Spectroscopic characterization of a DNA-binding domain, Z alpha from the editing enzyme, dsRNA adenosine deaminase: Evidence for left-handed Z-DNA in the Z alpha-DNA complex

Berger I.; Manoharan R.; Schwartz T.; Alfken J.; Kim YG. Lowenhaupt K.; Herbert A.; Rich A.; Winston W.

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Spectroscopic characterization of a DNA-binding domain, Z alpha from the editing enzyme, dsRNA adenosine deaminase: Evidence for left-handed Z-DNA in the Z alpha-DNA complex

机译：DNA结合结构域，编辑酶dsRNA腺苷脱氨酶的Z alpha的光谱表征：Z alpha-DNA复合物中左手Z-DNA的证据

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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. Z alpha, 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 Z alpha 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. [References: 50]

机译：双链RNA腺苷脱氨酶（ADAR1）是后生动物中的一种普遍存在的酶，它编辑前mRNA，将双链RNA区域中的腺苷变为肌苷。 Z alpha是人类ADAR1的N端结构域，包含76个氨基酸残基，它对通过溴化或甲基化修饰的交替（dGdC）聚合物采用的左手Z-DNA构象以及（dGdC）表现出明显的特异性（ 13）存在于超螺旋质粒中的插入片段。在此，结合了圆二色性，荧光和凝胶延迟研究，以表征重组Zα肽并检查其与DNA的相互作用。激光拉曼光谱实验的结果为肽DNA络合物中Z DNA的存在提供了直接证据。 [参考：50]

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《Biochemistry》 |1998年第38期|共9页
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Berger I.; Manoharan R.; Schwartz T.; Alfken J.; Kim YG. Lowenhaupt K.; Herbert A.; Rich A.; Winston W.;
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1. Spectroscopic characterization of a DNA-binding domain, Z alpha from the editing enzyme, dsRNA adenosine deaminase: Evidence for left-handed Z-DNA in the Z alpha-DNA complex [J] . Berger I., Manoharan R., Schwartz T., Biochemistry . 1998,第38期

机译：DNA结合结构域，编辑酶dsRNA腺苷脱氨酶的Z alpha的光谱表征：Z alpha-DNA复合物中左手Z-DNA的证据
2. Spectroscopic characterization of a DNA-binding domain, Z alpha from the editing enzyme, dsRNA adenosine deaminase: Evidence for left-handed Z-DNA in the Z alpha-DNA complex [J] . Berger I., Manoharan R., Schwartz T., Biochemistry . 1998,第38期

机译：DNA结合结构域，编辑酶dsRNA腺苷脱氨酶的Z alpha的光谱表征：Z alpha-DNA复合物中左手Z-DNA的证据
3. The Zα domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA [J] . Bernard A. Brown II, Ky Lowenhaupt, Christina M. Wiibert Proceedings of the National Academy of Sciences of the United States of America . 2000,第25期

机译：编辑酶dsRNA腺苷脱氨酶的Zα结构域与左手Z-RNA以及Z-DNA结合
4. Spectroscopic and theoretical studies on the {FENO}7 complexes of alpha-ketoacid-dependent and related enzymes: Using nitric oxide as a probe of oxygen reactivity [D] . Brown, Christina Dawn 2008

机译：关于α-酮酸依赖性酶和相关酶的{FENO} 7配合物的光谱和理论研究：使用一氧化氮作为氧反应性的探针
5. The Zα domain of the editing enzyme dsRNA adenosine deaminase binds left-handed Z-RNA as well as Z-DNA [O] . Bernard A. Brown II, Ky Lowenhaupt, Christina M. Wilbert, 2000

机译：编辑酶dsRNA腺苷脱氨酶的Zα域结合左手Z-RNA和Z-DNA
6. The role of binding domains for dsRNA and Z-DNA in the in vivo editing of minimal substrates by ADAR1 [O] . Herbert, Alan, Rich, Alexander 2001

机译：dsRNA和Z-DNA结合域在ADAR1体内最小限度底物编辑中的作用

Spectroscopic characterization of a DNA-binding domain, Z alpha from the editing enzyme, dsRNA adenosine deaminase: Evidence for left-handed Z-DNA in the Z alpha-DNA complex

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