Transposons: Prokaryotic

Transposons are movable genetic elements found ubiquitously in the genomes of living organisms. They generate a variety of DNA rearrangements that have profound consequences for cell survival and evolution.

Keywords: transposons; Mu; Tn10; Tn7; Tn5

Figure 1. Two transposition pathways. (a) Replicative ‘cointegrate’ pathway. 3¢-OH groups are denoted by arrowheads, and 5¢ phosphate groups by filled circles. The two target DNA phosphodiesters that will be attacked by transposon ends during strand transfer are shown already cleaved, for clarity. The short lines connecting the two DNA chains in the target represent the characteristic sequence duplicated after transposition. Wavy arrows denote alternative processing of the branched intermediate. Recombination between duplicated TEs in the cointegrate is signified by a cross. (b) Conservative ‘cut-and-paste’ pathway. All symbols as in (a).
Figure 2. Adjacent deletions and inversions produced as a consequence of intramolecular ‘cointegrate’ events. (a) Deletions; a–d represent genetic markers in the donor replicon. Following cleavage and strand transfer, replication of the branched intermediate produces two replicons, one deleted for markers c–d and the other for markers a–b flanking the original transposon. (b) Inversions; as in (a), except that opposite DNA strands are used as target in the strand transfer step. Replication of the branched intermediate produces inversion of markers a–b with respect to c–d. Symbols as in Figure 1.
Figure 3. Essential DNA and protein components of Mu transposition. (a) AttL, attR and enhancer regions encompass multiple DNA sites essential for transposition. Cleavage and strand transfer occurs at specific nucleotides (diamonds) outside L1 and R1, at the junction of Mu and non-Mu DNA. (b) Domain structure of transposase MuA. Of the three major proteolytic fragments or domains, I binds to sites in the enhancer and I to sites in attL and attR. Domain II has the catalytic DDE residues. Domain III is essential for assembly of the transpososome, as well as for interaction with the allosteric regulator MuB. Amino acid numbers are indicated below the protein structure.
Figure 4. Nucleoprotein complexes in the Mu transposition pathway. AttL, attR and the enhancer sequences are designated L, R and E, respectively.
Figure 5. Remodelling transposition complexes for Mu replication. The stable strand transfer complex (type II-1; see Figure 4) is first destabilized by ClpX (type II-2), allowing displacement and exchange of MuA with a host factor MRF2 (type II-3), prior to entry of PolIII holoenzyme for Mu replication.
Figure 6. Formation of a hairpin intermediate during the cut-and-paste pathway of Tn10 transposition. Symbols as in Figure 1.
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 References
    Blattner FR, Plunkett G 3rd, Bloch CA et al. (1997) The complete genome sequence of Escherichia coli K-12. Science 277: 1453–1474.
    Bolland S and Kleckner N (1996) The three chemical steps of Tn10/IS10 transposition involve repeated utilization of a single active site. Cell 84: 223–233.
    Davies DR, Braam LM, Reznikoff WS and Rayment I (1999) The three-dimensional structure of a Tn5 transposase-related protein determined to 2.9-Å resolution. Journal of Biological Chemistry 274: 11903–11913.
    Derbyshire KM and Grindley ND (1996) Cis preference of the IS903 transposase is mediated by a combination of transposase instability and inefficient translation. Molecular Microbiology 21: 1261–1272.
    Goryshin IY and Reznikoff WS (1998) Tn5 in vitro transposition. Journal of Biological Chemistry 273: 7367–7374.
    Jones JM and Nakai H (1997) The X174-type primosome promotes replisome assembly at the site of recombination in bacteriophage Mu transposition. The EMBO Journal 16: 6886–6895.
    Kennedy AK, Guhathakurta A, Kleckner N and Haniford DB (1998) Tn10 transposition via a DNA hairpin intermediate. Cell 95: 125–134.
    Naigamwalla DZ and Chaconas G (1997) A new set of Mu DNA transposition intermediates: alternate pathways of target capture preceding strand transfer. The EMBO Journal 16: 5227–5234.
    Namgoong S-Y and Harshey RM (1998) The same two monomers within a MuA tetramer provide the DDE domains for the strand cleavage and strand transfer steps of transposition. The EMBO Journal 17: 3775–3785.
    Sharpe PL and Craig NL (1998) Host proteins can stimulate Tn7 transposition: a novel role for the ribosomal protein L29 and the acyl carrier protein. The EMBO Journal 17: 5822–5831.
    Stellwagen AE and Craig NL (1997) Avoiding self: two Tn7-encoded proteins mediate target immunity in Tn7 transposition. The EMBO Journal 16: 6823–6834.
    Sapienza C and Doolittle WF (1980) Genes are things you have, whether you want them or not. Cold Spring Harbor Symposium for Quantitative Biology 45: 177–182.
 Further Reading
    book Berg DE and Howe MM (1989) Mobile DNA. Washington, DC: American Society for Microbiology.
    Chaconas G, Lavoie BD and Watson MA (1996) DNA transposition: jumping gene machine, some assembly required. Current Biology 7: 817–820.
    Craig NL (1997) Target site selection in transposition. Annual Review of Biochemistry 66: 437–474.
    Grindley NDF and Leschziner AE (1995) DNA transposition: from black box to color monitor. Cell 83: 1063–1066.
    Kleckner N (1990) Regulation of transposition in bacteria. Annual Review of Cell Biology 6: 297–327.
    Mahillon J and Chandler M (1998) Insertion sequences. Microbiology and Molecular Biology Reviews 62: 725–774.
    Mizuuchi K (1992) Transpositional recombination: Mechanistic insights from studies of Mu and other elements. Annual Review of Biochemistry 61: 1011–1051.
    Reznikoff WS (1993) The Tn5 transposon. Annual Review of Microbiology 47: 945–963.
    Roth DB and Craig NL (1998) VDJ recombination: A transposase goes to work. Cell 94: 411–414.
    book Symonds N, Toussaint A, Van de Putte P and Howe MM (1987) Phage Mu. New York: Cold Spring Harbor Laboratory.
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Harshey, Rasika M(Apr 2001) Transposons: Prokaryotic. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0000591]