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Accueil > Départements > Biochimie, Biophysique et Biologie Structurale > Françoise OCHSENBEIN & Raphaël GUEROIS : Assemblage moléculaire et intégrité du génome

pubmed : ochsenbein, francois...

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NCBI : db=pubmed ; Term=Ochsenbein, Francoise[Full Author Name] or Guerois, Raphael[Full Author Name] or Andreani, Jessica[Full Author Name] or Plançon, Laure[Full Author Name]

Articles syndiqués

  • InterEvDock2 : an expanded server for protein docking using evolutionary and biological information from homology models and multimeric inputs.

    10 mai, par Quignot C, Rey J, Yu J, Tufféry P, Guerois R, Andreani J
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    InterEvDock2: an expanded server for protein docking using evolutionary and biological information from homology models and multimeric inputs.

    Nucleic Acids Res. 2018 May 08;:

    Authors: Quignot C, Rey J, Yu J, Tufféry P, Guerois R, Andreani J

    Abstract
    Computational protein docking is a powerful strategy to predict structures of protein-protein interactions and provides crucial insights for the functional characterization of macromolecular cross-talks. We previously developed InterEvDock, a server for ab initio protein docking based on rigid-body sampling followed by consensus scoring using physics-based and statistical potentials, including the InterEvScore function specifically developed to incorporate co-evolutionary information in docking. InterEvDock2 is a major evolution of InterEvDock which allows users to submit input sequences - not only structures - and multimeric inputs and to specify constraints for the pairwise docking process based on previous knowledge about the interaction. For this purpose, we added modules in InterEvDock2 for automatic template search and comparative modeling of the input proteins. The InterEvDock2 pipeline was benchmarked on 812 complexes for which unbound homology models of the two partners and co-evolutionary information are available in the PPI4DOCK database. InterEvDock2 identified a correct model among the top 10 consensus in 29% of these cases (compared to 15-24% for individual scoring functions) and at least one correct interface residue among 10 predicted in 91% of these cases. InterEvDock2 is thus a unique protein docking server, designed to be useful for the experimental biology community. The InterEvDock2 web interface is available at http://bioserv.rpbs.univ-paris-diderot.fr/services/InterEvDock2/.

    PMID: 29741647 [PubMed - as supplied by publisher]

  • Sak4 of Phage HK620 Is a RecA Remote Homolog With Single-Strand Annealing Activity Stimulated by Its Cognate SSB Protein.

    10 mai, par Hutinet G, Besle A, Son O, McGovern S, Guerois R, Petit MA, Ochsenbein F, Lecointe F
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    Sak4 of Phage HK620 Is a RecA Remote Homolog With Single-Strand Annealing Activity Stimulated by Its Cognate SSB Protein.

    Front Microbiol. 2018;9:743

    Authors: Hutinet G, Besle A, Son O, McGovern S, Guerois R, Petit MA, Ochsenbein F, Lecointe F

    Abstract
    Bacteriophages are remarkable for the wide diversity of proteins they encode to perform DNA replication and homologous recombination. Looking back at these ancestral forms of life may help understanding how similar proteins work in more sophisticated organisms. For instance, the Sak4 family is composed of proteins similar to the archaeal RadB protein, a Rad51 paralog. We have previously shown that Sak4 allowed single-strand annealing in vivo, but only weakly compared to the phage λ Redβ protein, highlighting putatively that Sak4 requires partners to be efficient. Here, we report that the purified Sak4 of phage HK620 infecting Escherichia coli is a poorly efficient annealase on its own. A distant homolog of SSB, which gene is usually next to the sak4 gene in various species of phages, highly stimulates its recombineering activity in vivo. In vitro, Sak4 binds single-stranded DNA and performs single-strand annealing in an ATP-dependent way. Remarkably, the single-strand annealing activity of Sak4 is stimulated by its cognate SSB. The last six C-terminal amino acids of this SSB are essential for the binding of Sak4 to SSB-covered single-stranded DNA, as well as for the stimulation of its annealase activity. Finally, expression of sak4 and ssb from HK620 can promote low-level of recombination in vivo, though Sak4 and its SSB are unable to promote strand exchange in vitro. Regarding its homology with RecA, Sak4 could represent a link between two previously distinct types of recombinases, i.e., annealases that help strand exchange proteins and strand exchange proteins themselves.

    PMID: 29740405 [PubMed]

  • Correction : Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain.

