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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 (MuB)
Title: MuB is an AAA+ ATPase that forms helical filaments to control target selection for DNA transposition.
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A subset of the six subunits of MuA associated with their cognate sub-sites at L and R communicate with the enhancer to trigger the stepwise assembly of the functional transpososome
Title: Interactions of phage Mu enhancer and termini that specify the assembly of a topologically unique interwrapped transpososome.
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gp44 is an essential protein for baseplate assembly & forms a trimer comprising a complex consisting of 42 kDa & 40 kDa subunits that had been cleaved in C-terminal region. Thermodynamic analysis shows that C-terminal region forms a flexible domain[gp44]
Title: Expression and characterization of a baseplate protein for bacteriophage Mu, gp44.
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Data show that gp44 exists as a trimer exhibiting a hub-like structure with an inner diameter of 25 angstroms through which DNA can presumably pass during infection [gp44].
Title: Structure of the central hub of bacteriophage Mu baseplate determined by X-ray crystallography of gp44.
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Bacteriophage Mu baseplate protein gene product 44 (gp44) crystsals diffract X-rays to at least 2.1 A resolution and are stable in the X-ray beam and are therefore appropriate for structure determination (gp44)
Title: Crystallization and preliminary X-ray analysis of gene product 44 from bacteriophage Mu.
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MuA assembles DNA hairpin substrates into a catalytically competent transpososome, open the hairpin ends and accurately join the opened ends to the target DNA (MuA).
Title: Characteristics of MuA transposase-catalyzed processing of model transposon end DNA hairpin substrates.
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contribution of both MuA and DNA supercoiling to the 5-noded Mu synapse built at the 3-way junction [transposase MuA]
Title: The Mu transposase interwraps distant DNA sites within a functional transpososome in the absence of DNA supercoiling.