The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription.

Détails

ID Serval
serval:BIB_FF373E301845
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription.
Périodique
Molecular and Cellular Biology
Auteur(s)
Tanaka M., Clouston W.M., Herr W.
ISSN
0270-7306[print], 0270-7306[linking]
Statut éditorial
Publié
Date de publication
09/1994
Volume
14
Numéro
9
Pages
6046-6055
Langue
anglais
Notes
Publication types: In Vitro ; Journal Article ; Research Support, U.S. Gov't, P.H.S.
Publication Status: ppublish
Résumé
The B-cell POU homeodomain protein Oct-2 contains two transcriptional activation domains, one N terminal and the other C terminal of the central DNA-binding POU domain. The synergistic action of these two activation domains makes Oct-2 a more potent activator of mRNA promoters than the related broadly expressed octamer motif-binding protein Oct-1, which contains an N-terminal but not a C-terminal Oct-2-like activation domain. Both Oct-2 mRNA promoter activation domains were delineated by truncation analysis: the N-terminal Q domain is a 66-amino-acid region rich in glutamines, and the C-terminal P domain is a 42-amino-acid region rich in prolines. The Q and P domains synergized with each other or duplicates of themselves, independently of their N-terminal or C-terminal position relative to the POU domain. The C-terminal P domain, which differentiates Oct-2 from Oct-1, also activated transcription in conjunction with the heterologous GAL4 DNA-binding domain. Oct-2 thus contains three modular functional units, the DNA-binding POU domain and the two P and Q activation domains. An electrophoretic mobility shift assay with a variety of these Oct-2 activators revealed a distinct complex called QA that was dependent on the presence of an active glutamine-rich activation domain and migrated more slowly than the Oct-2-DNA complexes. Formation of the QA complex is consistent with interaction of the glutamine-rich activation domains with a regulatory protein important for the process of transcriptional activation.
Mots-clé
Amino Acid Sequence, Base Sequence, DNA-Binding Proteins/metabolism, DNA-Binding Proteins/physiology, Fungal Proteins, Gene Expression Regulation, Hela Cells, Humans, Molecular Sequence Data, Octamer Transcription Factor-2, Oligonucleotide Probes/chemistry, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Structure-Activity Relationship, Transcription Factors, Transcription, Genetic, Transcriptional Activation
Pubmed
Web of science
Création de la notice
24/01/2008 16:36
Dernière modification de la notice
20/08/2019 17:29
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