A. C. R. Ngo, B. Celebi, S. N. Hermann Hadewig, C. Mügge, D. Tischler Selective Pressure Leads to an Improved Synthetic Consortium Fit for Dye Degradation. Chemosphere (2024) DOI:10.1016/j.chemosphere.2024.142489
F. P. J. Schultes, L. Welter, D. Hufnagel, M. Heghmanns, M. Kasanmascheff, C. Muegge, An Active and Versatile Electron Transport System for Cytochrome P450 Monooxygenases from the Alkane Degrading Organism Acinetobacter Sp. OC4. ChemBioChem (2024) DOI:10.1002/cbic.202400098
B. M. Nestl, B. A. Nebel, V. Resch, M. Schürmann, D. Tischler, The development and opportunities of predictive biotechnology (2024) ChemBioChem. DOI: 10.1002/cbic.202300863
A. Maier, T. Knaus, F.G. Mutti, D. Tischler, Unlocking Catalytic Diversity of a Formate Dehydrogenase: Formamide Activity for NADPH Regeneration and Amine Supply for Asymmetric Reductive Amination (2024) ACS Catal. DOI: 10.1021/acscatal.3c05409
G. Vasilopoulos, L. Heflik, S. Czolkoss, F. Heinrichs, J. Kleetz, C. Yesilyurt, D. Tischler, P. Westhoff, M. Exterkate, M. Aktas, F. Narberhaus, Characterization of multiple lysophosphatidic acid acyltransferases in the plant pathogen Xanthomonas campestris (2024) FEBS J. DOI: 10.1111/febs.16996
S. Schröder, A. Maier, A. Schmidt, C. Mügge, D. Tischler, Enhancing biocatalytical N-N bond formation with the actinobacterial piperazate synthase KtzT (2024) Mol. Catal. DOI: 10.1016/j.mcat.2023.113733
2023
C. Mügge, N. Nowak, M. Strack, N. Metzler-Nolte and W. Weigand, Synthetic Approaches towards Peptide-Conjugates of Pt(II) Compounds with an (O,S) Chelating Moiety, European Journal of Inorganic Chemistry (2023) DOI:10.1002/ejic.202300519
D. Eggerichs, N. Weindorf, L.M. Mascotti, N. Welzel, M.W. Fraaijs, D. Tischler, Vanillyl alcohol oxidase from Diplodia corticola: Residues Ala420 and Glu466 allow for efficient catalysis of syringyl derivatives (2023) J. Biol. Chem. DOI: 10.1016/j.jbc.2023.104898
D. Eggerichs, K. Zilske, D. Tischler, Large Scale Production of Vanillin Using an Eugenol Oxidase from Nocardioides Sp. YR527. Molecular Catalysis (2023). https://doi.org/10.1016/j.mcat.2023.113277
J. Holste, C. Mügge, C. Distler, S. Schulz, The Uropygial Gland of the Great Cormorant (Phalacrocorax Carbo): II. Biochemical Analysis of the Uropygial Secretion. Journal of Ornithology (2023). https://doi.org/10.1007/s10336-023-02073-9
F.P.J. Schultes, M. Haarmann, D. Tischler, C. Mügge, Primary alcohols as substrates or products in whole-cell biocatalysis: Toxicity for Escherichia coli expression strains (2023) Molecular Catalysis DOI: 10.1016/j.mcat.2023.112979
J. Kratky, D. Eggerichs, T. Heine, S. Hofmann, P. Sowa, R.H. Weiße, D. Tischler, N. Sträter,Structural and Mechanistical Studies on Substrate and Stereo Selectivity of the Indole Monooxygenase VpIndA1: New Avenues for Biocatalytic Epoxidations and Sulfoxidations (2023) Angew. Chem. Int. Ed. DOI: 10.1002/anie.202300657
2022
V. Petkevičius, J. Vaitekūnas, M. Sadauskas, F.P.J. Schultes, D. Tischler, R. Meškys, The versatility of non-heme diiron monooxygenase PmlABCDEF: a single biocatalyst for a plethora of oxygenation reactions (2022) Catal. Sci. Technol. DOI: 10.1039/d2cy01167k.
J. Rolf, A.C.R. Ngo, S. Lütz, D. Tischler, K. Rosenthal, Cell-free protein synthesis for the screening of novel azoreductases and their preferred electron donor (2022) ChemBioChem DOI: 10.1002/cbic.202200121.
A.C.R. Ngo, D. Tischler, Microbial degradation of azo dyes: Approaches and prospects for a hazard-free conversion by microorganisms (2022) Int. J. Environ. Res. Public Health DOI: 10.3390/ijerph19084740.
D. Tischler, Buchrezension zu: The Autotrophic Biorefinery (2022) BioSpektrum DOI: 10.1007/s12268-022-1698-5.
A.C.R. Ngo, F.P.J. Schultes, A. Maier, S.N.H. Hadewig, D. Tischler, Improving biocatalytic properties of an azoreductase via the N-terminal fusion of formate dehydrogenase (2022) ChemBioChem DOI: 10.1002/cbic.202100643.
A.C.R. Ngo, J. Qi, C. Juric, I. Bento, D. Tischler, (2022) Identification of molecular basis that underlie enzymatic specificity of AzoRo from Rhodococcus opacus 1CP: A potential NADH:quinone oxidoreductase (2022) Arch. Biochem. Biophys. DOI: 10.1016/j.abb.2022.109123.
S. Kumaran, A.C.R. Ngo, F.P.J. Schultes, V.S. Saravanan, D. Tischler, In vitro and in silico analysis of Brilliant Black degradation by Actinobacteria and a Paraburkholderia sp. (2022) Genomics DOI: 10.1016/j.ygeno.2022.01.003.
D. Kowalczykiewicz, M. Przypis, L. Mestrom, A. Kumpf, D. Tischler, P.-L. Hagedoorn, U. Hanefeld, A. Jarzębski, K. Szymańska, Engineering of continuous bienzymatic cascade process using monolithic microreactors – in flow synthesis of trehalose (2022) Chem. Eng. J. DOI: 10.1016/j.cej.2021.131439.
2021
A.C.R. Ngo, C. Conrad, A.G. Baraibar, A. Matura, K.-H. van Pée, D. Tischler, Characterization of two hydrogen peroxide resistant peroxidases from Rhodococcus opacus 1CP (2021) Appl. Sci. DOI: 10.3390/app11177941.
A.C. Lienkamp, J. Burnik, T. Heine, E. Hofmann, D. Tischler, Characterization of the Glutathione S-Transferases Involved in Styrene Degradation in Gordonia rubripertincta CWB2 (2021) Microbiol. Spectr. DOI: 10.1128/Spectrum.00474-21.
R. Schwabe, C. Dittrich, J. Kadner, C.H.R. Senges, J.E. Bandow, D. Tischler, M. Schlömann, G. Levicán, O. Wiche, Secondary metabolites released by the rhizosphere bacteria Arthrobacter oxydans and Kocuria rosea enhance plant availability and soil–plant transfer of germanium (Ge) and rare earth elements (REEs) (2021) Chemosphere DOI:10.1016/j.chemosphere.2021.131466.
L. Martínez-Montero, D. Tischler, P. Süss, A. Schallmey, M.C.R. Franssen, F. Hollmann, C.E. Paul, Asymmetric azidohydroxylation of styrene derivatives mediated by a biomimetic styrene monooxygenase enzymatic cascade (2021) Catal. Sci. Technol. DOI:10.1039/D1CY00855B.
A.C. Lienkamp, M. Haarmann, D. Tischler, Gordonia: versatile actinobacteria for biotechnology (2021) IOP Conf. Ser.: Earth Environ. Sci. DOI:10.1088/1755-1315/689/1/012024.
O.Y. Mezenova, D. Tischler, S.V. Agafonova, N.Y. Mezenova, V.V. Volkov, D.A. Baranenko, T. Grimm, S. Riedel, Research and rational use of peptide and lipid compositions obtained by hydrolysis processing of collagen-containing tissues (2021) J. Int. Acad. Refrig. DOI:10.17586/1606-4313-2021-20-1-46-58.
A.H.Westphal, D. Tischler, W.J.H. van Berkel, Natural diversity of FAD-dependent 4-hydroxybenzoate hydroxylases (2021) Arch. Biochem. Biophyis. DOI: 10.1016/j.abb.2021.108820.
C.E. Paul, D. Eggerichs, A.H. Westphal, D. Tischler, W.J.H. van Berkel, Flavoprotein monooxygenases: Versatile biocatalysts (2021) Biotechnol. Adv. DOI: 10.1016/j.biotechadv.2021.107712.
