Franz Narberhaus

Ruhr University Bochum

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Meriyem Aktas

Ruhr University Bochum

Hauke Hennecke

ETH Zurich

Christian Twittenhoff

Ruhr University Bochum

Julia E. Bandow

Ruhr University Bochum

Birgit Klinkert

Ardeypharm (Germany)

Bernd Masepohl

Ruhr University Bochum

Sina Langklotz

Ruhr University Bochum

Francesco Righetti

Karolinska University Hospital

Erh‐Min Lai

Institute of Plant and Microbial Biology, Academia Sinica

Hans‐Martin Fischer

Stuttgart University of Applied Sciences

Cooperative Institutions

Ruhr University Bochum

175

Board of the Swiss Federal Institutes of Technology

ETH Zurich

Helmholtz Centre for Infection Research

Technische Universität Braunschweig

Max Planck Society

Czech Academy of Sciences, Institute of Microbiology

École Polytechnique Fédérale de Lausanne

University of Freiburg

Ohio University

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Separation of VUV/UV photons and reactive particles in the effluent of a He/O₂atmospheric pressure plasma jet

Journal of Physics D Applied Physics (2011)

Sebastian Schneider J-W Lackmann Franz Narberhaus Julia E. Bandow B Denis

The incorrect surface density of bacteria (4 × 10 6 cm -2 ) on the agar plate was given in the right column, line 16, on page 3 in section 3 'Substrate preparation'. The correct surface coverage was 2.2 × 10 3 cm -2 . This surface coverage was selected to obtain a homogeneous surface coverage after 18 hours of incubation at 37 °C. The term 'monolayer surface coverage' in the same section is used to stress the fact that there is no multilayer of bacteria during the treatment and that the shadowing effects can be neglected. However, the surface is not fully covered by one continuous layer of bacteria. This error and ambiguity in the use of the term 'monolayer surface coverage' does not affect the interpretation of the results and conclusions in the article. Additionally, the names of Volker Schulz-von der Gathen and Nikolas Knake have been misspelled in the 'Acknowledgments'. The authors apologize for any inconvenience and confusion they may have caused.

Confusion

Surface pressure

10.1088/0022-3727/44/37/379501

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Citations (19)

Faculty Opinions recommendation of Riboswitches for the alarmone ppGpp expand the collection of RNA-based signaling systems.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature (2018)

Franz Narberhaus

Riboswitch

10.3410/f.733278275.793546435

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In Vitro Characterization of the Enzyme Properties of the Phospholipid N -Methyltransferase PmtA from Agrobacterium tumefaciens

Journal of Bacteriology (2009)

Meriyem Aktas Franz Narberhaus

Agrobacterium tumefaciens requires phosphatidylcholine (PC) in its membranes for plant infection. The phospholipid N-methyltransferase PmtA catalyzes all three transmethylation reactions of phosphatidylethanolamine (PE) to PC via the intermediates monomethylphosphatidylethanolamine (MMPE) and dimethylphosphatidylethanolamine (DMPE). The enzyme uses S-adenosylmethionine (SAM) as the methyl donor, converting it to S-adenosylhomocysteine (SAH). Little is known about the activity of bacterial Pmt enzymes, since PC biosynthesis in prokaryotes is rare. In this article, we present the purification and in vitro characterization of A. tumefaciens PmtA, which is a monomeric protein. It binds to PE, the intermediates MMPE and DMPE, the end product PC, and phosphatidylglycerol (PG) and phosphatidylinositol. Binding of the phospholipid substrates precedes binding of SAM. We used a coupled in vitro assay system to demonstrate the enzymatic activity of PmtA and to show that PmtA is inhibited by the end products PC and SAH and the antibiotic sinefungin. The presence of PG stimulates PmtA activity. Our study provides insights into the catalysis and control of a bacterial phospholipid N-methyltransferase.

O-methyltransferase

Phosphatidylethanolamine

10.1128/jb.01591-08

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Citations (28)

Faculty Opinions recommendation of YtfK activates the stringent response by triggering the alarmone synthetase SpoT in Escherichia coli.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature (2020)

Franz Narberhaus

10.3410/f.737108188.793569430

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A Small Regulatory RNA Controls Cell Wall Biosynthesis and Antibiotic Resistance

mBio (2018)

Jessica Borgmann Sina Schäkermann Julia E. Bandow Franz Narberhaus

The alphaproteobacterium Agrobacterium tumefaciens is able to infect various eudicots causing crown gall tumor formation. Based on its unique ability of interkingdom gene transfer, Agrobacterium serves as a crucial biotechnological tool for genetic manipulation of plant cells. The presence of hundreds of putative sRNAs in this organism suggests a considerable impact of riboregulation on A. tumefaciens physiology. Here, we characterized the biological function of the sRNA PmaR that controls various processes crucial for growth, motility, and virulence. Among the genes directly targeted by PmaR is ampC coding for a beta-lactamase that confers ampicillin resistance, suggesting that the sRNA is crucial for fitness in the competitive microbial composition of the rhizosphere.

