VAAM-Jahrestagung 2012 18.–21. März in Tübingen

191Bei den verschiedenen Unfallversicherungsträgern (z. B. Unfallkassen desBundes und der Länder oder gewerbliche Berufsgenossenschaften wie dieBG RCI = Berufsgenossenschaft der chemischen Industrie) fließen unsereErgebnisse in branchenbezogene Handlungsanleitungen,Informationsschriften und Regeln ein. Mikrobiologische Untersuchungenwerden von diesen Institutionen auch durchgeführt, um denZusammenhang zwischen dem Auftreten einer berufs-bedingtenInfektionskrankheit oder auch allergisch oder toxisch bedingtenAtemwegserkrankung und dem Vorhandensein von bestimmtenInfektionserregern, Allergenen oder toxisch wirkenden Substanzenmikrobiologischen Ursprungs aufzuzeigen.In verschiedenen staatlichen Gremien, wie dem Ausschuss für biologischeArbeitsstoffe (ABAS) mit seinen verschiedenen Unterausschüssen undArbeitskreisen (http://www.baua.de/de/Themen-von-A-Z/Biologische-Arbeitsstoffe/ABAS/ABAS.html), werden Ergebnisse ausmikrobiologischen Untersuchungen herangezogen um technische Re-gelnzu biologischen Arbeitsstoffen zu erstellen(http://www.baua.de/de/Themen-von-A-Z/Biologische-Arbeitsstoffe/TRBA/TRBA.html).Die Untersuchungen zur Gefährdungsbeurteilung von Beschäftigten durchExposition gegenüber biologischen Arbeitsstoffen am Arbeitsplatzerfolgen mit Hilfe eines klassischen mikrobio-logischen Verfahrens: derAnzucht von Mikroorganismen (i. d. R. Bakterien, Hefen und Schimmelpilze)auf Nährböden und Bestimmung einer Koloniezahl als AnzahlKolonie bildender Ein-heiten, KBE bzw. englisch: colony forming units,cfu) bezogen auf ein Aliquot des Materials, aus dem die Organismenisoliert wurden (häufig Luft, aber auch Wasser u. a. Flüssigkeiten oderunterschiedliche feste Materialien, die als Mikroorganismenquelle inBetracht kommen).Insbesondere wenn es um einen raschen Nachweis des Vorhandenseinsvon Mikroorganismen überhaupt oder aber um den gezielten Nachweisausgewählter Organismen wie z. B. von Legionella pneumophila,Serogruppe 1 aus dem Befeuchterwasser einer sogenannten Klimaan-lageoder von Mycobacterium immunogenum im Kühlschmierstoff einesMetallfertigungsbetrie-bes geht, kommen auch modernemolekularbiologische Verfahren oder Fluoreszenzmikroskopi-scheTechniken zum Einsatz.QDV4-FGFrom academia to industry, and back: Microbiologicalresearch to make life easier, better and more beautifulM. EgertHochschule Furtwangen University, Department of Mechanical andProcess Engineering, Villingen-Schwenningen, GermanyThe consumer goods producing industry represents an attractive employerfor microbiologist, that are interested to use their knowledge andtechnological skills not only in the field of quality control, but also forresearch and development of novel products for very dynamic and profitorientedmarkets.The aim of this presentation is to provide some personal insight into thenature of the job of a microbiologist (with a strong background inmolecular microbial ecology), working in the area of consumer goods,using the Henkel AG & Co. KGaA as an example. Henkel, headquarteredin Düsseldorf / Germany, has about 48,000 employees worldwide andcounts among the most internationally aligned German-based companiesin the global marketplace. The company has three globally operatingbusiness sectors: Laundry & Homecare, Cosmetics & Toiletries andAdhesive Technologies.Using selected studies from the fields of skin microbiology [1], householdhygiene [2], and rapid methods for quality control, the talk will provide abrief overview of the diversity of factors and topics drivingmicrobiological projects at a company like Henkel. In addition, somepersonal comments on the requirements for a successful application andsome general pros and cons of starting a career in the consumer goodsproducing industry will be given. Finally, the job profile of a professorworking at an University of Applied Sciences will be presented as a careeroption that combines several aspects of an industrial and academic career.1.M. Egert, I. Schmidt, H. Höhne, T. Lachnit, R.A. Schmitz and R. Breves. Ribosomal RNA-basedprofiling of bacteria in the axilla of healthy males indicates right-left asymmetry in bacterialactivity. FEMS Microbiol. Ecol. 77 (2011), p. 146-153.2.M. Egert, I. Schmidt, K. Bussey and R. Breves. A glimpse under the rim – the composition ofmicrobial biofilm communities in domestic toilets. J. Appl. Microbiol. 