Docteur Simon BRUNET

Lieu de consultation

• CHRU BRETONNEAU - TOURS

  2 Boulevard TONNELLE, 37044 Tours

  ☎ 0247474747Hospitalier🏥 Voir cet établissement

Tarifs & secteur de conventionnement

Secteur de conventionnement non disponible (médecin hospitalier ou non présent dans l'Annuaire santé CNAM des libéraux conventionnés).

Prendre rendez-vous & contact

Lien Doctolib = recherche Google site:doctolib.fr (le 1er résultat est presque toujours le profil correct s'il existe).

Top publications · les plus citées

• 1

  Genome-wide protein interaction screens reveal functional networks involving Sm-like proteins

  Yeast (Chichester, England) · 2000

  📚 159 citations🎯 RCR 2.42Top 21% NIH🔓 Open Access

  Lire l'abstract Crossref ↓

  A set of seven structurally related Sm proteins forms the core of the snRNP particles containing the spliceosomal U1, U2, U4 and U5 snRNAs. A search of the genomic sequence ofSaccharomyces cerevisiaehas identified a number of open reading frames that potentially encode structurally similar proteins termed Lsm (L¯ike Sm¯) proteins. With the aim of analysing all possible interactions between the Lsm proteins and any protein encoded in the yeast genome, we performed exhaustive and iterative genomic two-hybrid screens, starting with the Lsm proteins as baits. Indeed, extensive interactions amongst eight Lsm proteins were found that suggest the existence of a Lsm complex or complexes. These Lsm interactions apparently involve the conserved Sm domain that also mediates interactions between the Sm proteins. The screens also reveal functionally significant interactions with splicing factors, in particular with Prp4 and Prp24, compatible with genetic studies and with the reported association of Lsm proteins with spliceosomal U6 and U4/U6 particles. In addition, interactions with proteins involved in mRNA turnover, such as Mrt1, Dcp1, Dcp2 and Xrn1, point to roles for Lsm complexes in distinct RNA metabolic processes, that are confirmed in independent functional studies. These results provide compelling evidence that two-hybrid screens yield functionally meaningful information about protein–protein interactions and can suggest functions for uncharacterized proteins, especially when they are performed on a genome-wide scale.

• 2

  The tetraspanin BcPls1 is required for appressorium-mediated penetration of Botrytis cinerea into host plant leaves

  Molecular microbiology · 2004

  📚 104 citations🎯 RCR 2.45Top 21% NIH

  Lire l'abstract Crossref ↓

  SummaryAnimal tetraspanins are membrane proteins controlling cell adhesion, morphology and motility. In fungi, the tetraspanin MgPls1 controls an appressorial function required for the penetration ofMagnaporthe griseainto host plants. An orthologue ofMgPLS1,BcPLS1, was identified in the necrotrophic fungal plant pathogenBotrytis cinerea. We constructed aBcpls1::barnull mutant by targeted gene replacement.Bcpls1::baris not pathogenic on intact plant tissues of bean, tomato or rose, but it infects wounded plant tissues. Both wild type andBcpls1::bardifferentiate appressoria on plant and artificial surfaces, a process involving an arrest of polarized growth, apex swelling and its cell wall reinforcement. Although wild‐type appressoria allowed the penetration of the fungus into the host plant within 6–12 h, no successful penetration events were observed withBcpls1::bar, suggesting that its appressoria are not functional. AneGFPtranscriptional fusion showed thatBcPLS1was specifically expressed in conidia, germ tubes and appressoria during host penetration. Our results indicate thatBcPLS1is required for the penetration ofB. cinereainto intact host plants. The defect in pathogenicity ofBcpls1::baralso demonstrates that functionalB. cinereaappressoria are required for a successful penetration process. AsBcpls1::barandMgpls1Δ::hphpenetration defects are similar, fungal tetraspanins are likely to be required for an essential appressorial function widespread among fungi.

• 3

  Cyclophilin A and calcineurin functions investigated by gene inactivation, cyclosporin A inhibition and cDNA arrays approaches in the phytopathogenic fungus Botrytis cinerea

  Molecular microbiology · 2003

  📚 100 citations🎯 RCR 2.38Top 22% NIH

  Lire l'abstract Crossref ↓

  SummaryCalcineurin phosphatase and cyclophilin A are cellular components involved in fungal morphogenesis and virulence. Their roles were investigated in the phytopathogenic fungusBotrytis cinereausing gene inactivation, drug inhibition and cDNA macroarrays approaches. First, theBCP1gene coding for cyclophilin A was identified and inactivated by homologous recombination. Thebcp1Δnull mutant obtained was still able to develop infection structures but was altered in symptom development on bean and tomato leaves. Opposite to this, calcineurin inhibition using cyclosporin A (CsA) modified hyphal morphology and prevented infection structure formation. CsA drug pattern signature on macroarrays allowed the identification of 18calcineurin‐dependent (CND) genes among 2839B. cinereagenes. Among the co‐regulatedCNDgenes, three were shown to be organized as a physical cluster that could be involved in secondary metabolism. The signature ofBCP1inactivation on macroarrays allowed the identification of only three BCP1cyclophilin‐dependent (CPD) genes that were different fromCNDgenes. Finally, no CsA drug pattern signature was observed in thebcp1Δnull mutant which provided a molecular target validation of the drug.

Publications scientifiques (14) — classées par pathologie

Source PubMed · Recherche par auteur (homonymes possibles, vérifier l'affiliation).

Partager cette fiche