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PMID: 1915275 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

POU proteins bend DNA via the POU-specific domain.

The EMBO journal ·Vol. 10 ·No. 10 ·1991-10-00 ·Pages 3007-14

Verrijzer CP, van Oosterhout JA, van Weperen WW, van der Vliet PC

Abstract

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.

MeSH Terms
Base Sequence DNA/chemistry,metabolism DNA Replication Electrophoresis, Polyacrylamide Gel Molecular Sequence Data Nucleic Acid Conformation Restriction Mapping Transcription Factors/metabolism
Chemicals
Transcription Factors DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Verrijzer C P
Laboratory for Physiological Chemistry, University of Utrecht, The Netherlands.
van Oosterhout J A
van Weperen W W
van der Vliet P C
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1991-10-00
Pages
3007-14
Language
English
Region
England
NLM ID
8208664
PMCID
PMC453015
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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