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  1. Article ; Online: Transcription-driven DNA supercoiling counteracts H-NS-mediated gene silencing in bacterial chromatin.

    Figueroa-Bossi, Nara / Fernández-Fernández, Rocío / Kerboriou, Patricia / Bouloc, Philippe / Casadesús, Josep / Sánchez-Romero, María Antonia / Bossi, Lionello

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 2787

    Abstract: In all living cells, genomic DNA is compacted through interactions with dedicated proteins and/or the formation of plectonemic coils. In bacteria, DNA compaction is achieved dynamically, coordinated with dense and constantly changing transcriptional ... ...

    Abstract In all living cells, genomic DNA is compacted through interactions with dedicated proteins and/or the formation of plectonemic coils. In bacteria, DNA compaction is achieved dynamically, coordinated with dense and constantly changing transcriptional activity. H-NS, a major bacterial nucleoid structuring protein, is of special interest due to its interplay with RNA polymerase. H-NS:DNA nucleoprotein filaments inhibit transcription initiation by RNA polymerase. However, the discovery that genes silenced by H-NS can be activated by transcription originating from neighboring regions has suggested that elongating RNA polymerases can disassemble H-NS:DNA filaments. In this study, we present evidence that transcription-induced counter-silencing does not require transcription to reach the silenced gene; rather, it exerts its effect at a distance. Counter-silencing is suppressed by introducing a DNA gyrase binding site within the intervening segment, suggesting that the long-range effect results from transcription-driven positive DNA supercoils diffusing toward the silenced gene. We propose a model wherein H-NS:DNA complexes form in vivo on negatively supercoiled DNA, with H-NS bridging the two arms of the plectoneme. Rotational diffusion of positive supercoils generated by neighboring transcription will cause the H-NS-bound negatively-supercoiled plectoneme to "unroll" disrupting the H-NS bridges and releasing H-NS.
    MeSH term(s) Chromatin/metabolism ; DNA-Binding Proteins/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Bacteria/genetics ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; DNA/metabolism ; Gene Silencing ; Gene Expression Regulation, Bacterial ; DNA, Bacterial/genetics ; DNA, Bacterial/metabolism ; Transcription, Genetic
    Chemical Substances Chromatin ; DNA-Binding Proteins ; Bacterial Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; DNA (9007-49-2) ; DNA, Bacterial
    Language English
    Publishing date 2024-03-30
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-47114-w
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Book: Bioterrorisme

    Bricaire, François / Bossi, Philippe

    (Collection médecine des risques)

    2003  

    Author's details François Bricaire ; Philippe Bossi
    Series title Collection médecine des risques
    Keywords Bioterrorism ; Disaster Planning ; France
    Language French
    Size 115 S. : Ill.
    Publisher Elsevier
    Publishing place Paris
    Publishing country France
    Document type Book
    HBZ-ID HT014129931
    ISBN 2-84299-387-X ; 978-2-84299-387-0
    Database Catalogue ZB MED Medicine, Health

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  3. Article ; Online: Regulatory interplay between small RNAs and transcription termination factor Rho.

    Bossi, Lionello / Figueroa-Bossi, Nara / Bouloc, Philippe / Boudvillain, Marc

    Biochimica et biophysica acta. Gene regulatory mechanisms

    2020  Volume 1863, Issue 7, Page(s) 194546

    Abstract: The largest and best studied group of regulatory small RNAs (sRNAs) in bacteria act by modulating translation or turnover of messenger RNAs (mRNAs) through base-pairing interactions that typically take place near the 5' end of the mRNA. This allows the ... ...

