DRADA

DRADA
	Existing structural data : 1QBJ , 1QGP , 1XMK , 2ACJ , 2GXB , 2L54 , 2MDR , 3F21 , 3F22 , 3F23 , 3IRQ , 3IRR
Properties of human protein
Mass / length primary structure	1226 amino acids
Secondary to quaternary structure	Homodimer
Cofactor	Zn 2+
Isoforms	5
Identifier
Gene names	ADAR ADAR1; AGS6; DRADA; DSH; DSRAD; G1P1; IFI-4; IFI4; K88DSRBP; P136
External IDs	OMIM : 146920 ; UniProt : P55265 ; MGI : 1889575 ;
Enzyme classification
EC, category	3.5.4.4 , adenosine deaminase
Occurrence
Homology family	ADAR
Parent taxon	Euteleostomi
	Orthologue

DRADA (abbreviation for double-stranded RNA-specific adenosine deaminase ) is an enzyme in the cells of vertebrates . DRADA converts adenosine - nucleotide building blocks within RNA to inosine . On the one hand, this reaction is part of the RNA editing of own mRNA in the nucleus . On the other hand, this can destroy the genetic information of virus RNA that has penetrated the cell . In humans, DRADA occurs in all tissue types, but especially in activated T cells , in the brain and the lungs . Mutations in the ADAR - gene can enzyme deficiency and run this to a (rare) skin disease.

${\ displaystyle \ mathrm {\ {\ xrightarrow {DRADA}}}}$

Deamination of adenosine to inosine

Inosine is considered guanosine during translation of RNA . Therefore, changing the RNA from adenosine to inosine will end up producing an altered protein. This is the protein - diversity increased considerably in the organism. The large number of proteins achieved by DRADA is vital for the organisms, since, for example, the glutamate receptor protein can only be produced in this way.

There is some evidence that reducing enzyme activity in mice could be helpful in treating melanoma . Surprisingly, DRADA is necessary for the HI virus to reproduce. Obviously, the RNA editing mechanism is used by the virus to splice its RNA.

Individual evidence

↑ ^a ^b UniProt P55265
↑ Laxminarayana D, Khan IU, O'Rourke KS, Giri B: Induction of 150-kDa adenosine deaminase that acts on RNA (ADAR) -1 gene expression in normal T lymphocytes by anti-CD3-epsilon and anti-CD28 . In: Immunology . 122, No. 4, December 2007, pp. 623-633. doi : 10.1111 / j.1365-2567.2007.02709.x . PMID 17897325 . PMC 2266038 (free full text).
↑ Hong J, Zhao Y, Li Z, Huang W: esiRNA to eri-1 and adar-1 genes improving high doses of c-myc-directed esiRNA effect on mouse melanoma growth inhibition . In: Biochem. Biophys. Res. Commun. . 361, No. 2, September 2007, pp. 373-378. doi : 10.1016 / j.bbrc.2007.07.003 . PMID 17658462 .
↑ Phuphuakrat A, Kraiwong R, Boonarkart C, Lauhakirti D, Lee TH, Auewarakul P: Double-stranded RNA adenosine deaminases enhance expression of human immunodeficiency virus type 1 proteins . In: J. Virol. . 82, No. 21, November 2008, pp. 10864-10872. doi : 10.1128 / JVI.00238-08 . PMID 18753201 .

literature

A. Gallo, S. Galardi: A-to-I RNA editing and cancer: from pathology to basic science. In: RNA Biol. , Vol. 5, No. 3, 2008, pp. 135-139. PMID 18758244 .

Web links

reactome.org: Deamination at C6 position of adenosine in Editosome (ADAR1)

[u-1] UniProt P55265

[2] Laxminarayana D, Khan IU, O'Rourke KS, Giri B: Induction of 150-kDa adenosine deaminase that acts on RNA (ADAR) -1 gene expression in normal T lymphocytes by anti-CD3-epsilon and anti-CD28 . In: Immunology . 122, No. 4, December 2007, pp. 623-633. doi : 10.1111 / j.1365-2567.2007.02709.x . PMID 17897325 . PMC 2266038 (free full text).

[3] Hong J, Zhao Y, Li Z, Huang W: esiRNA to eri-1 and adar-1 genes improving high doses of c-myc-directed esiRNA effect on mouse melanoma growth inhibition . In: Biochem. Biophys. Res. Commun. . 361, No. 2, September 2007, pp. 373-378. doi : 10.1016 / j.bbrc.2007.07.003 . PMID 17658462 .

[4] Phuphuakrat A, Kraiwong R, Boonarkart C, Lauhakirti D, Lee TH, Auewarakul P: Double-stranded RNA adenosine deaminases enhance expression of human immunodeficiency virus type 1 proteins . In: J. Virol. . 82, No. 21, November 2008, pp. 10864-10872. doi : 10.1128 / JVI.00238-08 . PMID 18753201 .