Publications

Search or filter publications

Filter by type:

Filter by publication type

Filter by year:

to

Results

  • Showing results for:
  • Reset all filters

Search results

  • Journal article
    Brown DR, Barton G, Pan Z, Buck M, Wigneshweraraj Set al., 2014,

    Nitrogen stress response and stringent response are coupled in Escherichia coli

    , Nature Communications, Vol: 5, ISSN: 2041-1723

    Assimilation of nitrogen is an essential process in bacteria. The nitrogen regulation stress response is an adaptive mechanism used by nitrogen-starved Escherichia coli to scavenge for alternative nitrogen sources and requires the global transcriptional regulator NtrC. In addition, nitrogen-starved E. coli cells synthesize a signal molecule, guanosine tetraphosphate (ppGpp), which serves as an effector molecule of many processes including transcription to initiate global physiological changes, collectively termed the stringent response. The regulatory mechanisms leading to elevated ppGpp levels during nutritional stresses remain elusive. Here, we show that transcription of relA, a key gene responsible for the synthesis of ppGpp, is activated by NtrC during nitrogen starvation. The results reveal that NtrC couples these two major bacterial stress responses to manage conditions of nitrogen limitation, and provide novel mechanistic insights into how a specific nutritional stress leads to elevating ppGpp levels in bacteria.
  • Journal article
    Lambert SM, Langley DR, Garnett JA, Angell R, Hedgethorne K, Meanwell NA, Matthews SJet al., 2014,

    The crystal structure of NS5A domain 1 from genotype 1a reveals new clues to the mechanism of action for dimeric HCV inhibitors

    , PROTEIN SCIENCE, Vol: 23, Pages: 723-734, ISSN: 0961-8368
  • Journal article
    Prosser GA, Larrouy-Maumus G, de Carvalho LPS, 2014,

    Metabolomic strategies for the identification of new enzyme functions and metabolic pathways

    , EMBO REPORTS, Vol: 15, Pages: 657-669, ISSN: 1469-221X
  • Journal article
    Xu Y, Plechanovova A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJet al., 2014,

    Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4

    , NATURE COMMUNICATIONS, Vol: 5, ISSN: 2041-1723
  • Journal article
    Phetcharaburanin J, Hong HA, Colenutt C, Bianconi I, Sempere L, Permpoonpattana P, Smith K, Dembek M, Tan S, Brisson M-C, Brisson AR, Fairweather NF, Cutting SMet al., 2014,

    The spore-associated protein BclA1 affects the susceptibility of animals to colonization and infection by Clostridium difficile

    , MOLECULAR MICROBIOLOGY, Vol: 92, Pages: 1025-1038, ISSN: 0950-382X
  • Journal article
    Stemberk V, Jones RPO, Moroz O, Atkin KE, Edwards AM, Turkenburg JP, Leech AP, Massey RC, Potts JRet al., 2014,

    Evidence for steric regulation of fibrinogen binding to staphylococcus aureus Fibronectin-binding Protein A ( FnBPA)

    , Journal of Biological Chemistry, Vol: 289, Pages: 12842-12851, ISSN: 0021-9258

    The adjacent fibrinogen (Fg)- and fibronectin (Fn)-binding sites on Fn-binding protein A (FnBPA), a cell surface protein from Staphylococcus aureus, are implicated in the initiation and persistence of infection. FnBPA contains a single Fg-binding site (that also binds elastin) and multiple Fn-binding sites. Here, we solved the structure of the N2N3 domains containing the Fg-binding site of FnBPA in the apo form and in complex with a Fg peptide. The Fg binding mechanism is similar to that of homologous bacterial proteins but without the requirement for “latch” strand residues. We show that the Fg-binding sites and the most N-terminal Fn-binding sites are nonoverlapping but in close proximity. Although Fg and a subdomain of Fn can form a ternary complex on an FnBPA protein construct containing a Fg-binding site and single Fn-binding site, binding of intact Fn appears to inhibit Fg binding, suggesting steric regulation. Given the concentrations of Fn and Fg in the plasma, this mechanism might result in targeting of S. aureus to fibrin-rich thrombi or elastin-rich tissues.
  • Journal article
    Hachani A, Allsopp LP, Oduko Y, Filloux Aet al., 2014,

