA bending. This was confirmed by detection of relative bend direction, using pre-bent DNA, and by enhanced ligase mediated cyclization. Bending was caused by interaction with the POU domain. By contrast, binding of the POU homeodomain did not distort the DNA structure, indicating that the POU-specific domain confers DNA bending.
Laboratory for Physiological Chemistry, University of Utrecht, The Netherlands.
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Verrijzer
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van Oosterhout
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van Weperen
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van der Vliet
D001483:Base Sequence; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004261:DNA Replication; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D015183:Restriction Mapping; D014157:Transcription Factors / Q000378:metabolism*
D014157:Transcription Factors; D004247:DNA