메뉴 건너뛰기




Volumn 80, Issue 10, 2014, Pages 2973-2980

Adaptation of the wine bacterium oenococcus oeni to ethanol stress: Role of the small heat shock protein lo18 in membrane integrity

Author keywords

[No Author keywords available]

Indexed keywords

BACILLI; EXPERIMENTS; FLUIDIZATION; LIPID BILAYERS; LIPOSOMES; MEMBRANES; PHOSPHOLIPIDS; PROTEINS; WINE;

EID: 84899066757     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.04178-13     Document Type: Article
Times cited : (56)

References (47)
  • 1
    • 0032846740 scopus 로고    scopus 로고
    • Lactic acid bacteria in the quality improvement and depreciation of wine
    • Lonvaud-Funel A. 1999. Lactic acid bacteria in the quality improvement and depreciation of wine. Antonie Van Leeuwenhoek 76:317-331. http://dx.doi.org/10.1023/A:1002088931106.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 317-331
    • Lonvaud-Funel, A.1
  • 2
    • 0028113809 scopus 로고
    • Induction of stress proteins in Leuconostoc oenos to perform direct inoculation of wine
    • Guzzo J, Cavin J, Divies C. 1994. Induction of stress proteins in Leuconostoc oenos to perform direct inoculation of wine. Biotechnol. Lett. 16: 1189-1194. http://dx.doi.org/10.1007/BF01020849.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 1189-1194
    • Guzzo, J.1    Cavin, J.2    Divies, C.3
  • 3
    • 0030978775 scopus 로고    scopus 로고
    • A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase
    • Guzzo J, Delmas F, Pierre F, Jobin M, Samyn B, Van Beeumen J, Cavin J, Divies C. 1997. A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase. Lett. Appl. Microbiol. 24:393-396. http://dx.doi.org/10.1046/j.1472-765X.1997.00042.x.
    • (1997) Lett. Appl. Microbiol. , vol.24 , pp. 393-396
    • Guzzo, J.1    Delmas, F.2    Pierre, F.3    Jobin, M.4    Samyn, B.5    Van Beeumen, J.6    Cavin, J.7    Divies, C.8
  • 4
    • 0032032195 scopus 로고    scopus 로고
    • Increase of sulfite tolerance in Oenococcus oeni by means of acidic adaptation
    • Guzzo J, Jobin M, Diviés C. 1998. Increase of sulfite tolerance in Oenococcus oeni by means of acidic adaptation. FEMS Microbiol. Lett. 160:43-47. http://dx.doi.org/10.1111/j.1574-6968.1998.tb12888.x.
    • (1998) FEMS Microbiol. Lett. , vol.160 , pp. 43-47
    • Guzzo, J.1    Jobin, M.2    Diviés, C.3
  • 5
    • 0030942271 scopus 로고    scopus 로고
    • Molecular characterization of the gene encoding an 18-kilodalton small heat shock protein associated with the membrane of Leuconostoc oenos
    • Jobin M, Delmas F, Garmyn D, Divies C, Guzzo J. 1997. Molecular characterization of the gene encoding an 18-kilodalton small heat shock protein associated with the membrane of Leuconostoc oenos. Appl. Environ. Microbiol. 63:609-614.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 609-614
    • Jobin, M.1    Delmas, F.2    Garmyn, D.3    Divies, C.4    Guzzo, J.5
  • 6
    • 0032729809 scopus 로고    scopus 로고
    • The Oenococcus oeni clpX homologue is a heat shock gene preferentially expressed in exponential growth phase
    • Jobin M, Garmyn D, Diviés C, Guzzo J. 1999. The Oenococcus oeni clpX homologue is a heat shock gene preferentially expressed in exponential growth phase. J. Bacteriol. 181:6634-6641.