    Abstract The largest and best studied group of regulatory small RNAs (sRNAs) in bacteria act by modulating translation or turnover of messenger RNAs (mRNAs) through base-pairing interactions that typically take place near the 5' end of the mRNA. This allows the sRNA to bind the complementary target sequence while the remainder of the mRNA is still being made, creating conditions whereby the action of the sRNA can extend to transcriptional steps, most notably transcription termination. Increasing evidence corroborates the existence of a functional interplay between sRNAs and termination factor Rho. Two general mechanisms have emerged. One mechanism operates in translated regions subjected to sRNA repression. By inhibiting ribosome binding co-transcriptionally, the sRNA uncouples translation from transcription, allowing Rho to bind the nascent RNA and promote termination. In the second mechanism, which functions in 5' untranslated regions, the sRNA antagonizes termination directly by interfering with Rho binding to the RNA or the subsequent translocation along the RNA. Here, we review the above literature in the context of other mechanisms that underlie the participation of Rho-dependent transcription termination in gene regulation. This article is part of a Special Issue entitled: RNA and gene control in bacteria edited by Dr. M. Guillier and F. Repoila.
    MeSH term(s) Bacteria/genetics ; Gene Expression Regulation, Bacterial ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Small Untranslated/genetics ; RNA, Small Untranslated/metabolism ; Rho Factor/genetics ; Rho Factor/metabolism ; Transcription Termination, Genetic
    Chemical Substances RNA, Messenger ; RNA, Small Untranslated ; Rho Factor
    Language English
    Publishing date 2020-03-23
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2918786-2
    ISSN 1876-4320 ; 1874-9399
    ISSN (online) 1876-4320
    ISSN 1874-9399
    DOI 10.1016/j.bbagrm.2020.194546
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Pervasive transcription enhances the accessibility of H-NS-silenced promoters and generates bistability in

    Figueroa-Bossi, Nara / Sánchez-Romero, María Antonia / Kerboriou, Patricia / Naquin, Delphine / Mendes, Clara / Bouloc, Philippe / Casadesús, Josep / Bossi, Lionello

    Proceedings of the National Academy of Sciences of the United States of America

    2022  Volume 119, Issue 30, Page(s) e2203011119

    Abstract: ... ...

    Abstract In
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Bacterial ; Gene Silencing ; Promoter Regions, Genetic ; Salmonella/genetics ; Salmonella/pathogenicity ; Single-Cell Analysis ; Transcription, Genetic ; Virulence/genetics
    Chemical Substances Bacterial Proteins ; DNA-Binding Proteins ; H-NS protein, bacteria ; Spi1 protein, Salmonella
    Language English
    Publishing date 2022-07-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2203011119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: 6S RNA-Dependent Susceptibility to RNA Polymerase Inhibitors.

    Esberard, Marick / Hallier, Marc / Liu, Wenfeng / Morvan, Claire / Bossi, Lionello / Figueroa-Bossi, Nara / Felden, Brice / Bouloc, Philippe

    Antimicrobial agents and chemotherapy

    2022  Volume 66, Issue 5, Page(s) e0243521

    Abstract: Bacterial small RNAs (sRNAs) contribute to a variety of regulatory mechanisms that modulate a wide range of pathways, including metabolism, virulence, and antibiotic resistance. We investigated the involvement of sRNAs in rifampicin resistance in the ... ...

    Abstract Bacterial small RNAs (sRNAs) contribute to a variety of regulatory mechanisms that modulate a wide range of pathways, including metabolism, virulence, and antibiotic resistance. We investigated the involvement of sRNAs in rifampicin resistance in the opportunistic pathogen Staphylococcus aureus. Using a competition assay with an sRNA mutant library, we identified 6S RNA as being required for protection against low concentrations of rifampicin, an RNA polymerase (RNAP) inhibitor. This effect applied to rifabutin and fidaxomicin, two other RNAP-targeting antibiotics. 6S RNA is highly conserved in bacteria, and its absence in two other major pathogens, Salmonella enterica and Clostridioides difficile, also impaired susceptibility to RNAP inhibitors. In S. aureus, 6S RNA is produced from an autonomous gene and accumulates in stationary phase. In contrast to what was reported for Escherichia coli, S. aureus 6S RNA does not appear to play a critical role in the transition from exponential to stationary phase but affects σ
    MeSH term(s) DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression Regulation, Bacterial ; RNA, Bacterial/genetics ; RNA, Untranslated ; Rifampin/pharmacology ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Staphylococcus aureus/genetics ; Staphylococcus aureus/metabolism ; Transcription, Genetic
    Chemical Substances 6S RNA ; RNA, Bacterial ; RNA, Untranslated ; Sigma Factor ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Rifampin (VJT6J7R4TR)
    Language English
    Publishing date 2022-04-07
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 217602-6
    ISSN 1098-6596 ; 0066-4804
    ISSN (online) 1098-6596
    ISSN 0066-4804
    DOI 10.1128/aac.02435-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Tracking the Elusive Function of Bacillus subtilis Hfq.

