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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

DRAP1  -  DR1-associated protein 1 (negative...

Homo sapiens

Synonyms: Dr1-associated corepressor, Dr1-associated protein 1, NC2-alpha, Negative cofactor 2-alpha
 
 
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High impact information on DRAP1

  • A model for DRAP1-dependent, Dr1-mediated repression of transcription is proposed [1].
  • A Dr1-associated polypeptide (DRAP1) was isolated from HeLa cells and found to function as a corepressor of transcription [1].
  • The confirmed interacting proteins include FEZ1 itself and three transcription controlling proteins (SAP30L, DRAP1, and BAF60a) [2].
  • At least eight genes with homologies to CBF-C are present in the Arabidopsis genome; one of them exhibits striking similarities to the gene for the human global transcriptional repressor Drap1 [3].
  • The two DR1-associated cellular specificities Dw1 and Dw20, as well as DR'Br' (Dw'BON'), cannot be unequivocally assigned by serological typing or restriction fragment length polymorphism (RFLP) analysis [4].
 

Biological context of DRAP1

  • Here we show that the transcriptional corepressor DRAP1 has a very specific role in regulation of Nodal activity during mouse embryogenesis [5].
  • This DR1-associated polymorphism has been identified as Dw20 by the Tenth International Histocompatibility Workshop. The molecular basis for this altered recognition of the DR1 molecule was determined by allele-specific oligonucleotide hybridization and by DNA sequencing studies [6].
 

Associations of DRAP1 with chemical compounds

 

Physical interactions of DRAP1

  • In the absence of the tethering domain, Dr1 interacts with its corepressor DRAP1, but this interaction is not functional [8].
 

Other interactions of DRAP1

  • Here, we investigated whether activator-reversible transcription repression by NC2 (Dr1/DRAP1) contributes to maximum induction levels in unfractionated HeLa nuclear extracts [9].
  • Interestingly, the gene locus encoding BLES03 is located between genes encoding the proteins DRAP1 and FOSL1, both of which are involved in transcription initiation [10].
 

Analytical, diagnostic and therapeutic context of DRAP1

References

  1. Requirement of a corepressor for Dr1-mediated repression of transcription. Mermelstein, F., Yeung, K., Cao, J., Inostroza, J.A., Erdjument-Bromage, H., Eagelson, K., Landsman, D., Levitt, P., Tempst, P., Reinberg, D. Genes Dev. (1996) [Pubmed]
  2. FEZ1 dimerization and interaction with transcription regulatory proteins involves its coiled-coil region. Assmann, E.M., Alborghetti, M.R., Camargo, M.E., Kobarg, J. J. Biol. Chem. (2006) [Pubmed]
  3. The assembly of the CAAT-box binding complex at a photosynthesis gene promoter is regulated by light, cytokinin, and the stage of the plastids. Kusnetsov, V., Landsberger, M., Meurer, J., Oelmüller, R. J. Biol. Chem. (1999) [Pubmed]
  4. HLA-DRB1*01 subtyping by allele-specific PCR amplification: a sensitive, specific and rapid technique. Olerup, O., Zetterquist, H. Tissue Antigens (1991) [Pubmed]
  5. Inhibition of excess nodal signaling during mouse gastrulation by the transcriptional corepressor DRAP1. Iratni, R., Yan, Y.T., Chen, C., Ding, J., Zhang, Y., Price, S.M., Reinberg, D., Shen, M.M. Science (2002) [Pubmed]
  6. Involvement of class II beta-chain amino acid residues 85 and 86 in T-cell allorecognition. Eckels, D.D., Geiger, M.J., Sell, T.W., Gorski, J.A. Hum. Immunol. (1990) [Pubmed]
  7. Behavioural and histological effects of atrazine on freshwater molluscs (Physa acuta Drap. and Ancylus fluviatilis Müll. Gastropoda). Rosés, N., Poquet, M., Muñoz, I. Journal of applied toxicology : JAT. (1999) [Pubmed]
  8. Functional dissection of a human Dr1-DRAP1 repressor complex. Yeung, K., Kim, S., Reinberg, D. Mol. Cell. Biol. (1997) [Pubmed]
  9. The C-terminal domain-phosphorylated IIO form of RNA polymerase II is associated with the transcription repressor NC2 (Dr1/DRAP1) and is required for transcription activation in human nuclear extracts. Castaño, E., Gross, P., Wang, Z., Roeder, R.G., Oelgeschläger, T. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  10. The structure at 2.5 A resolution of human basophilic leukemia-expressed protein BLES03. Bitto, E., Bingman, C.A., Robinson, H., Allard, S.T., Wesenberg, G.E., Phillips, G.N. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
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