Carbenicillin

10.1128/mbio.02100-18

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Citations (16)

The C‐terminal end of LpxC is required for degradation by the FtsH protease

Molecular Microbiology (2005)

Frank Führer Sina Langklotz Franz Narberhaus

Summary Lipopolysaccharide (LPS) biosynthesis is essential in Gram negative bacteria. LpxC, the key enzyme in LPS formation, catalyses the limiting reaction and controls the ratio between LPS and phospholipids. As overproduction of LPS is toxic, the cellular amount of LpxC must be regulated carefully. The membrane‐bound protease FtsH controls the level of LpxC via proteolysis making FtsH the only essential protease of Escherichia coli . We found that the chaperones DnaK and DnaJ co‐purified with LpxC. However, degradation of LpxC was DnaK/J‐independent in contrast to turnover of the heat shock sigma factor σ 32 (RpoH). The stability of LpxC in a bacterial one‐hybrid system suggested that a terminus of LpxC might be important for degradation. Different LpxC truncations and extensions were constructed . Removal of at least five amino acids from the C‐terminus abolished degradation by FtsH in vivo . While addition of two aspartic acids to LpxC did not alter its half‐life, the exchange of the last two residues against aspartic acids resulted in stabilization. All stable LpxC enzymes were active in vivo as assayed by their high toxicity. Our data demonstrate that the C‐terminus of LpxC contains a signal sequence necessary for FtsH‐dependent degradation.

Proteolysis

10.1111/j.1365-2958.2005.04994.x

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Citations (105)

FourU: a novel type of RNA thermometer in Salmonella

Molecular Microbiology (2007)

Torsten Waldminghaus Nadja Heidrich Sabine Brantl Franz Narberhaus

Summary The translation of many heat shock and virulence genes is controlled by RNA thermometers. Usually, they are located in the 5′‐untranslated region (5′‐UTR) and block the Shine‐Dalgarno (SD) sequence by base pairing. Destabilization of the structure at elevated temperature permits ribosome binding and translation initiation. We have identified a new type of RNA thermometer in the 5′‐UTR of the Salmonella agsA gene, which codes for a small heat shock protein. Transcription of the agsA gene is controlled by the alternative sigma factor σ 32 . Additional translational control depends on a stretch of four uridines that pair with the SD sequence. Mutations in this region affect translation in vivo . Structure probing experiments demonstrate a temperature‐controlled opening of the SD region in vitro . Toeprinting (primer extension inhibition) shows that ribosome binding is dependent on high temperatures. Together with a postulated RNA thermometer upstream of the Yersinia pestis virulence gene lcrF ( virF ), the 5′‐UTR of Salmonella agsA might be the founding member of a new class of RNA thermometers that we propose to name ‘fourU’ thermometers.

Thermometer

10.1111/j.1365-2958.2007.05794.x

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Citations (154)

Coordinated regulation of nitrogen fixation and molybdate transport by molybdenum

Molecular Microbiology (2018)

Lisa Demtröder Franz Narberhaus Bernd Masepohl

Summary Biological nitrogen fixation, the reduction of chemically inert dinitrogen to bioavailable ammonia, is a central process in the global nitrogen cycle highly relevant for life on earth. N 2 reduction to NH 3 is catalyzed by nitrogenases exclusively synthesized by diazotrophic prokaryotes. All diazotrophs have a molybdenum nitrogenase containing the unique iron‐molybdenum cofactor FeMoco. In addition, some diazotrophs encode one or two alternative Mo‐free nitrogenases that are less efficient at reducing N 2 than Mo‐nitrogenase. To permit biogenesis of Mo‐nitrogenase and other molybdoenzymes when Mo is scarce, bacteria synthesize the high‐affinity molybdate transporter ModABC. Generally, Mo supports expression of Mo‐nitrogenase genes, while it represses production of Mo‐free nitrogenases and ModABC. Since all three nitrogenases and ModABC can reach very high levels at suitable Mo concentrations, tight Mo‐mediated control saves considerable resources and energy. This review outlines the similarities and differences in Mo‐responsive regulation of nitrogen fixation and molybdate transport in diverse diazotrophs.

Sulfite oxidase

10.1111/mmi.14152

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Citations (51)

Identification of the Bradyrhizobium japonicum degP gene as part of an operon containing small heat-shock protein genes

Archives of Microbiology (1998)

Franz Narberhaus Wolfgang Weiglhofer Hans‐Martin Fischer Hauke Hennecke

Bradyrhizobium japonicum

10.1007/s002030050547

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Citations (12)

Identification of a Turnover Element in Region 2.1 of Escherichia coli σ ³² by a Bacterial One-Hybrid Approach

Journal of Bacteriology (2005)

Markus Obrist Franz Narberhaus

Induction of the heat shock response in Escherichia coli requires the alternative sigma factor sigma32 (RpoH). The cellular concentration of sigma32 is controlled by proteolysis involving FtsH, other proteases, and the DnaKJ chaperone system. To identify individual sigma32 residues critical for degradation, we used a recently developed bacterial one-hybrid system and screened for stabilized versions of sigma32. The five single point mutations that rendered the sigma factor more stable mapped to positions L47, A50, and I54 in region 2.1. Strains expressing the stabilized sigma32 variants exhibited elevated transcriptional activity, as determined by a groE-lacZ fusion. Structure calculations predicted that the three mutated residues line up on the same face of an alpha-helix in region 2.1, suggesting that they are positioned to interact with proteins of the degradation machinery.

Sigma factor

Proteolysis

Chaperone (clinical)

10.1128/jb.187.11.3807-3813.2005

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Citations (38)