    Rochat, Tatiana / Delumeau, Olivier / Figueroa-Bossi, Nara / Noirot, Philippe / Bossi, Lionello / Dervyn, Etienne / Bouloc, Philippe

    PloS one

    2015  Volume 10, Issue 4, Page(s) e0124977

    Abstract: RNA-binding protein Hfq is a key component of the adaptive responses of many proteobacterial species including Escherichia coli, Salmonella enterica and Vibrio cholera. In these organisms, the importance of Hfq largely stems from its participation to ... ...

    Abstract RNA-binding protein Hfq is a key component of the adaptive responses of many proteobacterial species including Escherichia coli, Salmonella enterica and Vibrio cholera. In these organisms, the importance of Hfq largely stems from its participation to regulatory mechanisms involving small non-coding RNAs. In contrast, the function of Hfq in Gram-positive bacteria has remained elusive and somewhat controversial. In the present study, we have further addressed this point by comparing growth phenotypes and transcription profiles between wild-type and an hfq deletion mutant of the model Gram-positive bacterium, Bacillus subtilis. The absence of Hfq had no significant consequences on growth rates under nearly two thousand metabolic conditions and chemical treatments. The only phenotypic difference was a survival defect of B. subtilis hfq mutant in rich medium in stationary phase. Transcriptomic analysis correlated this phenotype with a change in the levels of nearly one hundred transcripts. Albeit a significant fraction of these RNAs (36%) encoded sporulation-related functions, analyses in a strain unable to sporulate ruled out sporulation per se as the basis of the hfq mutant's stationary phase fitness defect. When expressed in Salmonella, B. subtilis hfq complemented the sharp loss of viability of a degP hfq double mutant, attenuating the chronic σE-activated phenotype of this strain. However, B. subtilis hfq did not complement other regulatory deficiencies resulting from loss of Hfq-dependent small RNA activity in Salmonella indicating a limited functional overlap between Salmonella and B. subtilis Hfqs. Overall, this study confirmed that, despite structural similarities with other Hfq proteins, B. subtilis Hfq does not play a central role in post-transcriptional regulation but might have a more specialized function connected with stationary phase physiology. This would account for the high degree of conservation of Hfq proteins in all 17 B. subtilis strains whose genomes have been sequenced.
    MeSH term(s) Bacillus subtilis/genetics ; Bacillus subtilis/metabolism ; Host Factor 1 Protein/genetics ; Host Factor 1 Protein/metabolism ; Phenotype ; Transcriptome
    Chemical Substances Host Factor 1 Protein
    Language English
    Publishing date 2015-04-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0124977
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: Rhabdomyolysis after ezetimibe/simvastatin therapy in an HIV-infected patient.

    Chanson, Noemie / Bossi, Philippe / Schneider, Luminita / Bourry, Edward / Izzedine, Hassane

    NDT plus

    2012  Volume 1, Issue 3, Page(s) 157–161

    Language English
    Publishing date 2012-12-31
    Publishing country England
    Document type Case Reports
    ZDB-ID 2410383-4
    ISSN 1753-0784
    ISSN 1753-0784
    DOI 10.1093/ndtplus/sfn012
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Introduction into the Marseille geographical area of a mild SARS-CoV-2 variant originating from sub-Saharan Africa: An investigational study.

    Colson, Philippe / Levasseur, Anthony / Gautret, Philippe / Fenollar, Florence / Thuan Hoang, Van / Delerce, Jeremy / Bitam, Idir / Saile, Rachid / Maaloum, Mossaab / Padane, Abdou / Bedotto, Marielle / Brechard, Ludivine / Bossi, Vincent / Ben Khedher, Mariem / Chaudet, Hervé / Million, Matthieu / Tissot-Dupont, Hervé / Lagier, Jean-Christophe / Mboup, Souleymane /
    Fournier, Pierre-Edouard / Raoult, Didier

    Travel medicine and infectious disease

    2021  Volume 40, Page(s) 101980

    Abstract: Background: In Marseille, France, the COVID-19 incidence evolved unusually with several successive epidemic phases. The second outbreak started in July, was associated with North Africa, and involved travelers and an outbreak on passenger ships. This ... ...

