Chicken double-stranded RNA adenosine deaminase has apparent specificity for Z-DNA.
A M(r) 140,000 protein has been purified from chicken lungs to apparent homogeneity. The protein binds with high affinity to a non-BNA conformation, which is most likely to the Z-DNA. The protein also has a binding site for double-stranded RNA (dsRNA). Peptide sequences from this protein show similarity to dsRNA adenosine deaminase, an enzyme that deaminates adenosine in dsRNA to form inosine. Assays for this enzyme confirm that dsRNA adenosine deaminase activity and Z-DNA binding are properties of the same molecule. The coupling of these two activities in a single molecule may indicate a distinctive mechanism of gene regulation that is, in part, dependent on DNA topology. As such, DNA topology, through its effects on the efficiency and extent of RNA editing may be important in the generation of new phenotypes during evolution.
Herbert
A
A
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
Lowenhaupt
K
K
Spitzner
J
J
Rich
A
A
D000243:Adenosine Deaminase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D004247:DNA / Q000737:chemistry; D006801:Humans; D066298:In Vitro Techniques; D008168:Lung / Q000201:enzymology; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016601:RNA-Binding Proteins; D051381:Rats; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D016601:RNA-Binding Proteins; D004247:DNA; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase