Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation

Tanaka, M., Herr, W. (February 1990) Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation. Cell, 60 (3). pp. 375-86. ISSN 0092-8674 (Print)0092-8674 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/2302733
DOI: 10.1016/0092-8674(90)90589-7

Abstract

The ubiquitous Oct-1 and lymphoid Oct-2 POU homeodomain transcription factors bind to the same DNA sequence but differ in their activation potential. Oct-2 is a positive, negative, or neutral regulator of beta-globin transcription depending on the position and sequence of multimerized binding sites. To activate transcription, Oct-2 relies on two interdependent nonacidic domains, an N-terminal glutamine-rich region and a C-terminal serine-, threonine-, and proline-rich region. Oct-1 also contains a functional glutamine-rich region but fails to activate beta-globin transcription in our assay because the Oct-1 C-terminus is inactive, indicating that differential activation by Oct-1 and Oct-2 is determined by the combination of multiple activation domains. Oct-2 displays a unique phosphorylation pattern that is absent from molecules lacking one or the other activation domain, suggesting the activation domains have a role in inducing protein phosphorylation.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Base Sequence DNA-Binding Proteins/*metabolism Gene Expression Regulation Genetic Vectors Globins/*genetics HeLa Cells/metabolism Host Cell Factor C1 Humans Molecular Sequence Data Octamer Transcription Factor-1 Octamer Transcription Factor-2 Oligonucleotide Probes Phosphorylation Promoter Regions, Genetic Protein Biosynthesis Transcription Factors/*metabolism Transcription, Genetic *Transcriptional Activation
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor
CSHL Authors:
Communities: CSHL labs > Herr lab
Depositing User: Matt Covey
Date: 9 February 1990
Date Deposited: 05 Apr 2016 16:35
Last Modified: 05 Apr 2016 16:35
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32276

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