    Abstract Background: In Marseille, France, the COVID-19 incidence evolved unusually with several successive epidemic phases. The second outbreak started in July, was associated with North Africa, and involved travelers and an outbreak on passenger ships. This suggested the involvement of a new viral variant.
    Methods: We sequenced the genomes from 916 SARS-CoV-2 strains from COVID-19 patients in our institute. The patients' demographic and clinical features were compared according to the infecting viral variant.
    Results: From June 26th to August 14th, we identified a new viral variant (Marseille-1). Based on genome sequences (n = 89) or specific qPCR (n = 53), 142 patients infected with this variant were detected. It is characterized by a combination of 10 mutations located in the nsp2, nsp3, nsp12, S, ORF3a, ORF8 and N/ORF14 genes. We identified Senegal and Gambia, where the virus had been transferred from China and Europe in February-April as the sources of the Marseille-1 variant, which then most likely reached Marseille through Maghreb when French borders reopened. In France, this variant apparently remained almost limited to Marseille. In addition, it was significantly associated with a milder disease compared to clade 20A ancestor strains, in univariate analysis.
    Conclusion: Our results demonstrate that SARS-CoV-2 can genetically diversify rapidly, its variants can diffuse internationally and cause successive outbreaks.
    MeSH term(s) Adult ; Africa South of the Sahara/epidemiology ; Aged ; Amino Acid Substitution ; COVID-19/epidemiology ; COVID-19/virology ; China/epidemiology ; Coronavirus Papain-Like Proteases/genetics ; Coronavirus RNA-Dependent RNA Polymerase/genetics ; Female ; France/epidemiology ; Genome, Viral ; Humans ; Male ; Middle Aged ; Mutation ; Phylogeny ; SARS-CoV-2/classification ; SARS-CoV-2/genetics ; Travel ; Viral Nonstructural Proteins/genetics ; Viral Proteins/genetics ; Viroporin Proteins/genetics
    Chemical Substances ORF3a protein, SARS-CoV-2 ; ORF8 protein, SARS-CoV-2 ; Viral Nonstructural Proteins ; Viral Proteins ; Viroporin Proteins ; nsp2 protein, SARS-CoV-2 ; Coronavirus RNA-Dependent RNA Polymerase (EC 2.7.7.48) ; NSP12 protein, SARS-CoV-2 (EC 2.7.7.48) ; Coronavirus Papain-Like Proteases (EC 3.4.22.2) ; papain-like protease, SARS-CoV-2 (EC 3.4.22.2)
    Language English
    Publishing date 2021-01-31
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 2170891-5
    ISSN 1873-0442 ; 1477-8939
    ISSN (online) 1873-0442
    ISSN 1477-8939
    DOI 10.1016/j.tmaid.2021.101980
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Tracking the Elusive Function of Bacillus subtilis Hfq.

    Tatiana Rochat / Olivier Delumeau / Nara Figueroa-Bossi / Philippe Noirot / Lionello Bossi / Etienne Dervyn / Philippe Bouloc

    PLoS ONE, Vol 10, Iss 4, p e

    2015  Volume 0124977

    Abstract: RNA-binding protein Hfq is a key component of the adaptive responses of many proteobacterial species including Escherichia coli, Salmonella enterica and Vibrio cholera. In these organisms, the importance of Hfq largely stems from its participation to ... ...

