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嗜热栖热菌DNA聚合酶IV全长与DNA二元复合物的主链归属

Backbone assignment of the binary complex of the full length Sulfolobus solfataricus DNA polymerase IV and DNA.

作者信息

Lee Eunjeong, Fowler Jason D, Suo Zucai, Wu Zhengrong

机构信息

Department of Chemistry and Biochemistry, The Ohio State University, 876 Biological Sciences, 484 West 12th Ave., Columbus, OH, 43210, USA.

出版信息

Biomol NMR Assign. 2017 Apr;11(1):39-43. doi: 10.1007/s12104-016-9717-4. Epub 2016 Oct 13.

DOI:10.1007/s12104-016-9717-4
PMID:27738883
Abstract

Sulfolobus solfataricus DNA polymerase IV (Dpo4), a model Y-family DNA polymerase, bypasses a wide range of DNA lesions in vitro and in vivo. In this paper, we report the backbone chemical shift assignments of the full length Dpo4 in its binary complex with a 14/14-mer DNA substrate. Upon DNA binding, several β-stranded regions in the isolated catalytic core and little finger/linker fragments of Dpo4 become more structured. This work serves as a foundation for our ongoing investigation of conformational dynamics of Dpo4 and future determination of the first solution structures of a DNA polymerase and its binary and ternary complexes.

摘要

嗜热栖热菌DNA聚合酶IV(Dpo4)是Y家族DNA聚合酶的一个模型,它在体外和体内都能绕过多种DNA损伤。在本文中,我们报告了全长Dpo4与14/14-mer DNA底物二元复合物的主链化学位移归属。DNA结合后,Dpo4分离的催化核心以及小指/连接片段中的几个β链区域变得更加有序。这项工作为我们正在进行的Dpo4构象动力学研究以及未来确定DNA聚合酶及其二元和三元复合物的首个溶液结构奠定了基础。

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引用本文的文献

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Investigating the Conformational Dynamics of a Y-Family DNA Polymerase during Its Folding and Binding to DNA and a Nucleotide.研究Y家族DNA聚合酶在折叠过程中以及与DNA和核苷酸结合时的构象动力学。
JACS Au. 2021 Dec 16;2(2):341-356. doi: 10.1021/jacsau.1c00368. eCollection 2022 Feb 28.
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Investigating the trade-off between folding and function in a multidomain Y-family DNA polymerase.研究多结构域 Y 家族 DNA 聚合酶中折叠与功能之间的权衡。
Elife. 2020 Oct 20;9:e60434. doi: 10.7554/eLife.60434.