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.
journal_name
Proc Natl Acad Sci U S Aauthors
Mizuno N,Dramićanin M,Mizuuchi M,Adam J,Wang Y,Han YW,Yang W,Steven AC,Mizuuchi K,Ramón-Maiques Sdoi
10.1073/pnas.1309499110subject
Has Abstractpub_date
2013-07-02 00:00:00pages
E2441-50issue
27eissn
0027-8424issn
1091-6490pii
1309499110journal_volume
110pub_type
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