    • (1999) J. Bacteriol. , vol.181 , pp. 6634-6641
    • Jobin, M.1    Garmyn, D.2    Diviés, C.3    Guzzo, J.4
  • 7
    • 0036053593 scopus 로고    scopus 로고
    • Lactobacillic acid accumulation in the plasma membrane of Oenococcus oeni: a response to ethanol stress?
    • Teixeira H, Goncalves M, Rozes N, Ramos A, San Romao M. 2002. Lactobacillic acid accumulation in the plasma membrane of Oenococcus oeni: a response to ethanol stress? Microb. Ecol. 43:146-153. http://dx.doi.org/10.1007/s00248-001-0036-6.
    • (2002) Microb.Ecol. , vol.43 , pp. 146-153
    • Teixeira, H.1    Goncalves, M.2    Rozes, N.3    Ramos, A.4    San Romao, M.5
  • 8
    • 53449086322 scopus 로고    scopus 로고
    • Changes in membrane lipid composition in ethanol-and acid-adapted Oenococcus oeni cells: characterization of the cfa gene by heterologous complementation
    • Grandvalet C, Assad-Garcia J, Chu-Ky S, Tollot M, Guzzo J, Gresti J, Tourdot-Maréchal R. 2008. Changes in membrane lipid composition in ethanol-and acid-adapted Oenococcus oeni cells: characterization of the cfa gene by heterologous complementation. Microbiology 154:2611-2619. http://dx.doi.org/10.1099/mic.0.2007/016238-0.
    • (2008) Microbiology , vol.154 , pp. 2611-2619
    • Grandvalet, C.1    Assad-Garcia, J.2    Chu-Ky, S.3    Tollot, M.4    Guzzo, J.5    Gresti, J.6    Tourdot-Maréchal, R.7
  • 9
    • 79961043150 scopus 로고    scopus 로고
    • Short-and long-term adaptation to ethanol stress and its cross-protective consequences in Lactobacillus plantarum
    • van Bokhorst-van de Veen H, Abee T, Tempelaars M, Bron P, Kleerebezem M, Marco M. 2011. Short-and long-term adaptation to ethanol stress and its cross-protective consequences in Lactobacillus plantarum. Appl. Environ. Microbiol. 77:5247-5256. http://dx.doi.org/10.1128/AEM.00515-11.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 5247-5256
    • Van Bokhorst-Van De Veen, H.1    Abee, T.2    Tempelaars, M.3    Bron, P.4    Kleerebezem, M.5    Marco, M.6
  • 11
    • 84858286603 scopus 로고    scopus 로고
    • DnaK and GroEL chaperones are recruited to the Bacillus subtilis membrane after short-term ethanol stress
    • Seydlova G, Halada P, Fiser R, Toman O, Ulrych A, Svobodova J. 2012. DnaK and GroEL chaperones are recruited to the Bacillus subtilis membrane after short-term ethanol stress. J. Appl. Microbiol. 112:765-774. http://dx.doi.org/10.1111/j.1365-2672.2012.05238.x.
    • (2012) J. Appl. Microbiol. , vol.112 , pp. 765-774
    • Seydlova, G.1    Halada, P.2    Fiser, R.3    Toman, O.4    Ulrych, A.5    Svobodova, J.6
  • 12
    • 0030903748 scopus 로고    scopus 로고
    • Evidence for a lipochaperonin: association of active protein folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions
    • Torok Z, Horvath I, Goloubinoff P, Kovacs E, Glatz A, Balogh G, Vigh L. 1997. Evidence for a lipochaperonin: association of active protein folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc. Natl. Acad. Sci. U. S. A. 94:2192-2197. http://dx.doi.org/10.1073/pnas.94.6.2192.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2192-2197
    • Torok, Z.1    Horvath, I.2    Goloubinoff, P.3    Kovacs, E.4    Glatz, A.5    Balogh, G.6    Vigh, L.7
  • 13
    • 46149125267 scopus 로고    scopus 로고
    • Membraneassociated stress proteins: more than simply chaperones
    • Horvath I, Multhoff G, Sonnleitner A, Vigh L. 2008. Membraneassociated stress proteins: more than simply chaperones. Biochim. Biophys. Acta 1778:1653-1664. http://dx.doi.org/10.1016/j.bbamem.2008.02.012.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1653-1664
    • Horvath, I.1    Multhoff, G.2    Sonnleitner, A.3    Vigh, L.4
  • 14
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • Nakamoto H, Vigh L. 2007. The small heat shock proteins and their clients. Cell Mol. Life Sci. 64:294-306. http://dx.doi.org/10.1007/s00018-006-6321-2.
