Transpososomes: Stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA

Surette, Michael G.; Buch, Shilpa; Chaconas, George

doi:10.1016/0092-8674(87)90566-6

Cited by 213 publications

(208 citation statements)

References 22 publications

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“…For example, in l site-specific recombination, the reaction direction is controlled by involving two overlapping sets of proteins under different physiological conditions, preferentially stabilizing one product set over another (Landy 1989). Another example is the strand transfer step of transposition reactions which should reach equilibrium at near 50%, at best, without the product stabilization that apparently pushes the reaction toward completion (Surette et al 1987;Haniford et al 1991).…”

Section: Energetic Considerations and Recombination Complexesmentioning

confidence: 99%

Polynucleotidyl transfer reactions in site‐specific DNA recombination

1997

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Site-specific DNA rearrangement reactions are widespread among organisms. They are used, for example, by vertebrates to boost immune response diversity, and in turn by parasitic organisms to evade the host immune system by surface antigen switching. Parasitic genetic elements ubiquitous to most organisms invade new host genomic sites by a variety of types of site-specific recombination. Polynucleotidyl transfer reactions are central to these DNA recombination reactions. The recombinase of each reaction system that 'catalyses' such chemical reactions at specific DNA sites are apparently designed to accomplish unique DNA geometrical specificity, or delicate control over the extent or direction of the reaction, with the sacrifice of protein turnover. Here we discuss our current understanding of several issues that relate to the polynucleotidyl transfer steps in several of the better studied site-specific recombination reactions.

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Section: Energetic Considerations and Recombination Complexesmentioning

confidence: 99%

Polynucleotidyl transfer reactions in site‐specific DNA recombination

1997

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“…However, paired structures where the left and right end were held together in a DNA-protein complex were not observed. Such paired structures are only found when, in addition to the A protein, the E.coli HU protein is also present (8). The complexes found at the right end were of the same size as those found at the left end.…”

Section: Dnasei Footprinting Experimentsmentioning

confidence: 55%

“…The precise function of the B protein is not yet known, however, biochemical studies indicate that it might be involved in bringing in the acceptor DNA molecule into the synaptic complex (8,20). In the absence of the B protein transposition is predominantly intra-molecular (20) and the B protein is essential for the conversion of the type I synaptic complex to the type II complex (8).…”

Section: Discussionmentioning

confidence: 99%

“…In the absence of the B protein transposition is predominantly intra-molecular (20) and the B protein is essential for the conversion of the type I synaptic complex to the type II complex (8). In the type I complex both ends of the phage are hold together by the A protein.…”

Section: Discussionmentioning

confidence: 99%

“…In the type I complex both ends of the phage are hold together by the A protein. In the type II complex the acceptor DNA molecule is also included and the strand transfer reactions have occurred (8).…”

Section: Discussionmentioning

confidence: 99%

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Interactions of the transposase with the ends of Mu: formation of specific nucleoprotein structures and non-cooperative binding of the transposase to its binding sites

et al. 1987

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Transposition of the E.coli bacteriophage Mu requires the phage encoded A and B proteins, the host protein HU and the host replication proteins. The ends of the genome of the phage, on which some of these proteins act, both contain three transposase (A) binding sites. The organization of these binding sites on each end, however, is different. Here we show, using DNase footprinting experiments with purified A protein, that mutant A binding sites, which affect transposition, have decreased affinity for the transposase. Furthermore the transposase binds non-cooperatively to all A binding sites both in the left and right end of Mu. Electron microscopic studies show that the A protein forms specific nucleoprotein structures upon binding to the ends of Mu. The A and B proteins interact with the ends of Mu to generate larger structures than with the A protein alone.

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Mechanism of Mu DNA transposition

Chaconas¹,

Surette²

1988

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SummaryThe study of Mu DNA transposition in vitro has resulted in a much better understanding of the biochemical details of the transposition process. An early step in transposition is the generation of a B structure which is the product of the strand-transfer reaction. The polarity of the strand transfer has been determined and substantial progress has been made on the role of the individual proteins. Moreover, the strand-transfer reaction is mediated by stable protein-DNA complexes, or transpososomes, and the reaction can be divided into two sequential steps. The role of the transpososomes and the requirement for a supercoiled Mu DNA substrate are also discussed.

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Transpososomes: Stable protein-DNA complexes involved in the in vitro transposition of bacteriophage Mu DNA

Cited by 213 publications

References 22 publications

Polynucleotidyl transfer reactions in site‐specific DNA recombination

Polynucleotidyl transfer reactions in site‐specific DNA recombination

Interactions of the transposase with the ends of Mu: formation of specific nucleoprotein structures and non-cooperative binding of the transposase to its binding sites

Mechanism of Mu DNA transposition

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