    8 mai, par Nguyen TQ, Chenon M, Vilela F, Velours C, Aumont-Nicaise M, Andreani J, Varela PF, Llinas P, Ménétrey J
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    Correction: Structural plasticity of the N-terminal capping helix of the TPR domain of kinesin light chain.

    PLoS One. 2018;13(5):e0197193

    Authors: Nguyen TQ, Chenon M, Vilela F, Velours C, Aumont-Nicaise M, Andreani J, Varela PF, Llinas P, Ménétrey J

    Abstract
    [This corrects the article DOI: 10.1371/journal.pone.0186354.].

    PMID: 29734375 [PubMed - in process]

  • Disentangling the molecular determinants for Cenp-F localization to nuclear pores and kinetochores.

    11 avril, par Berto A, Yu J, Morchoisne-Bolhy S, Bertipaglia C, Vallee R, Dumont J, Ochsenbein F, Guerois R, Doye V
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    Disentangling the molecular determinants for Cenp-F localization to nuclear pores and kinetochores.

    EMBO Rep. 2018 Apr 09;:

    Authors: Berto A, Yu J, Morchoisne-Bolhy S, Bertipaglia C, Vallee R, Dumont J, Ochsenbein F, Guerois R, Doye V

    Abstract
    Cenp-F is a multifaceted protein implicated in cancer and developmental pathologies. The Cenp-F C-terminal region contains overlapping binding sites for numerous proteins that contribute to its functions throughout the cell cycle. Here, we focus on the nuclear pore protein Nup133 that interacts with Cenp-F both at nuclear pores in prophase and at kinetochores in mitosis, and on the kinase Bub1, known to contribute to Cenp-F targeting to kinetochores. By combining in silico structural modeling and yeast two-hybrid assays, we generate an interaction model between a conserved helix within the Nup133 β-propeller and a short leucine zipper-containing dimeric segment of Cenp-F. We thereby create mutants affecting the Nup133/Cenp-F interface and show that they prevent Cenp-F localization to the nuclear envelope, but not to kinetochores. Conversely, a point mutation within an adjacent leucine zipper affecting the kinetochore targeting of Cenp-F KT-core domain impairs its interaction with Bub1, but not with Nup133, identifying Bub1 as the direct KT-core binding partner of Cenp-F. Finally, we show that Cenp-E redundantly contributes together with Bub1 to the recruitment of Cenp-F to kinetochores.

    PMID: 29632243 [PubMed - as supplied by publisher]

  • FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination.

    3 avril, par Fernandes JB, Duhamel M, Seguéla-Arnaud M, Froger N, Girard C, Choinard S, Solier V, De Winne N, De Jaeger G, Gevaert K, Andrey P, Grelon M, Guerois R, Kumar R, Mercier R
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    FIGL1 and its novel partner FLIP form a conserved complex that regulates homologous recombination.

    PLoS Genet. 2018 Apr 02;14(4):e1007317

    Authors: Fernandes JB, Duhamel M, Seguéla-Arnaud M, Froger N, Girard C, Choinard S, Solier V, De Winne N, De Jaeger G, Gevaert K, Andrey P, Grelon M, Guerois R, Kumar R, Mercier R

    Abstract
    Homologous recombination is central to repair DNA double-strand breaks, either accidently arising in mitotic cells or in a programed manner at meiosis. Crossovers resulting from the repair of meiotic breaks are essential for proper chromosome segregation and increase genetic diversity of the progeny. However, mechanisms regulating crossover formation remain elusive. Here, we identified through genetic and protein-protein interaction screens FIDGETIN-LIKE-1 INTERACTING PROTEIN (FLIP) as a new partner of the previously characterized anti-crossover factor FIDGETIN-LIKE-1 (FIGL1) in Arabidopsis thaliana. We showed that FLIP limits meiotic crossover together with FIGL1. Further, FLIP and FIGL1 form a protein complex conserved from Arabidopsis to human. FIGL1 interacts with the recombinases RAD51 and DMC1, the enzymes that catalyze the DNA strand exchange step of homologous recombination. Arabidopsis flip mutants recapitulate the figl1 phenotype, with enhanced meiotic recombination associated with change in counts of DMC1 and RAD51 foci. Our data thus suggests that FLIP and FIGL1 form a conserved complex that regulates the crucial step of strand invasion in homologous recombination.

    PMID: 29608566 [PubMed - as supplied by publisher]

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