G. Retamal-Morales, C.H.R. Senges, M. Stapf, A. Olguín, B. Modak, J.E. Bandow, D. Tischler, M. Schlömann, G. Levicán, Isolation and characterization of arsenic-binding siderophores from Rhodococcus erythropolis S43: role of heterobactin B and other heterobactin variants (2021) Appl. Microbiol. Biotechnol. DOI: 10.1007/s00253-021-11123-2
M. Hofmann, T. Heine, L. Malik, S. Hofmann, K. Joffroy, C.H.R Senges, J.E Bandow, D. Tischler, Screening for microbial metal-chelating siderophores for the removal of metal Ions from solutions (2021) Microorganisms DOI: 10.3390/microorganisms9010111
J. Zimmerling, M. Oelschlägel, C. Großmann, M. Voitel, M. Schlömann, D. Tischler, Biochemical characterization of phenylacetaldehyde dehydrogenases from styrene-degrading soil bacteria (2021) Appl. Biochem. Biotechnol. DOI: 10.1007/s12010-020-03421-8
2020
C. Mügge, T. Heine, A.G. Baraibar, W.J.H. van Berkel, C.E. Paul, D. Tischler, Flavin-dependent N-hydroxylating enzymes: distribution and application (2020) Appl. Microbiol. Biotechnol. DOI: 10.1007/s00253-020-10705-w
S. Böhmer, C. Marx, A. Gómez-Baraibar, M.M. Nowaczyk, D. Tischler, A. Hemschemeier, T. Happe, Evolutionary diverse Chlamydomonas reinhardtii Old Yellow Enzymes reveal distinctive catalytic properties and potential for whole-cell biotransformations (2020) Algal Res. DOI: 10.1016/j.algal.2020.101970
D. Tischler, A perspective on enzyme inhibitors from marine organisms (2020) Mar. Drugs DOI: 10.3390/MD18090431
D. Tischler, A. Kumpf, D. Eggerichs, T. Heine, Styrene monooxygenases, indole monooxygenases and related flavoproteins applied in bioremediation and biocatalysis (2020) Enzymes DOI: 10.1016/bs.enz.2020.05.011
A. Kumpf, D. Kowalczykiewicz, K. Szymańska, M. Mehnert, I. Bento, A. Łochowicz, A. Pollender, A. Jarzȩbski, D. Tischler, Immobilization of the highly active UDP-glucose pyrophosphorylase from Thermocrispum agreste provides a highly efficient biocatalyst for the production of UDP-glucose (2020) Front. Bioeng. Biotechnol. DOI: 10.3389/fbioe.2020.00740
D. Eggerichs, C. Mügge, J. Mayweg, U.-P. Apfel, D. Tischler, Enantioselective epoxidation by flavoprotein monooxygenases supported by organic solvents (2020) Catalysts DOI: 10.3390/catal10050568
M. Hofmann, G. Retamal-Morales, D. Tischler, Metal binding ability of microbial natural metal chelators and potential applications (2020) Nat. Prod. Rep. DOI: 10.1039/C9NP00058E
A. Maier, S. Wansel, A.G. Baraibar, C. Mügge, D. Tischler, N-hydroxydiamines - Versatile components for the synthesis of active ingredients (2020) BioSpektrum DOI: 10.1007/s12268-020-1374-6
R. Schwabe, C.H.R. Senges, J.E. Bandow, T. Heine, H. Lehmann, O. Wiche, M. Schlömann, G. Levicán, D. Tischler, Cultivation dependent formation of siderophores by Gordonia rubripertincta CWB2 (2020) Microbiol. Res. DOI: 10.1016/j.micres.2020.126481
R. Schwabe, C.H.R. Senges, J.E. Bandow, T. Heine, H. Lehmann, O. Wiche, M. Schlömann, G. Levicán, D. Tischler, Data on metal-chelating, -immobilisation and biosorption properties by Gordonia rubripertincta CWB2 in dependency on rare earth adaptation (2020) Data in Brief DOI: 10.1016/j.dib.2020.105739