    • (2007) Cell Mol. Life Sci. , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vigh, L.2
  • 16
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: molecular structure and chaperone function
    • Sun Y, MacRae T. 2005. Small heat shock proteins: molecular structure and chaperone function. Cell Mol. Life Sci. 62:2460-2476. http://dx.doi.org/10.1007/s00018-005-5190-4.
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.2
  • 17
    • 84860805572 scopus 로고    scopus 로고
    • The oligomer plasticity of the small heat shock protein Lo18 from Oenococcus oeni influences its role in both membrane stabilization and protein protection
    • Maitre M, Weidmann S, Rieu A, Fenel D, Schoehn G, Ebel C, Covés J, Guzzo J. 2012. The oligomer plasticity of the small heat shock protein Lo18 from Oenococcus oeni influences its role in both membrane stabilization and protein protection. Biochem. J. 444:97-104. http://dx.doi.org/10.1042/BJ20120066.
    • (2012) Biochem. J. , vol.444 , pp. 97-104
    • Maitre, M.1    Weidmann, S.2    Rieu, A.3    Fenel, D.4    Schoehn, G.5    Ebel, C.6    Covés, J.7    Guzzo, J.8
  • 18
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network
    • Narberhaus F. 2002. Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev. 66:64-93. http://dx.doi.org/10.1128/MMBR.66.1.64-93.2002.
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 19
    • 0037427451 scopus 로고    scopus 로고
    • Structural and functional defects caused by point mutations in the alpha-crystallin domain of a bacterial alpha-heat shock protein
    • Lentze N, Studer S, Narberhaus F. 2003. Structural and functional defects caused by point mutations in the alpha-crystallin domain of a bacterial alpha-heat shock protein. J. Mol. Biol. 328:927-937. http://dx.doi.org/10.1016/S0022-2836(03)00356-5.
    • (2003) J. Mol. Biol. , vol.328 , pp. 927-937
    • Lentze, N.1    Studer, S.2    Narberhaus, F.3
  • 20
    • 33846523468 scopus 로고    scopus 로고
    • Interaction of mammalian Hsp22 with lipid membranes
    • Chowdary T, Raman B, Ramakrishna T, Rao C. 2007. Interaction of mammalian Hsp22 with lipid membranes. Biochem. J. 401:437-445. http://dx.doi.org/10.1042/BJ20061046.
    • (2007) Biochem. J. , vol.401 , pp. 437-445
    • Chowdary, T.1    Raman, B.2    Ramakrishna, T.3    Rao, C.4
  • 21
    • 53149098981 scopus 로고    scopus 로고
    • A mutant small heat shock protein with increased thylakoid association provides an elevated resistance against UV-B damage in Synechocystis 6803
    • Balogi Z, Cheregi O, Giese K, Juhasz K, Vierling E, Vass I, Vigh L, Horvath I. 2008. A mutant small heat shock protein with increased thylakoid association provides an elevated resistance against UV-B damage in Synechocystis 6803. J. Biol. Chem. 283:22983-22991. http://dx.doi.org/10.1074/jbc.M710400200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22983-22991
    • Balogi, Z.1    Cheregi, O.2    Giese, K.3    Juhasz, K.4    Vierling, E.5    Vass, I.6    Vigh, L.7    Horvath, I.8
  • 22
    • 17044438616 scopus 로고    scopus 로고
    • The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: dissociation of oligomers is a prerequisite. Biochem.
