Differential transcriptional activation by Oct-1 and Oct-2: Interdependent activation domains induce Oct-2 phosphorylation
CellPublished 1 February 1990
Masafumi Tanaka, Winship Herr
Citations669
SJR quartileQ1
SJR score22.61
SNIP7.62
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TL;DR
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 phosphorylated.
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.
Keywords
Biochemistry, Genetics and Molecular Biology
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