M. Hofmann, J.S. Martin del Campo, P. Sobrado, D. Tischler, Biosynthesis of desferrioxamine siderophores initiated by decarboxylases: A functional investigation of two lysine/ornithine-decarboxylases from Gordonia rubripertincta CWB2 and Pimelobacter simplex 3E (2020) Arch. Biochem. Biophys. DOI: 10.1016/j.abb.2020.108429
M.J.C. Espinosa, A.C. Blanco, T. Schmidgall, A.K. Atanasoff-Kardjalieff, U. Kappelmeyer, D. Tischler, D.H. Pieper, H.J. Heipieper, C. Eberlein, Toward biorecycling: isolation of a soil bacterium that grows on a polyurethane oligomer and monomer (2020) Front. Microbiol. DOI 10.3389/fmicb.2020.00404
S. Kumaran, A.C.R. Ngo, F.P.J. Schultes, D. Tischler, Draft genome sequence of Kocuria indica DP-K7, a methyl red degrading actinobacterium (2020) 3 Biotech DOI: 10.1007/s13205-020-2136-3
D. Tischler, E. Gädke, D. Eggerichs, A. Gomez Baraibar, C. Mügge, A. Scholtissek, C.E. Paul, Asymmetric reduction of (R)-carvone through a thermostable and organic-solvent-tolerant ene-reductase (2020) ChemBioChem DOI: 10.1002/cbic.201900599
C. Willrodt, J.A.D. Gröning, P. Nerke, R. Koch, A. Scholtissek, T. Heine, A. Schmid, B. Bühler, D. Tischler, Highly efficient access to (S)-sulfoxides utilizing a promiscuous flavoprotein monooxygenase in a whole-cell biocatalyst format (2020) ChemCatChem DOI: 10.1002/cctc.201901894
M. Hofmann, T. Heine, V. Schulz, S. Hofmann, D. Tischler, Draft genomes and initial characterization of siderophore producing pseudomonads isolated from mine dump and mine drainage (2020) Biotechnol. Rep. DOI: 10.1016/j.btre.2019.e00403
T. Heine, A. Scholtissek, S. Hofmann, R. Koch, D. Tischler, Accessing enantiopure epoxides and sulfoxides: Related flavin-dependent monooxygenases provide reversed enantioselectivity (2020) ChemCatChem DOI: 10.1002/cctc.201901353
A.C. Lienkamp, T. Heine, D. Tischler, Glutathione: A powerful but rare cofactor among Actinobacteria (2020) Adv. Appl. Microbiol. DOI: 10.1016/bs.aambs.2019.12.003
2019
L. Mestrom, M. Przypis, D. Kowalczykiewicz, A. Pollender, A. Kumpf, I. Bento, A. Jarzebski, K. Szymańska, A. Chruściel, D. Tischler, R. Schoevaart, P.-L. Hagedoorn, U. Hanefeld, Leloir glycosyltransferases in applied biocatalysis: A multidisciplinary approach (2019) Int. J. Mol. Sci. DOI: 10.3390/ijms20215263
A. Kumpf, A. Partzsch, A. Pollender, I. Bento, D. Tischler, Two homologous enzymes of the GalU family in Rhodococcus opacus 1CP – RoGalU1 and RoGalU2 (2019) Int. J. Mol. Sci. DOI: 10.3390/ijms20225809
D. Eggerichs, A.C. Lienkamp, T. Heine, C. Mügge, D. Tischler, Chiral epoxidation of aryl-alkyl ethers from lignin (Chirale Epoxidierung von Aryl-Alkyl-Ethern aus Lignin) (2019) BIOspektrum DOI: 10.1007/s12268-019-0219-7
R. Schwabe, B. Obst, M. Mehnert, D. Tischler, O. Wiche, Influence of pH and presence of bacterial siderophores on the mobilization of trace elements in soil extracts (Mobilisierung von Spurenelementen in Bodenextrakten durch bakterielle Siderophore in Abhängigkeit des pH-Wertes) (2019) F. Ecol. Online