    • Zhang H, Fu X, Jiao W, Zhang X, Liu C, Chang Z. 2005. The association of small heat shock protein Hsp16.3 with the plasma membrane of Mycobacterium tuberculosis: dissociation of oligomers is a prerequisite. Biochem. Biophys. Res. Commun. 330:1055-1061. http://dx.doi.org/10.1016/j.bbrc.2005.03.092.
    • (2005) Biophys. Res. Commun. , vol.330 , pp. 1055-1061
    • Zhang, H.1    Fu, X.2    Jiao, W.3    Zhang, X.4    Liu, C.5    Chang, Z.6
  • 26
    • 32044462709 scopus 로고    scopus 로고
    • A small HSP, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium
    • Coucheney F, Gal L, Beney L, Lherminier J, Gervais P, Guzzo J. 2005. A small HSP, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium. Biochim. Biophys. Acta 1720:92-98. http://dx.doi.org/10.1016/j.bbamem.2005.11.017.
    • (2005) Biochim. Biophys. Acta , vol.1720 , pp. 92-98
    • Coucheney, F.1    Gal, L.2    Beney, L.3    Lherminier, J.4    Gervais, P.5    Guzzo, J.6
  • 27
    • 23644453928 scopus 로고    scopus 로고
    • CtsR is the master regulator of stress response gene expression in Oenococcus oeni
    • Grandvalet C, Coucheney F, Beltramo C, Guzzo J. 2005. CtsR is the master regulator of stress response gene expression in Oenococcus oeni. J. Bacteriol. 187:5614-5623. http://dx.doi.org/10.1128/JB.187.16.5614-5623.2005.
    • (2005) J. Bacteriol. , vol.187 , pp. 5614-5623
    • Grandvalet, C.1    Coucheney, F.2    Beltramo, C.3    Guzzo, J.4
  • 28
    • 77954359475 scopus 로고    scopus 로고
    • Distinct amino acids of the Oenococcus oeni small heat shock protein Lo18 are essential for damaged protein protection and membrane stabilization
    • Weidmann S, Rieu A, Rega M, Coucheney F, Guzzo J. 2010. Distinct amino acids of the Oenococcus oeni small heat shock protein Lo18 are essential for damaged protein protection and membrane stabilization. FEMS Microbiol. Lett. 309:8-15. http://dx.doi.org/10.1111/j.1574-6968.2010.01999.x.
    • (2010) FEMS Microbiol. Lett. , vol.309 , pp. 8-15
    • Weidmann, S.1    Rieu, A.2    Rega, M.3    Coucheney, F.4    Guzzo, J.5
  • 29
    • 0034859278 scopus 로고    scopus 로고
    • Biochemical and physiological studies of the small heat shock protein Lo18 from the lactic acid bacterium Oenococcus oeni
    • Delmas F, Pierre F, Coucheney F, Divies C, Guzzo J. 2001. Biochemical and physiological studies of the small heat shock protein Lo18 from the lactic acid bacterium Oenococcus oeni. J. Mol. Microbiol. Biotechnol. 3:601-610. http://www.horizonpress.com/backlist/jmmb/v/v3/v3n4/13.pdf.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 601-610
    • Delmas, F.1    Pierre, F.2    Coucheney, F.3    Divies, C.4    Guzzo, J.5
  • 30
    • 0000746045 scopus 로고
    • Medium for screening Leuconostoc oenos strains defective in malolactic fermentation
    • Cavin J, Prevost H, Lin J, Schmitt P, Divies C. 1989. Medium for screening Leuconostoc oenos strains defective in malolactic fermentation. Appl. Environ. Microbiol. 55:751-753.
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 751-753
    • Cavin, J.1    Prevost, H.2    Lin, J.3    Schmitt, P.4    Divies, C.5
  • 31
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi B, Sandine W. 1975. Improved medium for lactic streptococci and their bacteriophages. Appl. Microbiol. 29:807-813.
