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Chapter 17 : Transposition of Phage Mu DNA

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Abstract:

Mu is a temperate phage which derives its name (mutator) from its ability to integrate into numerous sites in the genome and cause mutations by insertional inactivation. The knowledge of the DNA transposition process in Mu was catapulted forward through in vitro studies which provided a paradigm for the study of other moveable elements. The Mu DNA transposition reaction in vitro has a strict requirement for negative DNA supercoiling in the donor substrate under standard reaction conditions. Although DNA supercoiling is not required for the transesterification step, supercoiled substrates are superior targets, and target capture (TC) complexes can only be stabilized for observation when a superhelical target molecule is used. Mu B protein (along with the Mu enhancer) is responsible for the phenomenal efficiency of Mu as a transposable element. Nonetheless, integration host factor (IHF) is a potent stimulator of the reaction under a variety of conditions and is probably normally present in the enhancer region because of its essential role in transcriptional regulation. Although the integration of infecting Mu DNA occurs without prior DNA replication, this could occur via a cointegrate pathway followed by repair of the θ intermediate in the minority of events that give rise to stable lysogens. The structural and functional core of Mu transpososomes is a stable, functionally active Mu A tetramer.

Citation: Chaconas G, Harshey R. 2002. Transposition of Phage Mu DNA, p 384-402. In Craig N, Craigie R, Gellert M, Lambowitz A (ed), Mobile DNA II. ASM Press, Washington, DC. doi: 10.1128/9781555817954.ch17

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Group II Introns
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Figures

Image of Figure 2.
Figure 2.

Regions of Mu DNA required for the strand transfer reaction. The substructures of the three required regions are shown in the enlargements. Reprinted from the ( ) with permission of the publisher.

Citation: Chaconas G, Harshey R. 2002. Transposition of Phage Mu DNA, p 384-402. In Craig N, Craigie R, Gellert M, Lambowitz A (ed), Mobile DNA II. ASM Press, Washington, DC. doi: 10.1128/9781555817954.ch17
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Image of Figure 3.
Figure 3.

Domain structure of Mu A. On the basis of limited proteolysis, three domains (I to III) were assigned to Mu A protein, whose general functions are indicated. Amino acid numbers corresponding to the amino terminus of each major domain are shown beneath the structure. DDE refers to residues in the catalytic triad. See the text for details.

Citation: Chaconas G, Harshey R. 2002. Transposition of Phage Mu DNA, p 384-402. In Craig N, Craigie R, Gellert M, Lambowitz A (ed), Mobile DNA II. ASM Press, Washington, DC. doi: 10.1128/9781555817954.ch17
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Image of Figure 1.
Figure 1.

Replicative transposition of Mu DNA in vitro. L, R, and E represent the Mu left end, right end, and transpositional enhancer, respectively. Reprinted from ( ) with permission of the publisher.

Citation: Chaconas G, Harshey R. 2002. Transposition of Phage Mu DNA, p 384-402. In Craig N, Craigie R, Gellert M, Lambowitz A (ed), Mobile DNA II. ASM Press, Washington, DC. doi: 10.1128/9781555817954.ch17
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