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J. Biol. Chem., Vol. 265, Issue 3, 1623-1627, 01, 1990
BD Lavoie and G Chaconas
Stable protein-DNA complexes or transpososomes mediate the Mu DNA strand
transfer reaction in vitro (Surette, M. G., Buch, S. J., and Chaconas, G.
(1987) Cell 49, 253-262; Craigie, R., and Mizuuchi, K. (1987) Cell 51,
493-501). Formation of the Type 1 complex, an intermediate in the strand
transfer reaction, requires the Mu A and Escherichia coli HU proteins.
Generation of the Type 2 complex, in which the Mu ends have been covalently
linked to the target DNA, requires the Mu B protein, ATP, and target DNA in
addition to A and HU. The protein content of these higher order synaptic
complexes has been studied by immunoelectron microscopy using protein
A-colloidal gold conjugates to visualize antibody-bound complexes. Under
our in vitro transposition conditions, Type 1 complexes were found to
contain A and HU; in addition, Type 2 complexes contained Mu B. However,
both the HU and the Mu B protein were found to be loosely associated and
could be quantitatively removed from the nucleoprotein core of both
complexes by incubation in 0.5 M NaCl. Depletion of HU from the Type 1
complex did not affect the ability of this complex to be converted into the
strand- transferred product. Hence, the indispensable role of the HU
protein in the Mu DNA strand transfer reaction is limited to the formation
of the Type 1 transpososome.
Immunoelectron microscopic analysis of the A, B, and HU protein content of bacteriophage Mu transpososomes
Department of Biochemistry, University of Western Ontario, London, Canada.
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