    • (1975) Appl. Microbiol. , vol.29 , pp. 807-813
    • Terzaghi, B.1    Sandine, W.2
  • 32
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E, Dyer W. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917. http://dx.doi.org/10.1139/o59-099.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.1    Dyer, W.2
  • 33
    • 0032901220 scopus 로고    scopus 로고
    • Adaptation of Pseudomonas aeruginosa ATCC 15442 to didecyldimethylammonium bromide induces changes in membrane fatty acid composition and in resistance of cells
    • Méchin L, Dubois-Brissonnet F, Heyd B, Leveau J. 1999. Adaptation of Pseudomonas aeruginosa ATCC 15442 to didecyldimethylammonium bromide induces changes in membrane fatty acid composition and in resistance of cells. J. Appl. Microbiol. 86:859-866. http://dx.doi.org/10.1046/j.1365-2672.1999.00770.x.
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 859-866
    • Méchin, L.1    Dubois-Brissonnet, F.2    Heyd, B.3    Leveau, J.4
  • 34
    • 11844274688 scopus 로고    scopus 로고
    • Determination of an internal control to apply reverse transcription quantitative PCR to study stress response in the lactic acid bacterium Oenococcus oeni
    • Desroche N, Beltramo C, Guzzo J. 2005. Determination of an internal control to apply reverse transcription quantitative PCR to study stress response in the lactic acid bacterium Oenococcus oeni. J. Microbiol. Methods 60:325-333. http://dx.doi.org/10.1016/j.mimet.2004.10.010.
    • (2005) J. Microbiol. Methods , vol.60 , pp. 325-333
    • Desroche, N.1    Beltramo, C.2    Guzzo, J.3
  • 35
    • 0035710746 scopus 로고    scopus 로고
    • ΔΔCT method
    • ΔΔCT method. Methods 25: 402-408. http://dx.doi.org/10.1006/meth.2001.1262.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.1    Schmittgen, T.2
  • 36
    • 0037290306 scopus 로고    scopus 로고
    • Effect of selected environmental and physico-chemical factors on bacterial cytoplasmic membranes
    • Denich T, Beaudette L, Lee H, Trevors J. 2003. Effect of selected environmental and physico-chemical factors on bacterial cytoplasmic membranes. J. Microbiol. Methods 52:149-182. http://dx.doi.org/10.1016/S0167-7012(02)00155-0.
    • (2003) J. Microbiol. Methods , vol.52 , pp. 149-182
    • Denich, T.1    Beaudette, L.2    Lee, H.3    Trevors, J.4
  • 37
    • 79958241187 scopus 로고    scopus 로고
    • Cyclopropanation of membrane unsaturated fatty acids is not essential to the acid stress response of Lactococcus lactis subsp. cremoris
    • To T, Grandvalet C, Tourdot-Maréchal R. 2011. Cyclopropanation of membrane unsaturated fatty acids is not essential to the acid stress response of Lactococcus lactis subsp. cremoris. Appl. Environ. Microbiol. 77:3327-3334. http://dx.doi.org/10.1128/AEM.02518-10.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 3327-3334
    • To, T.1    Grandvalet, C.2    Tourdot-Maréchal, R.3
  • 38
    • 0032584147 scopus 로고    scopus 로고
    • Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a "fluidity gene
    • Horvath I, Glatz A, Varvasovszki V, Torok Z, Pali T, Balogh G, Kovacs E, Nadasdi L, Benko S, Joo F, Vigh L. 1998. Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803: identification of hsp17 as a "fluidity gene." Proc. Natl. Acad. Sci. U. S. A. 95:3513-3518. http://dx.doi.org/10.1073/pnas.95.7.3513.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3513-3518
    • Horvath, I.1    Glatz, A.2    Varvasovszki, V.3    Torok, Z.4    Pali, T.5    Balogh, G.6    Kovacs, E.7    Nadasdi, L.8    Benko, S.9    Joo, F.10    Vigh, L.11
  • 40
    • 34547190663 scopus 로고    scopus 로고
    • Can.the stress protein response be controlled by "membrane-lipid therapy"?
