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

Tanaka, M., Clouston, W. M., Herr, W. (September 1994) The Oct-2 glutamine-rich and proline-rich activation domains can synergize with each other or duplicates of themselves to activate transcription. Mol Cell Biol, 14 (9). pp. 6046-55. ISSN 0270-7306 (Print)

URL: http://www.ncbi.nlm.nih.gov/pubmed/8065338
DOI: 10.1128/MCB.14.9.6046

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Base Sequence DNA-Binding Proteins/metabolism/ physiology Fungal Proteins Gene Expression Regulation Hela Cells Humans In Vitro Molecular Sequence Data Octamer Transcription Factor-2 Oligonucleotide Probes/chemistry Recombinant Fusion Proteins Research Support, U.S. Gov't, P.H.S. Saccharomyces cerevisiae Proteins Structure-Activity Relationship Trans-Activation (Genetics) Transcription Factors Transcription, Genetic
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Matt Covey
Date: September 1994
Date Deposited: 05 Aug 2015 19:23
Last Modified: 05 Aug 2015 19:23
PMCID: PMC359131
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31448

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