D.N. Proença, T. Heine, C.H. Senges, J.E. Bandow, P.V. Morais, D. Tischler, Bacterial metabolites produced under iron limitation kill pinewood nematode and attract Caenorhabditis elegans (2019) Front. Microbiol. DOI: 10.3389/fmicb.2019.02166
D. Tischler, W.J.H van Berkel, M.W. Fraaije, Actinobacteria, a source of biocatalytic tools (2019) Front. Microbiol.: DOI: 10.3389/fmicb.2019.00800
T. Heine, C. Großmann, S. Hofmann, D. Tischler, Indigoid dyes by group E monooxygenases: mechanism and biocatalysis (2019) Biol. Chem.: DOI: 10.1515/hsz-2019-0109
J. Enoki, M. Linhorst, F. Busch, A. Gomez-Baraibar, K. Miyamoto, R. Kourist, C. Mügge, Preparation of optically pure flurbiprofen via an integrated chemo-enzymatic synthesis pathway (2019) Mol. Catal.: DOI: 10.1016/j.mcat.2019.01.024
J. Enoki, C. Mügge, D. Tischler, K. Miyamoto, R. Kourist, Chemoenzymatic cascade synthesis of optically pure alkanoic acids using engineered arylmalonate decarboxylase variants (2019) Chem. Eur. J.: DOI: 10.1002/chem.201806339
2018
A.H. Westphal, D. Tischler, F. Heinke, S. Hofmann, J.A.D. Gröning, D. Labudde, W.J.H. van Berkel, Pyridine Nucleotide Coenzyme Specificity of p-Hydroxybenzoate Hydroxylase and Related Flavoprotein Monooxygenases (2018) Front. Microbiol.: DOI: 10.3389/fmicb.2018.03050
R. Schwabe, M.K. Anke, K. Szymańska, O. Wiche, D. Tischler, Analysis of desferrioxamine-like siderophores and their capability to selectively bind metals and metalloids: development of a robust analytical RP-HPLC method (2018) Res. Microbiol.: DOI: 10.1016/j.resmic.2018.08.002.
A. Scholtissek, E. Gädke, C.E. Paul, A.H. Westphal, W.J.H. van Berkel, D. Tischler, Catalytic performance of a class III Old yellow enzyme and its cysteine variants (2018) Front. Microbiol.: DOI: 10.3389/fmicb.2018.02410.
J. Trögl, C.O. Esuola, S. Kříženecká, P. Kuráň, L. Seidlová, P. Veronesi-Dáňová, J. Popelka, O.O. Babalola, P. Hrabák, M. Czinnerová, E. Kakosová, A. Ševců, D. Tischler, Biodegradation of high concentrations of aliphatic hydrocarbons in soil from a petroleum refinery: Implications for applicability of new actinobacterial strains (2018) Appl. Sci.: DOI: 10.3390/app8101855.
T. Heine, W.J.H. van Berkel, G.T. Gassner, K.H. van Pée, D. Tischler, Two-component fad-dependent monooxygenases: Current knowledge and biotechnological opportunities (2018) Biology: DOI: 10.3390/biology7030042.
G. Retamal-Morales, T. Heine, J.S. Tischler, B. Erler, J.A.D. Gröning, S.R. Kaschabek, M. Schlömann, G. Levicán, D. Tischler, Draft genome sequence of Rhodococcus erythropolis B7g, a biosurfactant producing actinobacterium (2018) J. Biotechnol.: DOI: 10.1016/j.jbiotec.2018.06.001.
T. Heine, C. Großmann, S. Hofmann, D. Tischler, Enzymgesteuerte Indigoproduktion (2018) BioSpektrum: DOI: 10.1007/s12268-018-0938-1
T. Heine, J. Zimmerling, A. Ballmann, S.B. Kleeberg, C. Rückert, T. Busche, A. Winkler, J. Kalinowski, A. Poetsch, A. Scholtissek, M. Oelschlägel, G. Schmidt, D. Tischler, On the enigma of glutathione-dependent styrene degradation in Gordonia rubripertincta CWB2 (2018) Appl. Environ. Microbiol.: DOI: 10.1128/AEM.00154-18.
