Disease relevance of ADARB2

• Two ketoreductases, RED1 and RED2, are involved in the biosynthesis of actinorhodin in Streptomyces coelicolor A3(2) and dihydrogranaticin in S. violaceoruber Tu22, respectively [1].

High impact information on ADARB2

• Interestingly, endogenous ADAR3 also appears to form a homodimer complex, indicating the presence of a brain-specific mechanism for ADAR3 dimerization [2].
• ADAR3 inhibited in vitro the activities of RNA editing enzymes of the ADAR gene family, raising the possibility of a regulatory role in RNA editing [3].
• A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains [3].
• We have isolated hADAR3, the third member of this class of human enzyme and investigated its editing site selectivity using in vitro RNA editing assay systems [3].
• Deletion mutagenesis identified a region rich in arginine residues located in the N-terminus that is responsible for binding of ADAR3 to ssRNA [3].

Biological context of ADARB2

• Localization of a novel human RNA-editing deaminase (hRED2 or ADARB2) to chromosome 10p15 [4].
• Using the sequence of rat RED2, we identified a homologous human expressed sequence tag, and subsequently designed primers in the 3' untranslated region of the hRED2 transcript to perform polymerase chain reaction amplification on two somatic cell hybrid mapping panels [4].

Associations of ADARB2 with chemical compounds

• Upon addition of methyl-coenzyme M, the red2 signal disappeared and the red1 signal increased again [5].
• We report here that in vitro the MCR-red2 state is converted into the MCR-ox1 state by the addition of polysulfide and into a light-sensitive MCR-ox2 state by the addition of sulfite [6].

Analytical, diagnostic and therapeutic context of ADARB2

• Homology modelling studies and site directed mutagenesis showed remarkable differences in three-dimensional structures and catalytic mechanisms between RED1 and RED2 [1].

References