메뉴 건너뛰기




Volumn 3, Issue , 2016, Pages 120-129

Development of a plasmid-based expression system in Clostridium thermocellum and its use to screen heterologous expression of bifunctional alcohol dehydrogenases (adhEs)

Author keywords

adhE; Clostridium Thermocellum; Gene expression; Plasmid; Structural stability

Indexed keywords

ALCOHOL DEHYDROGENASE; ALDEHYDE;

EID: 84997226657     PISSN: None     EISSN: 22140301     Source Type: Journal    
DOI: 10.1016/j.meteno.2016.04.001     Document Type: Article
Times cited : (19)

References (39)
  • 2
    • 33747775622 scopus 로고    scopus 로고
    • Enzyme assays
    • Wiley-Blackwell Weinheim, Germany ⟨⟩
    • Bisswanger, H., Enzyme assays. Practical Enzymology, 2011, Wiley-Blackwell, Weinheim, Germany, 101–103 ⟨ http://dx.doi.org/10.1016/0958-1669(91)90057-C⟩.
    • (2011) Practical Enzymology , pp. 101-103
    • Bisswanger, H.1
  • 3
    • 84895533735 scopus 로고    scopus 로고
    • Increase in ethanol yield via elimination of lactate production in an ethanol-tolerant mutant of Clostridium thermocellum
    • Biswas, R., Prabhu, S., Lynd, L.R., Guss, A.M., Increase in ethanol yield via elimination of lactate production in an ethanol-tolerant mutant of Clostridium thermocellum. PLoS One 9 (2014), 1–7, 10.1371/journal.pone.0086389.
    • (2014) PLoS One , vol.9 , pp. 1-7
    • Biswas, R.1    Prabhu, S.2    Lynd, L.R.3    Guss, A.M.4
  • 5
    • 0024474533 scopus 로고
    • Replication Origins Of Single-stranded-DNA plasmid pUB110
    • Boe, L., Gros, M.-F., Te Riele, H., Ehrlich, S.D., Gruss, A., Replication Origins Of Single-stranded-DNA plasmid pUB110. J. Bacteriol. 171 (1989), 3366–3372.
    • (1989) J. Bacteriol. , vol.171 , pp. 3366-3372
    • Boe, L.1    Gros, M.-F.2    Te Riele, H.3    Ehrlich, S.D.4    Gruss, A.5
  • 6
    • 0025778362 scopus 로고
    • Plasmid deletion formation between short direct repeats in Bacillus subtilis is stimulated by single-stranded rolling-circle replication intermediates
    • Bron, S., Holsappel, S., Venema, G., Peeters, B.P.H., Plasmid deletion formation between short direct repeats in Bacillus subtilis is stimulated by single-stranded rolling-circle replication intermediates. Mol. Gen. Genet. 226 (1991), 88–96, 10.1007/BF00273591.
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 88-96
    • Bron, S.1    Holsappel, S.2    Venema, G.3    Peeters, B.P.H.4
  • 8
    • 84871402263 scopus 로고    scopus 로고
    • Redirecting carbon flux through exogenous pyruvate kinase to achieve high ethanol yields in Clostridium thermocellum
    • Deng, Y., Olson, D.G., Zhou, J., Herring, C.D., Shaw, A.J., Lynd, L.R., Redirecting carbon flux through exogenous pyruvate kinase to achieve high ethanol yields in Clostridium thermocellum. Metab. Eng. 15 (2013), 151–158, 10.1016/j.ymben.2012.11.006.
    • (2013) Metab. Eng. , vol.15 , pp. 151-158
    • Deng, Y.1    Olson, D.G.2    Zhou, J.3    Herring, C.D.4    Shaw, A.J.5    Lynd, L.R.6
  • 9
    • 79961096901 scopus 로고    scopus 로고
    • Proteomic characterization of cellular and molecular processes that enable the Nanoarchaeum equitans-ignicoccus hospitalis relationship
