Substrate recognition and induced DNA deformation by transposase at the target-capture stage of Tn10 transposition

Pribil, Patrick; Haniford, David B.

doi:10.1006/jmbi.2000.4135

Cited by 30 publications

(25 citation statements)

References 46 publications

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“…This can be an additive process, as suggested for IHF binding by Rice et al (61) and for Tn10 transposase target recognition by Pribil and Haniford (29). Transpososome binding to the consensus base pairs may facilitate a kink formation, which in turn would permit additional contacts with flanking DNA.…”

Section: Discussionmentioning

confidence: 89%

“…Taken together, these results suggest that the Mu transpososome probably makes contacts with (or is influenced by) a target covering a region up to 23-25 bp. A broad zone of contacts (ϳ24-bp) has been detected with contact-probing experiments between the transpososome and target DNA in the target-capture complex of Tn10 (29). For IS903 a preferred target has been found to consist of a 21-bp palindromic sequence pattern, with preferred 5-bp sequences in the flanks around a 9-bp target duplication area (60).…”

Section: Discussionmentioning

confidence: 99%

“…Similarly, DNA bent around nucleosomes and cruciform DNA are favored as retroviral integration target sites in vitro (27,28). The DNA sequence-related structure has been proposed for Tn10 target site flanking sequences (21,29) and P element insertion sites (30).…”

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confidence: 99%

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DNA Transposition of Bacteriophage Mu

Haapa-Paananen¹,

Rita²,

Savilahti³

2002

Journal of Biological Chemistry

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The Mu transpositional DNA recombination machinery selects target sites by assembling a protein-DNA complex that interacts with the target DNA and reacts whenever it locates a favorable sequence composition. Splicing of a transposon into the target generates a 5-bp duplication that reflects the original target site. Preferential usage of different target pentamers was examined with a minimal Mu in vitro system and quantitatively compiled consensus sequences for the most preferred and the least preferred sites were generated. When analyzed as base steps, preferences toward certain steps along the 5-bp target site were detected. We further show that insertion sites can be predicted on the basis of additively calculated base step values. Also surrounding sequences influence the preference of a given pentamer; a symmetrical structural component was revealed, suggesting potential hinges at and around the target site.

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

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DNA Transposition of Bacteriophage Mu

Haapa-Paananen¹,

Rita²,

Savilahti³

2002

Journal of Biological Chemistry

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“…OE substrate with 15 bp of flanking donor DNA was generated by annealing oligonucleotides 78-NTS and 80-TS, as described by Allingham et al (2001). Target DNA containing the HisG1 hotspot for Tn10 insertion (Halling and Kleckner 1982) was generated by annealing oligonucleotides HisG1-40mer-T and HisG1-40mer-B, as described by Pribil and Haniford (2000).The mini-Tn10 element used for the in vivo analysis was present on pDH50 (Haniford and Kleckner 1994).…”

Section: Proteins and Oe Substratesmentioning

confidence: 99%

The global regulator H-NS acts directly on the transpososome to promote Tn10 transposition

Wardle¹,

O'Carroll²,

Derbyshire³

et al. 2005

Genes Dev.

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The histone-like nucleoid structuring (H-NS) protein is a global transcriptional regulator that is known to regulate stress response pathways and virulence genes in bacteria. It has also been implicated in the regulation of bacterial transposition systems, including Tn10. We demonstrate here that H-NS promotes Tn10 transposition by binding directly to the transposition complex (or transpososome). We present evidence that, upon binding, H-NS induces the unfolding of the Tn10 transpososome and helps to maintain the transpososome in an unfolded state. This ensures that intermolecular (as opposed to self-destructive intramolecular) transposition events are favored. We present evidence that H-NS binding to the flanking donor DNA of the transpososome is the initiating event in the unfolding process. We propose that by recruiting H-NS as a modulator of transposition, Tn10 has evolved a means of sensing changes in host physiology, as the amount of H-NS in the cell, as well its activity, are responsive to changes in environmental conditions. Sensing of environmental changes through H-NS would allow transposition to occur when it is most opportune for both the transposon and the host.

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“…In the alternate pathway, another accessory protein, TnsE, targets transposition events to altered DNA structures associated with replication (27). Tn10, another transposase that shares many functional similarities with the RAG proteins, also induces DNA distortion near the integration site (28).…”

mentioning

confidence: 99%

Targeted Transposition by the V(D)J Recombinase

Lee¹,

Neiditch²,

Sinden

et al. 2002

Molecular and Cellular Biology

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Cleavage by the V(D)J recombinase at a pair of recombination signal sequences creates two coding ends and two signal ends. The RAG proteins can integrate these signal ends, without sequence specificity, into an unrelated target DNA molecule. Here we demonstrate that such transposition events are greatly stimulated by-and specifically targeted to-hairpins and other distorted DNA structures. The mechanism of target selection by the RAG proteins thus appears to involve recognition of distorted DNA. These data also suggest a novel mechanism for the formation of alternative recombination products termed hybrid joints, in which a signal end is joined to a hairpin coding end. We suggest that hybrid joints may arise by transposition in vivo and propose a new model to account for some recurrent chromosome translocations found in human lymphomas. According to this model, transposition can join antigen receptor loci to partner sites that lack recombination signal sequence elements but bear particular structural features. The RAG proteins are capable of mediating all necessary breakage and joining events on both partner chromosomes; thus, the V(D)J recombinase may be far more culpable for oncogenic translocations than has been suspected.The immune system's vast repertoire of B-and T-cell receptors results from a site-specific gene rearrangement process known as V(D)J recombination. Assorted variable (V), diversity (D), and joining (J) coding gene segments are recombined in developing lymphocyte precursors to form the variable region genes that encode antigen-binding sites of immunoglobulin and T-cell receptor molecules (40). The DNA is first cleaved at specific recombination signal sequences (RSS) located adjacent to the coding segments. RSS consist of conserved heptamer and nonamer sequences, separated by either 12 or 23 nucleotides of spacer DNA (referred to as 12 RSS and 23 RSS). The RAG1 and RAG2 recombinase proteins, assisted by either of the nonspecific DNA-bending proteins HMG1 and HMG2 (41), generate a nick between the RSS and the adjacent coding segment by hydrolysis. The newly formed 3Ј OH group then attacks the phosphodiester bond connecting the coding segment to the RSS on the opposite strand.

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Substrate recognition and induced DNA deformation by transposase at the target-capture stage of Tn10 transposition

Cited by 30 publications

References 46 publications

DNA Transposition of Bacteriophage Mu

DNA Transposition of Bacteriophage Mu

The global regulator H-NS acts directly on the transpososome to promote Tn10 transposition

Targeted Transposition by the V(D)J Recombinase

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