    • Vigh L, Horvath I, Maresca B, Harwood J. 2007. Can. the stress protein response be controlled by "membrane-lipid therapy"? Trends Biochem. Sci. 32:357-363. http://dx.doi.org/10.1016/j.tibs.2007.06.009.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 357-363
    • Vigh, L.1    Horvath, I.2    Maresca, B.3    Harwood, J.4
  • 41
    • 0021360943 scopus 로고
    • Effects of ethanol on the Escherichia coli plasma membrane
    • Dombek K, Ingram L. 1984. Effects of ethanol on the Escherichia coli plasma membrane. J. Bacteriol. 157:233-239.
    • (1984) J. Bacteriol. , vol.157 , pp. 233-239
    • Dombek, K.1    Ingram, L.2
  • 42
    • 0029048826 scopus 로고
    • Mechanisms of membrane toxicity of hydrocarbons
    • Sikkema J, De Bont J, Poolman B. 1995. Mechanisms of membrane toxicity of hydrocarbons. Microbiol. Rev. 59:201-222.
    • (1995) Microbiol. Rev. , vol.59 , pp. 201-222
    • Sikkema, J.1    De Bont, J.2    Poolman, B.3
  • 43
    • 0030606016 scopus 로고    scopus 로고
    • Adaptation mechanisms of microorganisms to the toxic effects of organic solvents on membranes
    • Weber F, De Bont J. 1996. Adaptation mechanisms of microorganisms to the toxic effects of organic solvents on membranes. Biochim. Biophys. Acta 1286:225-245. http://dx.doi.org/10.1016/S0304-4157(96)00010-X.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 225-245
    • Weber, F.1    De Bont, J.2
  • 44
    • 0027291426 scopus 로고
    • Regulation of fatty acid biosynthesis in Escherichia coli
    • Magnuson K, Jackowski S, Rock C, Cronan J, Jr. 1993. Regulation of fatty acid biosynthesis in Escherichia coli. Microbiol. Rev. 57:522-542.
    • (1993) Microbiol. Rev. , vol.57 , pp. 522-542
    • Magnuson, K.1    Jackowski, S.2    Rock, C.3    Cronan, J.4
  • 45
    • 33645051218 scopus 로고    scopus 로고
    • Transcriptional regulation of fatty acid biosynthesis in Streptococcus pneumoniae
    • Lu Y, Rock C. 2006. Transcriptional regulation of fatty acid biosynthesis in Streptococcus pneumoniae. Mol. Microbiol. 59:551-566. http://dx.doi.org/10.1111/j.1365-2958.2005.04951.x.
    • (2006) Mol. Microbiol. , vol.59 , pp. 551-566
    • Lu, Y.1    Rock, C.2
  • 46
    • 0031457094 scopus 로고    scopus 로고
    • Cyclopropane ring formation in membrane lipids of bacteria
    • Grogan D, Cronan J, Jr. 1997. Cyclopropane ring formation in membrane lipids of bacteria. Microbiol. Mol. Biol. Rev. 61:429-441.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 429-441
    • Grogan, D.1    Cronan, J.2
  • 47
    • 0026467088 scopus 로고
    • The conversion of cis into trans unsaturated fatty acids in Pseudomonas putida P8: evidence for a role in the regulation of membrane fluidity
    • Diefenbach R, Heipieper H, Keweloh H. 1992. The conversion of cis into trans unsaturated fatty acids in Pseudomonas putida P8: evidence for a role in the regulation of membrane fluidity. Appl. Microbiol. Biotechnol. 38: 382-387. http://dx.doi.org/10.1007/BF00170090.
    • (1992) Appl. Microbiol. Biotechnol. , vol.38 , pp. 382-387
    • Diefenbach, R.1    Heipieper, H.2    Keweloh, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.