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

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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

  • Seibutsu Butsuri

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

    The Biophysical Society of Japan General Incorporated Association

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