de.mpg.escidoc.pubman.appbase.FacesBean
English
 
Help Guide Disclaimer Contact us Login
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78408

Mizuno,  Naoko
Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons101697

Adam,  Julia
Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-4E9E-0
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.