DOUBLE-STRANDED RNA-SPECIFIC ADENOSINE-DEAMINASE - NUCLEIC-ACID BINDING-PROPERTIES

Citation
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
Citations number
42
Categorie Soggetti
Biology,"Biochemical Research Methods
ISSN journal
10462023
Volume
15
Issue
3
Year of publication
1998
Pages
199 - 205
Database
ISI
SICI code
1046-2023(1998)15:3<199:DRA-NB>2.0.ZU;2-K
Abstract
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.