    Abstract RNA-binding protein Hfq is a key component of the adaptive responses of many proteobacterial species including Escherichia coli, Salmonella enterica and Vibrio cholera. In these organisms, the importance of Hfq largely stems from its participation to regulatory mechanisms involving small non-coding RNAs. In contrast, the function of Hfq in Gram-positive bacteria has remained elusive and somewhat controversial. In the present study, we have further addressed this point by comparing growth phenotypes and transcription profiles between wild-type and an hfq deletion mutant of the model Gram-positive bacterium, Bacillus subtilis. The absence of Hfq had no significant consequences on growth rates under nearly two thousand metabolic conditions and chemical treatments. The only phenotypic difference was a survival defect of B. subtilis hfq mutant in rich medium in stationary phase. Transcriptomic analysis correlated this phenotype with a change in the levels of nearly one hundred transcripts. Albeit a significant fraction of these RNAs (36%) encoded sporulation-related functions, analyses in a strain unable to sporulate ruled out sporulation per se as the basis of the hfq mutant's stationary phase fitness defect. When expressed in Salmonella, B. subtilis hfq complemented the sharp loss of viability of a degP hfq double mutant, attenuating the chronic σE-activated phenotype of this strain. However, B. subtilis hfq did not complement other regulatory deficiencies resulting from loss of Hfq-dependent small RNA activity in Salmonella indicating a limited functional overlap between Salmonella and B. subtilis Hfqs. Overall, this study confirmed that, despite structural similarities with other Hfq proteins, B. subtilis Hfq does not play a central role in post-transcriptional regulation but might have a more specialized function connected with stationary phase physiology. This would account for the high degree of conservation of Hfq proteins in all 17 B. subtilis strains whose genomes have been sequenced.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2015-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Lack of interchangeability of Hfq-like proteins.

    Rochat, Tatiana / Bouloc, Philippe / Yang, Qi / Bossi, Lionello / Figueroa-Bossi, Nara

    Biochimie

    2012  Volume 94, Issue 7, Page(s) 1554–1559

    Abstract: Hfq is an RNA-binding protein that participates in the regulatory activity of small non-coding RNAs (sRNAs) in many species of bacteria. Hfq protein was first crystallized from Staphylococcus aureus and this crystal structure constitutes a hallmark for ... ...

    Abstract Hfq is an RNA-binding protein that participates in the regulatory activity of small non-coding RNAs (sRNAs) in many species of bacteria. Hfq protein was first crystallized from Staphylococcus aureus and this crystal structure constitutes a hallmark for bacterial Sm-like proteins. Paradoxically, however, the functional relevance/role of S. aureus Hfq (Hfq(SA)) remains uncertain, as growing evidence suggests that the hfq(SA) gene is expressed at very low levels or unexpressed in many S. aureus strains. To gather further insight, in the present work we exchanged the structural portion of the hfq gene of Salmonella enterica serovar Typhimurium (hfq(STM)) with hfq(SA) and analyzed the effects of the replacement on various Hfq-related phenotypes. Our results show that the replacement strain - in spite of expressing Hfq(SA) at levels comparable to Hfq(STM) in wild-type Salmonella - behaves as an hfq null mutant in three discrete small RNA-mediated regulatory responses. These defects correlate with an abrupt reduction in the intracellular concentration of sRNAs, as observed in an hfq null mutant. Failure of Hfq(SA) to protect Salmonella sRNAs from degradation suggests that Hfq(Sa) does not bind to these sRNAs. A parallel study with the Borrelia burgdorferi hfq gene (hfq(BB)) gave essentially identical results: when made from a single copy chromosomal gene, Hfq(BB) fails to substitute for Hfq(STM) in sRNA-mediated regulation.
    MeSH term(s) Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Base Sequence ; Borrelia burgdorferi/genetics ; Chromosomes, Bacterial/genetics ; Genetic Engineering ; Host Factor 1 Protein/genetics ; Host Factor 1 Protein/metabolism ; RNA, Bacterial/metabolism ; RNA, Small Untranslated/metabolism ; Recombination, Genetic ; Salmonella enterica/genetics ; Staphylococcus aureus/genetics
    Chemical Substances Bacterial Proteins ; Host Factor 1 Protein ; RNA, Bacterial ; RNA, Small Untranslated
    Language English
    Publishing date 2012-07
    Publishing country France
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120345-9
    ISSN 1638-6183 ; 0300-9084
    ISSN (online) 1638-6183
    ISSN 0300-9084
    DOI 10.1016/j.biochi.2012.01.016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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