Abstract
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.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Binding Sites
-
DNA / chemistry
-
DNA / genetics
-
DNA / metabolism*
-
DNA-Binding Proteins / chemistry
-
DNA-Binding Proteins / genetics
-
DNA-Binding Proteins / metabolism
-
Escherichia coli
-
Herpes Simplex Virus Protein Vmw65 / chemistry
-
Herpes Simplex Virus Protein Vmw65 / metabolism
-
Homeodomain Proteins / chemistry
-
Homeodomain Proteins / genetics
-
Homeodomain Proteins / metabolism*
-
Host Cell Factor C1
-
Humans
-
Octamer Transcription Factor-1
-
Protein Conformation
-
Transcription Factors / chemistry
-
Transcription Factors / genetics
-
Transcription Factors / metabolism*
-
Transcription, Genetic*
Substances
-
DNA-Binding Proteins
-
HCFC1 protein, human
-
Herpes Simplex Virus Protein Vmw65
-
Homeodomain Proteins
-
Host Cell Factor C1
-
Octamer Transcription Factor-1
-
POU2F1 protein, human
-
Transcription Factors
-
DNA