The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

TfIIA-S  -  Transcription-factor-IIA-S

Drosophila melanogaster

Synonyms: BcDNA:RE44302, CG5163, Dmel\CG5163, F121, General transcription factor IIA subunit 2, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on TfIIA-S

  • Drosophila TFIIA-S is up-regulated and required during Ras-mediated photoreceptor determination [1].
  • Subunit interaction studies indicate that dTFIIA-S binds to an amino-terminal domain of dTFIIA-L, which likely corresponds to the endogenous 30-kD processed species [2].
  • Drosophila TFIIA directs cooperative DNA binding with TBP and mediates transcriptional activation [2].
  • Importantly, this phenotype is suppressed by overexpression of the TFIIA subunits, indicating that the yTAF145 inhibitory domain is involved in TFIIA function [3].
 

Other interactions of TfIIA-S

  • We reported previously the characterization of cDNAs that encode a precursor (dTFIIA-L) of the Drosophila TFIIA 30- and 20-kD subunits [2].
 

Analytical, diagnostic and therapeutic context of TfIIA-S

References

  1. Drosophila TFIIA-S is up-regulated and required during Ras-mediated photoreceptor determination. Zeidler, M.P., Yokomori, K., Tjian, R., Mlodzik, M. Genes Dev. (1996) [Pubmed]
  2. Drosophila TFIIA directs cooperative DNA binding with TBP and mediates transcriptional activation. Yokomori, K., Zeidler, M.P., Chen, J.L., Verrijzer, C.P., Mlodzik, M., Tjian, R. Genes Dev. (1994) [Pubmed]
  3. The yeast TAF145 inhibitory domain and TFIIA competitively bind to TATA-binding protein. Kokubo, T., Swanson, M.J., Nishikawa, J.I., Hinnebusch, A.G., Nakatani, Y. Mol. Cell. Biol. (1998) [Pubmed]
 
WikiGenes - Universities