    The VgrG Proteins Are "à la Carte" Delivery Systems for Bacterial Type VI Effectors

    , Journal of Biological Chemistry, Vol: 289, Pages: 17872-17884, ISSN: 1083-351X

    The bacterial type VI secretion system (T6SS) is a supra-molecular complex akin to bacteriophage tails, with VgrG proteins acting as a puncturing device. The Pseudomonas aeruginosa H1-T6SS has been extensively characterized. It is involved in bacterial killing and in the delivery of three toxins, Tse1–3. Here, we demonstrate the independent contribution of the three H1-T6SS co-regulated vgrG genes, vgrG1abc, to bacterial killing. A putative toxin is encoded in the vicinity of each vgrG gene, supporting the concept of specific VgrG/toxin couples. In this respect, VgrG1c is involved in the delivery of an Rhs protein, RhsP1. The RhsP1 C terminus carries a toxic activity, from which the producing bacterium is protected by a cognate immunity. Similarly, VgrG1a-dependent toxicity is associated with the PA0093 gene encoding a two-domain protein with a putative toxin domain (Toxin_61) at the C terminus. Finally, VgrG1b-dependent killing is detectable upon complementation of a triple vgrG1abc mutant. The VgrG1b-dependent killing is mediated by PA0099, which presents the characteristics of the superfamily nuclease 2 toxin members. Overall, these data develop the concept that VgrGs are indispensable components for the specific delivery of effectors. Several additional vgrG genes are encoded on the P. aeruginosa genome and are not linked genetically to other T6SS genes. A closer inspection of these clusters reveals that they also encode putative toxins. Overall, these associations further support the notion of an original form of secretion system, in which VgrG acts as the carrier.
  • Journal article
    Liu B, Shadrin A, Sheppard C, Mekler V, Xu Y, Severinov K, Matthews S, Wigneshweraraj Set al., 2014,

    A bacteriophage transcription regulator inhibits bacterial transcription initiation by Sigma-factor displacement

    , Nucleic Acids Research, Vol: 42, Pages: 4294-4305, ISSN: 0305-1048

    Bacteriophages (phages) appropriate essential processes of bacterial hosts to benefit their own development. The multisubunit bacterial RNA polymerase (RNAp) enzyme, which catalyses DNA transcription, is targeted by phage-encoded transcription regulators that selectively modulate its activity. Here, we describe the structural and mechanistic basis for the inhibition of bacterial RNAp by the transcription regulator P7 encoded by Xanthomonas oryzae phage Xp10. We reveal that P7 uses a two-step mechanism to simultaneously interact with the catalytic β and β’ subunits of the bacterial RNAp and inhibits transcription initiation by inducing the displacement of the σ70-factor on initial engagement of RNAp with promoter DNA. The new mode of interaction with and inhibition mechanism of bacterial RNAp by P7 underscore the remarkable variety of mechanisms evolved by phages to interfere with host transcription.
  • Journal article
    Reichmann NT, Cassona CP, Monteiro JM, Bottomley AL, Corrigan RM, Foster SJ, Pinho MG, Gruendling Aet al., 2014,

    Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in <i>Staphylococcus aureus</i>

    , MOLECULAR MICROBIOLOGY, Vol: 92, Pages: 273-286, ISSN: 0950-382X
  • Journal article
    Sharma A, Leach RN, Gell C, Zhang N, Burrows PC, Shepherd DA, Wigneshweraraj S, Smith DA, Zhang X, Buck M, Stockley PG, Tuma Ret al., 2014,

    Domain movements of the enhancer-dependent sigma factor drive DNA delivery into the RNA polymerase active site: insights from single molecule studies

    , NUCLEIC ACIDS RESEARCH, Vol: 42, Pages: 5177-5190, ISSN: 0305-1048

This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.

Request URL: http://www.imperial.ac.uk:80/respub/WEB-INF/jsp/search-t4-html.jsp Request URI: /respub/WEB-INF/jsp/search-t4-html.jsp Query String: id=288&limit=10&page=64&respub-action=search.html Current Millis: 1713578004486 Current Time: Sat Apr 20 02:53:24 BST 2024