Article: article from journal or magazin.
Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking.
Proceedings of the National Academy of Sciences of the United States of America
The Oct-1 POU domain binds diverse DNA-sequence elements and forms a higher-order regulatory complex with the herpes simplex virus coregulator VP16. The POU domain contains two separate DNA-binding domains joined by a flexible linker. By protein-DNA photocrosslinking we show that the relative positioning of the two POU DNA-binding domains on DNA varies depending on the nature of the DNA target. On a single VP16-responsive element, the POU domain adopts multiple conformations. To determine the structure of the Oct-1 POU domain in a multiprotein complex with VP16, we allowed VP16 to interact with previously crosslinked POU-domain-DNA complexes and found that VP16 can associate with multiple POU-domain conformations. These results reveal the dynamic potential of a DNA-binding domain in directing transcriptional regulatory complex formation.
Binding Sites, DNA, DNA-Binding Proteins, Escherichia coli, Herpes Simplex Virus Protein Vmw65, Homeodomain Proteins, Host Cell Factor C1, Humans, Octamer Transcription Factor-1, Protein Conformation, Transcription Factors, Transcription, Genetic
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