The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16.

Détails

ID Serval
serval:BIB_30252E636975
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The Oct-1 homoeodomain directs formation of a multiprotein-DNA complex with the HSV transactivator VP16.
Périodique
Nature
Auteur(s)
Stern S., Tanaka M., Herr W.
ISSN
0028-0836
Statut éditorial
Publié
Date de publication
10/1989
Peer-reviewed
Oui
Volume
341
Numéro
6243
Pages
624-630
Langue
anglais
Résumé
The herpes simplex virus transactivator VP16 participates in the formation of a multiprotein-DNA complex with the ubiquitous octamer-motif-binding factor Oct-1. Complex formation is dependent on specific amino acids in the Oct-1 homoeodomain which are in positions analogous to positive control mutations in helix 2 of the lambda phage repressor helix-turn-helix motif, indicating that this structure is an ancient target for protein-protein interactions mediating transcriptional control.
Mots-clé
Amino Acid Sequence, DNA-Binding Proteins, Gene Expression Regulation, Viral, Genes, Homeobox, Host Cell Factor C1, Macromolecular Substances, Molecular Sequence Data, Multiprotein Complexes, Octamer Transcription Factor-1, Octamer Transcription Factor-2, Phosphoproteins, Protein Binding, Protein Conformation, Simplexvirus, Structure-Activity Relationship, Trans-Activators, Transcription Factors
Pubmed
Web of science
Création de la notice
24/01/2008 15:36
Dernière modification de la notice
20/08/2019 13:14
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