English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

New type of POU domain in germ line-specific protein Oct-4.

MPS-Authors

Schoeler,  H.
Max Planck Society;

/persons/resource/persons15899

Suzuki,  N.
Department of Molecular Cell Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14945

Chowdhury,  K.
Department of Molecular Cell Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15156

Gruss,  P.
Department of Molecular Cell Biology, MPI for biophysical chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

603024.pdf
(Publisher version), 764KB

Supplementary Material (public)
There is no public supplementary material available
Citation

Schoeler, H., Ruppert, S., Suzuki, N., Chowdhury, K., & Gruss, P. (1990). New type of POU domain in germ line-specific protein Oct-4. Nature, 344(6265), 435-439. doi:10.1038/344435a0.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0013-0E16-F
Abstract
Members of a family of murine octamer-binding proteins interact specifically with the octamer motif, a transcription regulatory element found in the promoter and enhancer regions of many genes. Oct-4 is a maternally expressed protein that is also present in the pre-implantation mouse embryo. Although many regulatory proteins are expressed in post-implantation embryos, transcription factors regulating pre-implantation processes have remained elusive. The Oct-4 gene is therefore a prime candidate for an early developmental control gene. Here we report the complementary DNA cloning of the mouse Oct-4 gene, and the characterization of the encoded protein(s) by sequential in vitro transcription, translation, DNA-binding and protease-clipping analysis. Deletion analysis shows that the DNA-binding activity is mediated by a POU domain encoded in an open reading frame corresponding to a 324-amino-acid protein. Sequence comparison with known POU domains reveals that Oct-4 is a novel member of the POU-family.