Double-stranded RNA-specific adenosine deaminase: Nucleic acid binding properties

被引:29
作者
Liu, Y
Herbert, A
Rich, A
Samuel, CE [1 ]
机构
[1] Univ Calif Santa Barbara, Dept Mol Cellular & Dev Biol, Santa Barbara, CA 93106 USA
[2] Univ Calif Santa Barbara, Interdept Grad Program Biochem & Mol Biol, Santa Barbara, CA 93106 USA
[3] MIT, Dept Biol, Cambridge, MA 02139 USA
关键词
D O I
10.1006/meth.1998.0624
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The RNA-specific adenosine deaminase (ADAR1, herein referred to as ADAR) 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 substrates. ADAR possesses three functionally distinct copies of the highly conserved double-stranded RNA binding R motif (R-I, R-II, R-III) implicated in the recognition of dsRNA structures within the substrate RNAs. ADAR is also a Z-DNA-binding protein. Two Z-DNA binding motifs (Z alpha and Z beta) present in ADAR correspond to repeated regions homologous 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.
引用
收藏
页码:199 / 205
页数:7
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