Spectroscopic Characterization of a DNA-Binding Domain, Zα, from the Editing Enzyme, dsRNA Adenosine Deaminase: Evidence for Left-Handed Z-DNA in the Zα−DNA Complex
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. Zα, an N-terminal domain of human ADAR1 encompassing 76 amino acid residues, shows apparent specificity for the left-handed Z-DNA co...
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| Veröffentlicht in: | Biochemistry (Easton) 1998-09, Vol.37 (38), p.13313-13321 |
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| container_title | Biochemistry (Easton) |
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| creator | Berger, Imre Winston, William Manoharan, Ramasamy Schwartz, Thomas Alfken, Jens Kim, Yang-Gyun Lowenhaupt, Ky Herbert, Alan Rich, Alexander |
| description | 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. Zα, 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 Zα 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. |
| doi_str_mv | 10.1021/bi9813126 |
| format | Article |
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Zα, 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 Zα 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.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi9813126</identifier><identifier>PMID: 9748339</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Adenosine Deaminase - chemistry ; Adenosine Deaminase - metabolism ; Amino Acid Sequence ; Animals ; Chickens ; Circular Dichroism ; Deoxycytidine - chemistry ; Deoxyguanosine - chemistry ; DNA - chemistry ; DNA - metabolism ; Hot Temperature ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Nucleic Acid Conformation ; Peptides - chemistry ; Polydeoxyribonucleotides - chemistry ; Protein Conformation ; Protein Denaturation ; RNA Editing ; RNA-Binding Proteins ; Space life sciences ; Spectrometry, Fluorescence ; Spectrum Analysis, Raman</subject><ispartof>Biochemistry (Easton), 1998-09, Vol.37 (38), p.13313-13321</ispartof><rights>Copyright © 1998 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a379t-55df4325c85ca700fb9c7f3cb07ccfc83a673b8447dd975def584644bf1953e83</citedby><cites>FETCH-LOGICAL-a379t-55df4325c85ca700fb9c7f3cb07ccfc83a673b8447dd975def584644bf1953e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bi9813126$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi9813126$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9748339$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Berger, Imre</creatorcontrib><creatorcontrib>Winston, William</creatorcontrib><creatorcontrib>Manoharan, Ramasamy</creatorcontrib><creatorcontrib>Schwartz, Thomas</creatorcontrib><creatorcontrib>Alfken, Jens</creatorcontrib><creatorcontrib>Kim, Yang-Gyun</creatorcontrib><creatorcontrib>Lowenhaupt, Ky</creatorcontrib><creatorcontrib>Herbert, Alan</creatorcontrib><creatorcontrib>Rich, Alexander</creatorcontrib><title>Spectroscopic Characterization of a DNA-Binding Domain, Zα, from the Editing Enzyme, dsRNA Adenosine Deaminase: Evidence for Left-Handed Z-DNA in the Zα−DNA Complex</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>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. 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Results from laser-Raman spectroscopy experiments provide direct evidence for the existence of Z-DNA in peptide−DNA complexes.</description><subject>Adenosine Deaminase - chemistry</subject><subject>Adenosine Deaminase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Chickens</subject><subject>Circular Dichroism</subject><subject>Deoxycytidine - chemistry</subject><subject>Deoxyguanosine - chemistry</subject><subject>DNA - chemistry</subject><subject>DNA - metabolism</subject><subject>Hot Temperature</subject><subject>Humans</subject><subject>Macromolecular Substances</subject><subject>Molecular Sequence Data</subject><subject>Nucleic Acid Conformation</subject><subject>Peptides - chemistry</subject><subject>Polydeoxyribonucleotides - chemistry</subject><subject>Protein Conformation</subject><subject>Protein Denaturation</subject><subject>RNA Editing</subject><subject>RNA-Binding Proteins</subject><subject>Space life sciences</subject><subject>Spectrometry, Fluorescence</subject><subject>Spectrum Analysis, Raman</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1uEzEAhUcIVEJhwQGQvAEJKQN2bI_H7MIktEhRQG3ZdGN5_ENdMvZgT1DbFUvYcg1WXIRD9CQ4JMoKiZVlv0_vye8VxWMEXyA4QS9bx2uE0aS6U4wQncCScE7vFiMIYVVOeAXvFw9SusxXAhk5KA44IzXGfFT8PO2NGmJIKvROgeZCRqkGE92NHFzwIFggwWw5LV87r53_CGahk86PwfnvX2NgY-jAcGHAXLtho879zXVnxkCnk-UUTLXxITlvwMzIznmZzKvbr9_B_IvLijLAhggWxg7lsfTaaHBe5ijg_F_PnHD77cfmoQldvzJXD4t7Vq6SebQ7D4sPb-ZnzXG5eHf0tpkuSokZH0pKtSV4QlVNlWQQ2pYrZrFqIVPKqhrLiuG2JoRpzRnVxtKaVIS0FnGKTY0Pi2db3z6Gz2uTBtG5pMxqJb0J6yQY5iiXSv4LIoZqBgnL4PMtqHLTKRor-ug6Ga8FgmKzoNgvmNknO9N12xm9J3eTZb3c6i4N5movy_hJ5H8xKs7en4qjaolPaMNFk_mnW16qJC7DOvrc3T9y_wDOxrM1</recordid><startdate>19980922</startdate><enddate>19980922</enddate><creator>Berger, Imre</creator><creator>Winston, William</creator><creator>Manoharan, Ramasamy</creator><creator>Schwartz, Thomas</creator><creator>Alfken, Jens</creator><creator>Kim, Yang-Gyun</creator><creator>Lowenhaupt, Ky</creator><creator>Herbert, Alan</creator><creator>Rich, Alexander</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19980922</creationdate><title>Spectroscopic Characterization of a DNA-Binding Domain, Zα, from the Editing Enzyme, dsRNA Adenosine Deaminase: Evidence for Left-Handed Z-DNA in the Zα−DNA Complex</title><author>Berger, Imre ; 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Zα, 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 Zα 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.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>9748339</pmid><doi>10.1021/bi9813126</doi><tpages>9</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1998-09, Vol.37 (38), p.13313-13321 |
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| subjects | Adenosine Deaminase - chemistry Adenosine Deaminase - metabolism Amino Acid Sequence Animals Chickens Circular Dichroism Deoxycytidine - chemistry Deoxyguanosine - chemistry DNA - chemistry DNA - metabolism Hot Temperature Humans Macromolecular Substances Molecular Sequence Data Nucleic Acid Conformation Peptides - chemistry Polydeoxyribonucleotides - chemistry Protein Conformation Protein Denaturation RNA Editing RNA-Binding Proteins Space life sciences Spectrometry, Fluorescence Spectrum Analysis, Raman |
| title | Spectroscopic Characterization of a DNA-Binding Domain, Zα, from the Editing Enzyme, dsRNA Adenosine Deaminase: Evidence for Left-Handed Z-DNA in the Zα−DNA Complex |
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