G. Retamal-Morales, M. Mehnert, R. Schwabe, D. Tischler, M. Schlömann, G. Levicán, Detection of arsenic-binding siderophores in arsenic-tolerating Actinobacteria by a modified CAS assay (2018) Ecotoxicol. Environ. Saf.: DOI: 10.1016/j.ecoenv.2018.03.087
M. Oelschlägel, J. Zimmerling, D. Tischler, A review: The styrene metabolizing cascade of side-chain oxygenation as biotechnological basis to gain various valuable compounds (2018) Front. Microbiol.: DOI: 10.3389/fmicb.2018.00490
D. Tischler, R. Schwabe, L. Siegel, A. Scholtissek, T. Heine, VpStyA1/VpStyA2B of variovorax paradoxus EPS: An aryl alkyl sulfoxidase rather than a styrene epoxidizing monooxygenase (2018) Molecules: DOI: 10.3390/molecules23040809
Veröffentlichungen der Nachwuchgruppe ChemBioCat unter der Leitung von Professor Kourist
2017
S. Bojarra, D. Reichert, M. Grote, A. Gómez-Baraibar, A. Dennig, B. Nidetzky, C. Mügge, R. Kourist, Bio‐based α,ω‐Functionalized Hydrocarbons from Multi‐step Reaction Sequences with Bio‐ and Metallo‐catalysts Based on the Fatty Acid Decarboxylase OleTJE (2017) ChemCatChem: DOI: 10.1002/cctc.201701804
S. Böhmer, K. Köninger, A. Gómez-Baraibar, S. Bojarra, C. Mügge, S. Schmidt, M. Nowaczyk, R. Kourist, Enzymatic Oxyfunctionalization Driven by Photosynthetic Water-Splitting in the Cyanobacterium Synechocystis sp. PCC 6803 (2017) Catalysts: DOI: 10.3390/catal7080240
M. Aßmann, C. Mügge, S. Gaßmeyer, J. Enoki, L. Hilterhaus, R. Kourist, A. Liese, S. Kara, Improvement of the Process Stability of Arylmalonate Decarboyxlase by Immobilization for Biocatalytic Profen Synthesis (2017) Front. Microbiol.: DOI: 10.3389/fmicb.2017.00448
2016
A. Gómez-Baraibar, D. Reichert, C. Mügge, S. Seger, H. Gröger and R. Kourist, A sequential one-pot cascade reaction combining an encapsulated decarboxylase with metathesis for the synthesis of bio-based antioxidants (2016) Ang. Chem., Int. Ed.: DOI: 10.1002/anie.201607777
J. Enoki, J. Meisborn, A. Müller and R. Kourist, A multi-enzymatic cascade reaction for the stereoselective production of γ-oxyfunctionalyzed amino acids (2016) Front. Microbiol.: DOI: 10.3389/fmicb.2016.00425.
K. Köninger, A. Gómez-Baraibar, C. Mügge, C. Paul., F. Hollmann, M. Nowaczyk and R. Kourist, Recombinant cyanobacteria as tools for asymmetric C=C bond reduction fueled by biocatalytic water oxidation (2016) Ang. Chem., Int. Ed.: DOI: 10.1002/anie.201601200/full
F. Busch, N. Hülsemann, J. Enoki, K. Miyamoto, M. Bocola and R. Kourist, Semiempirical QM/MM calculations reveal a step-wise proton transfer and an unusual thiolate pocket in the mechanism of the racemizing mutant G74C of arylmalonate decarboxylase (2016) Catalysis Science & Technology: DOI: 10.1039/C5CY01964H
S. K. Gaßmeyer, J. Wetzig, C. Mügge, M. Assmann, J. Enoki, L. Hilterhaus, R. Zuhse, K. Miyamoto, A. Liese and R. Kourist, Arylmalonate decarboxylase-catalyzed asymmetric synthesis of both enantiomers of optically pure flurbiprofen (2015) ChemCatChem: DOI: 10.1002/cctc.201501205.
2015
S. K. Gaßmeyer, H. Yoshikawa, J. Enoki, N. Hülsemann, R. Stoll, K. Miyamoto and R. Kourist, STD-NMR based protein engineering of the unique arylpropionate-racemase AMDase G74C (2015), ChemBioChem, 16, 1943-1949.
S. Yoshida, J. Enoki, R. Kourist, K. Miyamoto, Engineered hydrophobic pocket of (S)-selective arylmalonate decarboxylase variant by simultaneous saturation mutagenesis to improve catalytic performance (2015) Bioscience, Biotechnology and Biochemistry, doi: 10.1080/09168451.2015.1060844.
S. Yoshida, J. Enoki, R. Hemmi, R. Kourist, N. Kawakami, and K. Miyamoto, Draft genome sequence of Bordetella bronchiseptica KU1201, the first isolation source of arylmalonate decarboxylase (2015) Genome Announcements, 3, e00373-15.
