DNA Unwinding and Oligomerization Dynamics of <i>Escherichia coli</i> UvrD Helicase Revealed by Single-molecule Fluorescence Imaging

• YOKOTA Hiroaki

  The Graduate School for the Creation of Photonics Industries

Bibliographic Information

Other Title

• 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

Abstract

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.

Journal

• Seibutsu Butsuri

  Seibutsu Butsuri 61 (4), 227-231, 2021

  The Biophysical Society of Japan General Incorporated Association

Keywords

• protein-nucleic acid interactions
• single-molecule fluorescence imaging
• helicase
• protein assemblies
• enzyme function
• C-terminal amino acids

Details

• CRID: 1390288867187714688
• NII Article ID: 130008068992
• NII Book ID: AN00129693
• DOI: 10.2142/biophys.61.227
• ISSN: 13474219
• ISSN: 05824052
• NDL BIB ID: 031678646
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I031678646
• Web Site: https://www.jstage.jst.go.jp/article/biophys/61/4/61_227/_pdf
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed