DNA Unwinding and Oligomerization Dynamics of <i>Escherichia coli</i> UvrD Helicase Revealed by Single-molecule Fluorescence Imaging
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- YOKOTA Hiroaki
- The Graduate School for the Creation of Photonics Industries
Bibliographic Information
- Other Title
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- 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
- 1 ブンシ カンサツ カラ ミエテ キタ ダイチョウキン ヘリカーゼ UvrD ノ DNA マキモドシ キノウ ト タリョウタイ ケイセイ
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Abstract
<p>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.</p>
Journal
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- Seibutsu Butsuri
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Seibutsu Butsuri 61 (4), 227-231, 2021
The Biophysical Society of Japan General Incorporated Association
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Keywords
Details
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- CRID
- 1390288867187714688
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- NII Article ID
- 130008068992
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- NII Book ID
- AN00129693
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- ISSN
- 13474219
- 05824052
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- NDL BIB ID
- 031678646
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed