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XB-ART-40931
J Biol Chem March 12, 2010; 285 (11): 8408-21.

Reversal of Xenopus Oct25 function by disruption of the POU domain structure.

Cao Y , Oswald F , Wacker SA , Bundschu K , Knöchel W .


Abstract
Xenopus Oct25 is a POU family subclass V (POU-V) transcription factor with a distinct domain structure. To investigate the contribution of different domains to the function of Oct25, we have performed gain of function analyses. Deletions of the N- or C-terminal regions and of the Hox domain (except its nuclear localization signal) result in mutants being indistinguishable from the wild type protein in the suppression of genes promoting germ layer formation. Deletion of the complete POU domain generates a mutant that has no effect on embryogenesis. However, disruption of the alpha-helical structures in the POU domain, even by a single amino acid mutation, causes reversal of protein function. Overexpression of such mutants leads to dorsalization of embryos and formation of secondary axial structures. The underlying mechanism is an enhanced transcription of genes coding for antagonists of the ligands for ventralizing bone morphogenetic protein and Wnt pathways. Corresponding deletion mutants of Xenopus Oct60, Oct91, or mouse Oct4 also exhibit such a dominant-negative effect. Therefore, our results reveal that the integrity of the POU domain is crucial for the function of POU-V transcription factors in the regulation of genes that promote germ layer formation.

PubMed ID: 20064932
PMC ID: PMC2832990
Article link: J Biol Chem

Genes referenced: pou5f3.1 pou5f3.2 pou5f3.3 vegt
Morpholinos: vegt MO6

References:
Agius, 2000, Pubmed, Xenbase [+]


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