| Literature DB >> 9735305 |
Y Liu1, A Herbert, A Rich, C E Samuel.
Abstract
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 (RI, RII, RIII) implicated in the recognition of dsRNA structures within the substrate RNAs. ADAR is also a Z-DNA-binding protein. Two Z-DNA binding motifs (Zalpha and Zbeta) 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. Copyright 1998 Academic Press.Entities:
Keywords: Non-programmatic
Mesh:
Substances:
Year: 1998 PMID: 9735305 DOI: 10.1006/meth.1998.0624
Source DB: PubMed Journal: Methods ISSN: 1046-2023 Impact factor: 3.608