生物物理
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
総説
1分子観察から見えてきた大腸菌ヘリカーゼUvrDのDNA巻き戻し機能と多量体形成
横田 浩章
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ジャーナル フリー

2021 年 61 巻 4 号 p. 227-231

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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.

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© 2021 by THE BIOPHYSICAL SOCIETY OF JAPAN
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