Structural Flexibility in Transcription Complex Formation Revealed by Protein-DNA Photocrosslinking

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 positi...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 1997-08, Vol.94 (16), p.8450-8455
Hauptverfasser: Cleary, Michele A., Pendergrast, P. Shannon, Herr, Winship
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Sprache:eng
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Zusammenfassung: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.94.16.8450