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  MuB is an AAA plus ATPase that forms helical filaments to control target selection for DNA transposition

Mizuno, N., Dramicanin, M., Mizuuchi, M., Adam, J., Wang, Y., Han, Y.-W., et al. (2013). MuB is an AAA plus ATPase that forms helical filaments to control target selection for DNA transposition. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 110(27), E2441-E2450. doi:10.1073/pnas.1309499110.

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 Creators:
Mizuno, Naoko1, Author           
Dramicanin, Marija2, Author
Mizuuchi, Michiyo2, Author
Adam, Julia1, Author           
Wang, Yi2, Author
Han, Yong-Woon2, Author
Yang, Wei2, Author
Steven, Alasdair C.2, Author
Mizuuchi, Kiyoshi2, Author
Ramon-Maiques, Santiago2, Author
Affiliations:
1Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_1688137              
2external, ou_persistent22              

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Free keywords: C-TERMINAL DOMAIN; BACTERIOPHAGE-MU; B-PROTEIN; ELECTRON-MICROSCOPY; STRAND-TRANSFER; PHAGE-MU; STRUCTURE PREDICTION; IMMUNITY; BINDING; COMPLEXPhage Mu; nucleoprotein filament;
 Abstract: MuB is an ATP-dependent nonspecific DNA-binding protein that regulates the activity of the MuA transposase and captures target DNA for transposition. Mechanistic understanding of MuB function has previously been hindered by MuB's poor solubility. Here we combine bioinformatic, mutagenic, biochemical, and electron microscopic analyses to unmask the structure and function of MuB. We demonstrate that MuB is an ATPase associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or without DNA. We also identify critical residues for MuB's ATPase, DNA binding, protein polymerization, and MuA interaction activities. Using single-particle electron microscopy, we show that MuB assembles into a helical filament, which binds the DNA in the axial channel. The helical parameters of the MuB filament do not match those of the coated DNA. Despite this protein-DNA symmetry mismatch, MuB does not deform the DNA duplex. These findings, together with the influence of MuB filament size on strand-transfer efficiency, lead to a model in which MuB-imposed symmetry transiently deforms the DNA at the boundary of the MuB filament and results in a bent DNA favored by MuA for transposition.

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Language(s): eng - English
 Dates: 2013
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000321978000005
DOI: 10.1073/pnas.1309499110
 Degree: -

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Title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Source Genre: Journal
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Publ. Info: 2101 CONSTITUTION AVE NW, WASHINGTON, DC 20418 USA : NATL ACAD SCIENCES
Pages: - Volume / Issue: 110 (27) Sequence Number: - Start / End Page: E2441 - E2450 Identifier: ISSN: 0027-8424