    • Giannone, R.J., Huber, H., Karpinets, T., Heimerl, T., Küper, U., Rachel, R., Keller, M., Hettich, R.L., Podar, M., Proteomic characterization of cellular and molecular processes that enable the Nanoarchaeum equitans-ignicoccus hospitalis relationship. PLoS One, 6, 2011, e22942, 10.1371/journal.pone.0022942.
    • (2011) PLoS One , vol.6 , pp. e22942
    • Giannone, R.J.1    Huber, H.2    Karpinets, T.3    Heimerl, T.4    Küper, U.5    Rachel, R.6    Keller, M.7    Hettich, R.L.8    Podar, M.9
  • 10
    • 84938630861 scopus 로고    scopus 로고
    • Rescuing those left behind: recovering and characterizing underdigested membrane and hydrophobic proteins to enhance proteome measurement depth
    • Giannone, R.J., Wurch, L.L., Podar, M., Hettich, R.L., Rescuing those left behind: recovering and characterizing underdigested membrane and hydrophobic proteins to enhance proteome measurement depth. Anal. Chem., 2015, 10.1021/acs.analchem.5b01187.
    • (2015) Anal. Chem.
    • Giannone, R.J.1    Wurch, L.L.2    Podar, M.3    Hettich, R.L.4
  • 11
    • 79957471219 scopus 로고    scopus 로고
    • Enzymatic assembly of overlapping DNA fragments
    • Gibson, D.G., Enzymatic assembly of overlapping DNA fragments. Methods Enzymol. 498 (2011), 349–361, 10.1016/B978–0-12–385120–8.00015–2.
    • (2011) Methods Enzymol. , vol.498 , pp. 349-361
    • Gibson, D.G.1
  • 12
    • 84872191690 scopus 로고    scopus 로고
    • Dcm methylation is detrimental to plasmid transformation in Clostridium thermocellum
    • Guss, A.M., Olson, D.G., Caiazza, N.C., Lynd, L.R., Dcm methylation is detrimental to plasmid transformation in Clostridium thermocellum. Biotechnol. Biofuels, 5, 2012, 30, 10.1186/1754–6834–5-30.
    • (2012) Biotechnol. Biofuels , vol.5 , pp. 30
    • Guss, A.M.1    Olson, D.G.2    Caiazza, N.C.3    Lynd, L.R.4
  • 14
    • 14544275047 scopus 로고    scopus 로고
    • Plasmid rolling-circle replication: highlights of two decades of research
    • Khan, S.A., Plasmid rolling-circle replication: highlights of two decades of research. Plasmid 53 (2005), 126–136, 10.1016/j.plasmid.2004.12.008.
    • (2005) Plasmid , vol.53 , pp. 126-136
    • Khan, S.A.1
  • 17
    • 84924067126 scopus 로고    scopus 로고
    • The bifunctional alcohol and aldehyde dehydrogenase gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
    • Lo, J., Zheng, T., Hon, S., Olson, D.G., Lynd, L.R., The bifunctional alcohol and aldehyde dehydrogenase gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum. J. Bacteriol. 197 (2015), 1386–1393, 10.1128/JB.02450–14.
    • (2015) J. Bacteriol. , vol.197 , pp. 1386-1393
    • Lo, J.1    Zheng, T.2    Hon, S.3    Olson, D.G.4    Lynd, L.R.5
  • 18
    • 0036714783 scopus 로고    scopus 로고
    • Microbial cellulose utilization : fundamentals and biotechnology
    • Lynd, L.R., Weimer, P.J., Zyl, W.H., Van, Pretorius, I.S., Microbial cellulose utilization : fundamentals and biotechnology. Microbiol. Mol. Biol. Rev. 66 (2002), 506–577, 10.1128/MMBR.66.3.506.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 506-577
    • Lynd, L.R.1    Weimer, P.J.2    Zyl, W.H.3    Van, Pretorius, I.S.4
  • 20
    • 84873530148 scopus 로고    scopus 로고
    • Role of the CipA scaffoldin protein in cellulose solubilization, as determined by targeted gene deletion and complementation in Clostridium thermocellum
