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TitleMuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 110, Issue 27, Page E2441-E2450, Year 2013
Publish dateJul 2, 2013
AuthorsNaoko Mizuno / Marija Dramićanin / Michiyo Mizuuchi / Julia Adam / Yi Wang / Yong-Woon Han / Wei Yang / Alasdair C Steven / Kiyoshi Mizuuchi / Santiago Ramón-Maiques /
PubMed AbstractMuB 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:23776210 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution16.0 - 18.0 Å
Structure data

2395

4bs1

EMDB-2395: MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition
PDB-4bs1: MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA transposition
Method: EM (helical sym.) / Resolution: 18.0 Å

2398

4bt0

EMDB-2398: MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition
PDB-4bt0: MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA transposition
Method: EM (helical sym.) / Resolution: 17.0 Å

2400

4bt1

EMDB-2400: MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition
PDB-4bt1: MuB is an AAAplus ATPase that forms helical filaments to control target selection for DNA transposition
Method: EM (helical sym.) / Resolution: 16.0 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • enterobacteria phage mu (virus)
KeywordsHYDROLASE / AAA+ DNA TRANSPOSITION / NUCLEOPROTEIN FILAMENT / SYMMETRY MISMATCH / TRANSCRIPTION / AAA+ ATPASE / DNA TRANSPOSITION / AAAPLUS ATPASE

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