108 (2010), p. 1167-1174.RSV001Functional interaction of the Escherichia coli transportersDctA and DcuB with the sensor kinase DcuSJ. Witan*, G. UndenJohannes Gutenberg-Universität, Institut für Mikrobiologie undWeinforschung, Mainz, GermanyEscherichia coli can use C 4-dicarboxylates as carbon and energy sourcesfor aerobic or anaerobic respiration. The two component system DcuSRactivates the transcription of dctA (succinate import), dcuB (fumaratesuccinateantiport), fumB (fumarase) and frdABCD (fumarate reductase) inthe presence of C 4-dicarboxylates [1]. DcuSR consists of the membraneintegral sensor kinase DcuS and the cytoplasmic response regulator DcuR.DcuS contains a periplasmic PAS domain which responds to the presenceof C 4-dicarboxylates.DctA is the main transporter for the uptake of C 4-dicarboxylates underaerobic conditions. Under anaerobic conditions the DcuB transportercatalyses a fumarate/succinate antiport which is essential for the fumaraterespiration [1]. DctA and DcuB function as essential co-sensors of DcuS.Deletion of the carriers causes constitutive activation of DcuSR [2, 3].Overproduction of DctA under anaerobic conditions allowed it to replaceDcuB in co-sensing, suggesting that DcuB and DctA are functionallyequivalent in this capacity. Interaction of the integral membrane proteinDcuS with DctA and DcuB was analysedin vivowith a bacterial twohybridsystem based on theBordetella pertussisadenylate cyclase (BACTH)and by fluorescence resonance energy transfer (FRET). Direct interactionof DctA and DcuB with DcuS was observed. DctA contains a cytosolicamphipathic helix following its last transmembrane helix. Mutationalanalysis demonstrated the importance of this helix in interactions, cosensingand transport.1. Zientzet al.J. Bacteriol.180(1998), p. 5421-54252. Golbyet al.J. Bacteriol.181(1999), p. 1238-12483. Kleefeldet al.J. Biol. Chem.284(2009), p. 265-275RSV002YhbJ - a novel RNA binding protein functions as mediator ofsignal transductionin the hierarchically acting GlmYZ sRNAcascadeY. Göpel* 1 , B. Reichenbach 1 , K. Papenfort 2 , C. Sharma 2 , J. Vogel 2 , B. Görke 11 Institute for Mikrobiology & Genetics, General Mikrobiology, Göttingen,Germany2 Institute for Molecular Infection Biology, RNA Biology, Würzburg, GermanyIn Escherichia coli, expression of key enzyme glucosamine-6-phosphatesynthase (GlmS) is feedback-regulated by two homologous sRNAs, GlmYand GlmZ, in a hierarchical manner [1,2,3,4]. GlmS catalyzes formation ofglucosamine-6-phosphate (GlcN6P), an essential precursor for cell wallbiosynthesis. Depletion of cellular GlcN6P induces accumulation of GlmYby a post-transcriptional mechanism [5]. GlmY counteracts processing ofGlmZ. Exclusively unprocessed GlmZ can base-pair with the glmS 5’ UTRand activate translation. Subsequently, GlmS is synthesized and refills theGlcN6P pool in the cell. The mechanism of signal transduction fromGlmY to GlmZ involves the novel RNA binding protein YhbJ. In mutantslacking yhbJ processing of GlmZ is abolished and glmS is chronicallyactivated [1,4]. Here we show that GlmZ is processed by RNase E and thatYhbJ and RNase E interact. Furthermore, YhbJ drastically stimulates theRNase E-dependent processing of GlmZ in vitro suggesting that YhbJrecruits GlmZ to its processing machinery. Indeed, YhbJ specifically bindsboth sRNAs in vivo and in vitro and this binding appears to be modulatedby cellular GlcN6P levels. Upon GlcN6P-starvation GlmY accumulatesand sequesters YhbJ thereby outcompeting GlmZ. Under these conditionsGlmZ is protected from processing and able to activate glmS expression.Our data indicate that YhbJ could be a novel specificity factor guidingRNase E to its substrate GlmZ.1. Kalamorz, F.et al.,2007 Mol.Microbiol. 65:1518-15332. Urban, J.H.et al.,2007 J.Mol.Biol. 373:521-5283. Reichenbach, B.et al.,2008 Nucleic Acids Res. 36:2570-25804. Urban, J.H. and J. Vogel, 2008 PLoS Biol.6:e645. Reichenbach, B., Göpel, Y. and B. Görke, 2009 Mol. Microbiol. 75:1054-1070RSV003Structural insights into the redox-switch mechanism of HypR, adisulfide stress-sensing MarR/DUF24-family regulator of BacillussubtilisH. Antelmann* 1 , B.K. Chi 1 , P. Waack 2 , K. Gronau 1 , D. Becher 1 ,D. Albrecht 1 , W. Hinrichs 2 , R.J. Read 3 , G. Palm 21 University of Greifswald, Institute for Microbiology, Greifswald, Germany2 University of Greifswald, Institute for Biochemistry, Greifswald, Germany3 University of Cambridge, CIMR Haematology, Cambridge, United KingdomBacillus subtilis encodes redox-sensing MarR-type regulators belonging tothe 1-Cys OhrR and 2-Cys DUF24-families that are conserved amongbacteria and control virulence functions in pathogens via thiol-basedredox-switches. While OhrR proteins respond to organic hydroperoxides,the DUF24-family senses electrophiles such as diamide, quinones oraldehydes [1]. Here, we characterize the novel redox-sensingMarR/DUF24-family regulator HypR (YybR) that is activated by disulfidestress caused by diamide and NaOCl in B. subtilis. HypR controlspositively a flavin oxidoreductase HypO that confers protection againstNaOCl stress [2]. The conserved N-terminal Cys14 residue of HypR has alower pK a of 6.4 and is essential for activation of hypO transcription bydisulfide stress. HypR resembles a 2-Cys-type regulator that is activated byCys14-Cys49' intersubunit disulfide formation. The crystal structures ofreduced and oxidized HypR proteins were resolved revealing themechanism of HypR activation. In reduced HypR a hydrogen-bondingBIOspektrum | Tagungsband 2012