    • Olson, D.G., Giannone, R.J., Hettich, R.L., Lynd, L.R., Role of the CipA scaffoldin protein in cellulose solubilization, as determined by targeted gene deletion and complementation in Clostridium thermocellum. J. Bacteriol. 195 (2013), 733–739, 10.1128/JB.02014–12.
    • (2013) J. Bacteriol. , vol.195 , pp. 733-739
    • Olson, D.G.1    Giannone, R.J.2    Hettich, R.L.3    Lynd, L.R.4
  • 21
    • 84861156874 scopus 로고    scopus 로고
    • Transformation of Clostridium thermocellum by Electroporation, Methods in Enzymology
    • 1st ed. Elsevier Inc
    • Olson, D.G., Lynd, L.R., Transformation of Clostridium thermocellum by Electroporation, Methods in Enzymology. 1st ed., 2012, Elsevier Inc, 10.1016/B978–0-12–415931–0.00017–3.
    • (2012)
    • Olson, D.G.1    Lynd, L.R.2
  • 22
    • 84860791422 scopus 로고    scopus 로고
    • Computational design and characterization of a temperature-sensitive plasmid replicon for gram positive thermophiles
    • Olson, D.G., Lynd, L.R., Computational design and characterization of a temperature-sensitive plasmid replicon for gram positive thermophiles. J. Biol. Eng., 2012, 6, 10.1186/1754–1611–6-5.
    • (2012) J. Biol. Eng. , pp. 6
    • Olson, D.G.1    Lynd, L.R.2
  • 23
  • 27
    • 84942612938 scopus 로고    scopus 로고
    • Elimination of metabolic pathways to all traditional fermentation products increases ethanol yields in Clostridium thermocellum
    • Papanek, B., Biswas, R., Rydzak, T., Guss, A.M., Elimination of metabolic pathways to all traditional fermentation products increases ethanol yields in Clostridium thermocellum. Metab. Eng., 2015, 1–6, 10.1016/j.ymben.2015.09.002.
    • (2015) Metab. Eng. , pp. 1-6
    • Papanek, B.1    Biswas, R.2    Rydzak, T.3    Guss, A.M.4
  • 28
    • 84939139436 scopus 로고    scopus 로고
    • Elimination of formate production in Clostridium thermocellum
    • Rydzak, T., Lynd, L.R., Guss, A.M., Elimination of formate production in Clostridium thermocellum. J. Ind. Microbiol. Biotechnol., 2015, 10.1007/s10295–015–1644–3.
    • (2015) J. Ind. Microbiol. Biotechnol.
    • Rydzak, T.1    Lynd, L.R.2    Guss, A.M.3
  • 29
    • 84866481432 scopus 로고    scopus 로고
    • Proteomic analysis of Clostridium thermocellum core metabolism: relative protein expression profiles and growth phase-dependent changes in protein expression
    • Rydzak, T., McQueen, P.D., Krokhin, O.V., Spicer, V., Ezzati, P., Dwivedi, R.C., Shamshurin, D., Levin, D.B., Wilkins, J.A., Sparling, R., Proteomic analysis of Clostridium thermocellum core metabolism: relative protein expression profiles and growth phase-dependent changes in protein expression. BMC Microbiol., 12, 2012, 214, 10.1186/1471–2180–12–214.
    • (2012) BMC Microbiol. , vol.12 , pp. 214
    • Rydzak, T.1    McQueen, P.D.2    Krokhin, O.V.3    Spicer, V.4    Ezzati, P.5    Dwivedi, R.C.6    Shamshurin, D.7    Levin, D.B.8    Wilkins, J.A.9    Sparling, R.10
  • 30
    • 84865597185 scopus 로고    scopus 로고
    • Urease expression in a Thermoanaerobacterium saccharolyticum ethanologen allows high titer ethanol production
    • Shaw, A.J., Covalla, S.F., Miller, B.B., Firliet, B.T., Hogsett, D.A., Herring, C.D., Urease expression in a Thermoanaerobacterium saccharolyticum ethanologen allows high titer ethanol production. Metab. Eng. 14 (2012), 528–532, 10.1016/j.ymben.2012.06.004.
