Y. Liu et al., DOUBLE-STRANDED RNA-SPECIFIC ADENOSINE-DEAMINASE - NUCLEIC-ACID BINDING-PROPERTIES, Methods (San Diego, Calif., Print), 15(3), 1998, pp. 199-205
The RNA-specific adenosine deaminase (ADAR1, herein referred to as ADA
R) is an interferon-inducible RNA-editing enzyme. ADAR catalyzes the C
-6 deamination of adenosine in double-stranded (ds) structures present
in viral RNAs and cellular pre-mRNAs as well as synthetic dsRNA subst
rates. ADAR possesses three functionally distinct copies of the highly
conserved double-stranded RNA binding R motif (R-I, R-II, R-III) impl
icated in the recognition of dsRNA structures within the substrate RNA
s. ADAR is also a Z-DNA-binding protein. Two Z-DNA binding motifs (Z a
lpha and Z beta) present in ADAR correspond to repeated regions homolo
gous to the N-terminal region of the vaccinia virus E3L protein. Here
we describe assay methods for measurement of ADAR enzymatic activity,
dsRNA binding activity, and Z-DNA binding activity. (C) 1998 Academic
Press.