著者

横田 浩章

出版者

一般社団法人 日本生物物理学会

雑誌

生物物理 (ISSN:05824052)

巻号頁・発行日

vol.61, no.4, pp.227-231, 2021 (Released:2021-07-30)

参考文献数

20

被引用文献数

1

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The Escherichia coli UvrD protein is a superfamily 1, non-hexameric DNA helicase that plays a crucial role in repair mechanisms. Previous studies suggested that wild-type UvrD has optimal activity in its oligomeric form. Nevertheless, a conflicting monomer model was proposed using a UvrD mutant lacking the C-terminal 40 amino acids (UvrDΔ40C). Here, single-molecule direct visualization of UvrDΔ40C revealed that two or three UvrDΔ40C molecules were simultaneously involved in DNA unwinding, presumably in an oligomeric form, similar to that with wild-type UvrD. Thus, single-molecule direct visualization of nucleic acid-binding proteins provides quantitative and kinetic information to address their fundamental mechanisms.