    • (2012) Metab. Eng. , vol.14 , pp. 528-532
    • Shaw, A.J.1    Covalla, S.F.2    Miller, B.B.3    Firliet, B.T.4    Hogsett, D.A.5    Herring, C.D.6
  • 31
    • 41149141711 scopus 로고    scopus 로고
    • End-product pathways in the xylose fermenting bacterium Thermoanaerobacterium saccharolyticum
    • Shaw, A.J., Jenney, F.E., Adams, M.W.W., Lynd, L.R., End-product pathways in the xylose fermenting bacterium Thermoanaerobacterium saccharolyticum. Enzym. Microb. Technol. 42 (2008), 453–458, 10.1016/j.enzmictec.2008.01.005.
    • (2008) Enzym. Microb. Technol. , vol.42 , pp. 453-458
    • Shaw, A.J.1    Jenney, F.E.2    Adams, M.W.W.3    Lynd, L.R.4
  • 33
    • 33847401893 scopus 로고    scopus 로고
    • MyriMatch: highly accurate tandem mass spectral peptide identificaiton by multivariate hypergeometric analysis
    • Tabb, D.L., Fernando, C.G., Chambers, M.C., MyriMatch: highly accurate tandem mass spectral peptide identificaiton by multivariate hypergeometric analysis. J. Proteome Res. 6 (2008), 654–661, 10.1021/pr0604054.MyriMatch.
    • (2008) J. Proteome Res. , vol.6 , pp. 654-661
    • Tabb, D.L.1    Fernando, C.G.2    Chambers, M.C.3
  • 37
    • 0037439184 scopus 로고    scopus 로고
    • Quantification of cell and cellulase mass concentrations during anaerobic cellulose fermentation: Development of an enzyme-linked immunosorbent assay-based method with application to Clostridium thermocellum batch cultures
    • Zhang, Y., Lynd, L.R., Quantification of cell and cellulase mass concentrations during anaerobic cellulose fermentation: Development of an enzyme-linked immunosorbent assay-based method with application to Clostridium thermocellum batch cultures. Anal. Chem. 75 (2003), 219–227, 10.1021/ac020271n.
    • (2003) Anal. Chem. , vol.75 , pp. 219-227
    • Zhang, Y.1    Lynd, L.R.2
  • 38
    • 84936991306 scopus 로고    scopus 로고
    • Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutants of Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
    • Zheng, T., Olson, D.G., Tian, L., Bomble, Y.J., Himmel, M.E., Lo, J., Hon, S., Shaw, A.J., van Dijken, J.P., Lynd, L.R., Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutants of Clostridium thermocellum and Thermoanaerobacterium saccharolyticum. J. Bacteriol. 197 (2015), 2610–2619, 10.1128/JB.00232–15.
    • (2015) J. Bacteriol. , vol.197 , pp. 2610-2619
    • Zheng, T.1    Olson, D.G.2    Tian, L.3    Bomble, Y.J.4    Himmel, M.E.5    Lo, J.6    Hon, S.7    Shaw, A.J.8    van Dijken, J.P.9    Lynd, L.R.10
  • 39
    • 84941563834 scopus 로고    scopus 로고
    • Physiological roles of pyruvate ferredoxin oxidoreductase and pyruvate formate-lyase in Thermoanaerobacterium saccharolyticum JW/SL-YS485
    • Zhou, J., Olson, D.G., Lanahan, A.A., Tian, L., Murphy, S.J.-L., Lo, J., Lynd, L.R., Physiological roles of pyruvate ferredoxin oxidoreductase and pyruvate formate-lyase in Thermoanaerobacterium saccharolyticum JW/SL-YS485. Biotechnol. Biofuels, 8, 2015, 138, 10.1186/s13068–015–0304–1.
    • (2015) Biotechnol. Biofuels , vol.8 , pp. 138
    • Zhou, J.1    Olson, D.G.2    Lanahan, A.A.3    Tian, L.4    Murphy, S.J.-L.5    Lo, J.6    Lynd, L.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.