Abstract
Double-stranded RNA adenosine deaminase (ADAR1) is an ubiquitous enzyme in metazoa that edits pre-mRNA changing adenosine to inosine in regions of double-stranded RNA. Zalpha, an N-terminal domain of human ADAR1 encompassing 76 amino acid residues, shows apparent specificity for the left-handed Z-DNA conformation adopted by alternating (dGdC) polymers modified by bromination or methylation, as well as for (dGdC)13 inserts present in supercoiled plasmids. Here, a combination of circular dichroism, fluorescence, and gel-retardation studies is utilized to characterize recombinant Zalpha peptide and to examine its interaction with DNA. Results from laser-Raman spectroscopy experiments provide direct evidence for the existence of Z-DNA in peptide-DNA complexes.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Deaminase / chemistry*
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Adenosine Deaminase / metabolism
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Amino Acid Sequence
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Animals
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Chickens
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Circular Dichroism
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DNA / chemistry*
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DNA / metabolism
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Deoxycytidine / chemistry
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Deoxyguanosine / chemistry
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Hot Temperature
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Humans
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Macromolecular Substances
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Molecular Sequence Data
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Nucleic Acid Conformation
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Peptides / chemistry
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Polydeoxyribonucleotides / chemistry
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Protein Conformation
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Protein Denaturation
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RNA Editing*
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RNA-Binding Proteins
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Spectrometry, Fluorescence
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Spectrum Analysis, Raman
Substances
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Macromolecular Substances
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Peptides
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Polydeoxyribonucleotides
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RNA-Binding Proteins
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Deoxycytidine
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poly(dC-dG)
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DNA
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ADARB1 protein, human
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Adenosine Deaminase
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Deoxyguanosine