@article{BarazaNeserJacksonetal.2016, author = {Baraza, Lilechi D. and Neser, Wekesa and Jackson, Korir Cheruiyot and Fredrick, Juma B. and Dennis, Ochieno and Wairimu, Kamau R. and Keya, Aggrey Osogo and Heydenreich, Matthias}, title = {Antimicrobial Coumarins from the Oyster Culinary-Medicinal Mushroom, Pleurotus ostreatus (Agaricomycetes), from Kenya}, series = {International journal of medicinal mushrooms}, volume = {18}, journal = {International journal of medicinal mushrooms}, publisher = {Begell House}, address = {Danbury}, issn = {1521-9437}, doi = {10.1615/IntJMedMushrooms.v18.i10.60}, pages = {905 -- 913}, year = {2016}, abstract = {Pleurotus ostreatus has been widely used as food because of its nutritional and medicinal properties. These have been attributed to the presence of macronutrients, minerals, vitamins, and amino acids, among other secondary metabolites. There are, however, few reports on the antimicrobial activities of different classes of purified compounds from P. ostreatus. This led to the current study, the objective of which was to chemically characterize the antibiotic activities of P. ()streams against selected human pathogenic bacteria and endophytic fungi. Chemical structures were determined using spectroscopic methods and by comparison with values of related structures reported in the literature. Pure compounds from P. ostreatus were tested in vitro against pathogenic bacteria (Staphylococcus aureus and Escherichia coli) and endophytic fungi (Pencillium digitatum and Fusarium prolferatum). A new compound, (E)-5,7-dimethoxy-6-(3-methylbuta-1,3-dienyl)-2H-chromen-2-one (5-methoxy-(E)-suberodiene) (compound 2), along with ergosterol (compound I.) and 5,7-dimethoxy-6-(3-methylbut-2-enyl)-2H-chromen-2-one (toddaculin; compound 3), were isolated from the fruiting bodies of P. ostreatus. The growth of S. aureus,E proliferatum, and P. digitatum colonies was inhibited in media containing compound 2, with minimum inhibitory concentrations closely comparable to those of conventional antibiotics.}, language = {en} } @article{BartholomaeusFedyuninFeistetal.2016, author = {Bartholom{\"a}us, Alexander and Fedyunin, Ivan and Feist, Peter and Sin, Celine and Zhang, Gong and Valleriani, Angelo and Ignatova, Zoya}, title = {Bacteria differently regulate mRNA abundance to specifically respond to various stresses}, series = {Geology}, volume = {374}, journal = {Geology}, publisher = {Royal Society}, address = {London}, issn = {1364-503X}, doi = {10.1098/rsta.2015.0069}, pages = {16}, year = {2016}, abstract = {Environmental stress is detrimental to cell viability and requires an adequate reprogramming of cellular activities to maximize cell survival. We present a global analysis of the response of Escherichia coli to acute heat and osmotic stress. We combine deep sequencing of total mRNA and ribosome-protected fragments to provide a genome-wide map of the stress response at transcriptional and translational levels. For each type of stress, we observe a unique subset of genes that shape the stress-specific response. Upon temperature upshift, mRNAs with reduced folding stability up-and downstream of the start codon, and thus with more accessible initiation regions, are translationally favoured. Conversely, osmotic upshift causes a global reduction of highly translated transcripts with high copy numbers, allowing reallocation of translation resources to not degraded and newly synthesized mRNAs.}, language = {en} } @misc{ConnorZantowHustetal.2016, author = {Connor, Daniel Oliver and Zantow, Jonas and Hust, Michael and Bier, Frank Fabian and von Nickisch-Rosenegk, Markus}, title = {Identification of novel immunogenic proteins of Neisseria gonorrhoeae by phage display}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, number = {541}, issn = {1866-8372}, doi = {10.25932/publishup-41107}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-411077}, pages = {24}, year = {2016}, abstract = {Neisseria gonorrhoeae is one of the most prevalent sexually transmitted diseases worldwide with more than 100 million new infections per year. A lack of intense research over the last decades and increasing resistances to the recommended antibiotics call for a better understanding of gonococcal infection, fast diagnostics and therapeutic measures against N. gonorrhoeae. Therefore, the aim of this work was to identify novel immunogenic proteins as a first step to advance those unresolved problems. For the identification of immunogenic proteins, pHORF oligopeptide phage display libraries of the entire N. gonorrhoeae genome were constructed. Several immunogenic oligopeptides were identified using polyclonal rabbit antibodies against N. gonorrhoeae. Corresponding full-length proteins of the identified oligopeptides were expressed and their immunogenic character was verified by ELISA. The immunogenic character of six proteins was identified for the first time. Additional 13 proteins were verified as immunogenic proteins in N. gonorrhoeae.}, language = {en} } @misc{YanFriemelAloisietal.2016, author = {Yan, Robert and Friemel, Martin and Aloisi, Claudia and Huynen, Martijn and Taylor, Ian A. and Leimk{\"u}hler, Silke and Pastore, Annalisa}, title = {The eukaryotic-specific Isd11 is a complex- orphan protein with ability to bind the prokaryotic IscS}, series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, journal = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe}, number = {551}, issn = {1866-8372}, doi = {10.25932/publishup-41190}, url = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-411906}, pages = {14}, year = {2016}, abstract = {The eukaryotic protein Isd11 is a chaperone that binds and stabilizes the central component of the essential metabolic pathway responsible for formation of iron-sulfur clusters in mitochondria, the desulfurase Nfs1. Little is known about the exact role of Isd11. Here, we show that human Isd11 (ISD11) is a helical protein which exists in solution as an equilibrium between monomer, dimeric and tetrameric species when in the absence of human Nfs1 (NFS1). We also show that, surprisingly, recombinant ISD11 expressed in E. coli co-purifies with the bacterial orthologue of NFS1, IscS. Binding is weak but specific suggesting that, despite the absence of Isd11 sequences in bacteria, there is enough conservation between the two desulfurases to retain a similar mode of interaction. This knowledge may inform us on the conservation of the mode of binding of Isd11 to the desulfurase. We used evolutionary evidence to suggest Isd11 residues involved in the interaction.}, language = {en} }