Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking.

Détails

ID Serval
serval:BIB_7A4741AE3E1B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Structural flexibility in transcription complex formation revealed by protein-DNA photocrosslinking.
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Cleary M.A., Pendergrast P.S., Herr W.
ISSN
0027-8424
Statut éditorial
Publié
Date de publication
08/1997
Peer-reviewed
Oui
Volume
94
Numéro
16
Pages
8450-8455
Langue
anglais
Résumé
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.
Mots-clé
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
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 16:36
Dernière modification de la notice
08/05/2019 20:46
Données d'usage