Chaperone-assisted Excisive Recombination, a Solitary Role for DnaJ (Hsp40) Chaperone in Lysogeny Escape

Champ, Stéphanie; Puvirajesinghe, Tania M.; Perrody, Elsa; Menouni, Rachid; Genevaux, Pierre; Ansaldi, Mireille

doi:10.1074/jbc.m111.281865

Cited by 10 publications

(13 citation statements)

References 56 publications

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“…Direct Association of DnaJ and TorI-We have previously shown that DnaJ has the ability to increase the excision efficiency of the KplE1 prophage from the K12 bacterial chromosome (24). The presence of DnaJ increased the affinity of TorI for its specific DNA targets on attL.…”

Section: Resultsmentioning

confidence: 99%

“…Recently, we have shown that DnaJ is also involved in prophage excision of a class of (pro)phages that share very similar recombination modules (24). As this role appeared to be a bona fide chaperone activity of DnaJ, which was independent of DnaK, we have now further characterized the structural features underlying the TorI/DnaJ interaction.…”

mentioning

confidence: 90%

“…This close proximity of the DnaJ and DNA-binding sites on TorI structure may have a direct influence on the observed increased affinity of TorI for DNA (24).…”

mentioning

confidence: 99%

“…Conclusions-We have previously identified a functional role of DnaJ in assisting prophage excision (24). Initial experimental data showed that DnaJ did not bind to the attL DNA itself but somehow increased the affinity of TorI for this site.…”

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confidence: 99%

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DnaJ (Hsp40 Protein) Binding to Folded Substrate Impacts KplE1 Prophage Excision Efficiency

Puvirajesinghe

Elantak

Lignon

et al. 2012

Journal of Biological Chemistry

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Background: DnaJ positively modulates KplE1 prophage excision and is involved in lysogeny escape. Results: The recombination directionality factor TorI, from KplE1 prophage, interacts with the DnaJ chaperone, and they protect each other from limited trypsin digestion. Conclusion: DnaJ stabilizes TorI recombination directionality factor conformation. Significance: DnaJ cochaperone can bind folded substrates and induces the conformational stabilization of the TorI protein.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 90%

“…This close proximity of the DnaJ and DNA-binding sites on TorI structure may have a direct influence on the observed increased affinity of TorI for DNA (24).…”

mentioning

confidence: 99%

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confidence: 99%

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DnaJ (Hsp40 Protein) Binding to Folded Substrate Impacts KplE1 Prophage Excision Efficiency

Puvirajesinghe

Elantak

Lignon

et al. 2012

Journal of Biological Chemistry

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“…Values represent the average of at least three independent determinations. Alternatively, a PCR amplification was performed on 15 randomly chosen LCB6069 colonies treated or not treated with BCM, using specific primer pairs to test for the presence of attL and attB (44).…”

Section: Methodsmentioning

confidence: 99%

Transcription termination controls prophage maintenance in Escherichia coli genomes

Menouni

Champ

Espinosa

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Prophages represent a large fraction of prokaryotic genomes and often provide new functions to their hosts, in particular virulence and fitness. How prokaryotic cells maintain such gene providers is central for understanding bacterial genome evolution by horizontal transfer. Prophage excision occurs through site-specific recombination mediated by a prophage-encoded integrase. In addition, a recombination directionality factor (or excisionase) directs the reaction toward excision and prevents the phage genome from being reintegrated. In this work, we describe the role of the transcription termination factor Rho in prophage maintenance through control of the synthesis of transcripts that mediate recombination directionality factor expression and, thus, excisive recombination. We show that Rho inhibition by bicyclomycin allows for the expression of prophage genes that lead to excisive recombination. Thus, besides its role in the silencing of horizontally acquired genes, Rho also maintains lysogeny of defective and functional prophages.bacteriophage | transduction | transcriptional regulation

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Screening and Identification of DnaJ Interaction Proteins in Streptococcus pneumoniae

Cai

Yan

et al. 2013

Curr Microbiol

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Streptococcus pneumoniae DnaJ is recognized as a virulence factor whose role in pneumococcal virulence remains unclear. Here, we attempted to reveal the contribution of DnaJ in pneumococcal virulence from the identification of its interacting proteins using co-immunoprecipitation method. dnaJ was cloned into plasmid pAE03 generating pAE03-dnaJ-gfp which was used to transform S. pneumoniae D39 strain. Then anti-GFP coated beads were used to capture GFP-coupled proteins from the bacterial lysate. The resulting protein mixtures were subjected to SDS-PAGE and those differential bands were determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry. We finally obtained nine proteins such as DnaK, Gap, Eno, SpxB using this method. Furthermore, to confirm the interaction between DnaJ and these candidates, bacterial two-hybrid system was employed to reveal, for example, the interaction between DnaJ and DnaK, Eno, SpxB. Further protein expression experiments suggested that DnaJ prevented denaturation of Eno and SpxB at high temperature. These results help to understand the role of DnaJ in the pathogenesis of S. pneumoniae.

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Chaperone-assisted Excisive Recombination, a Solitary Role for DnaJ (Hsp40) Chaperone in Lysogeny Escape

Cited by 10 publications

References 56 publications

DnaJ (Hsp40 Protein) Binding to Folded Substrate Impacts KplE1 Prophage Excision Efficiency

DnaJ (Hsp40 Protein) Binding to Folded Substrate Impacts KplE1 Prophage Excision Efficiency

Transcription termination controls prophage maintenance in Escherichia coli genomes

Screening and Identification of DnaJ Interaction Proteins in Streptococcus pneumoniae

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