메뉴 건너뛰기




Volumn 194, Issue 5, 2012, Pages 1092-1099

Growth and localization of polyhydroxybutyrate granules in ralstonia eutropha

Author keywords

[No Author keywords available]

Indexed keywords

POLY(3 HYDROXYBUTYRIC ACID);

EID: 84857812606     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06125-11     Document Type: Article
Times cited : (55)

References (57)
  • 1
    • 79951541783 scopus 로고    scopus 로고
    • Fast tomographic reconstruction on multicore computers
    • Agulleiro JI, Fernandez JJ. 2011. Fast tomographic reconstruction on multicore computers. Bioinformatics 27:582-583.
    • (2011) Bioinformatics , vol.27 , pp. 582-583
    • Agulleiro, J.I.1    Fernandez, J.J.2
  • 2
    • 40649105010 scopus 로고    scopus 로고
    • Markov random field based automatic image alignment for electron tomography
    • Amat F, et al. 2008. Markov random field based automatic image alignment for electron tomography. J. Struct. Biol. 161:260-275.
    • (2008) J. Struct. Biol. , vol.161 , pp. 260-275
    • Amat, F.1
  • 3
    • 36549055736 scopus 로고    scopus 로고
    • Polar explorations: recent insights into the polarity of bacterial proteins
    • Bardy SL, Maddock JR. 2007. Polar explorations: recent insights into the polarity of bacterial proteins. Curr. Opin. Microbiol. 10:617-623.
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 617-623
    • Bardy, S.L.1    Maddock, J.R.2
  • 4
    • 58149478360 scopus 로고    scopus 로고
    • Exploiting genomic patterns to discover new supramolecular protein assemblies
    • Beeby M, Bobik TA, Yeates TO. 2009. Exploiting genomic patterns to discover new supramolecular protein assemblies. Protein Sci. 18:69-79.
    • (2009) Protein Sci. , vol.18 , pp. 69-79
    • Beeby, M.1    Bobik, T.A.2    Yeates, T.O.3
  • 5
    • 70350126125 scopus 로고    scopus 로고
    • Universal architecture of bacterial chemoreceptor arrays
    • Briegel A, et al. 2009. Universal architecture of bacterial chemoreceptor arrays. Proc. Natl. Acad. Sci. U. S. A. 106:17181-17186.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 17181-17186
    • Briegel, A.1
  • 6
    • 77957842036 scopus 로고    scopus 로고
    • Elucidation of beta-oxidation pathways in Ralstonia eutropha H16 by examination of global gene expression
    • Brigham CJ, et al. 2010. Elucidation of beta-oxidation pathways in Ralstonia eutropha H16 by examination of global gene expression. J. Bacteriol. 192:5454-5464.
    • (2010) J. Bacteriol. , vol.192 , pp. 5454-5464
    • Brigham, C.J.1
  • 7
    • 79952370252 scopus 로고    scopus 로고
    • Spiral architecture of the nucleoid in Bdellovibrio bacteriovorus
    • Butan C, et al. 2011. Spiral architecture of the nucleoid in Bdellovibrio bacteriovorus. J. Bacteriol. 193:1341-1350.
    • (2011) J. Bacteriol. , vol.193 , pp. 1341-1350
    • Butan, C.1
  • 8
    • 79960620016 scopus 로고    scopus 로고
    • Structural diversity of bacterial flagellar motors
    • Chen S, et al. 2011. Structural diversity of bacterial flagellar motors. EMBO J. 30:2972-2981.
    • (2011) EMBO J. , vol.30 , pp. 2972-2981
    • Chen, S.1
  • 9
    • 33745830137 scopus 로고    scopus 로고
    • Characterization of intact subcellular bodies in whole bacteria by cryo-electron tomography and spectroscopic imaging
    • Comolli L, Kundmann M, Downing K. 2006. Characterization of intact subcellular bodies in whole bacteria by cryo-electron tomography and spectroscopic imaging. J. Microsc. 223:40-52.
    • (2006) J. Microsc. , vol.223 , pp. 40-52
    • Comolli, L.1    Kundmann, M.2    Downing, K.3
  • 10
    • 33947206157 scopus 로고    scopus 로고
    • Synthesis, storage and degradation of neutral lipids in yeast
    • Czabany T, Athenstaedt K, Daum G. 2007. Synthesis, storage and degradation of neutral lipids in yeast. Biochim. Biophys. Acta 1771:299-309.
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 299-309
    • Czabany, T.1    Athenstaedt, K.2    Daum, G.3
  • 11
    • 33845567410 scopus 로고    scopus 로고
    • Detection and characterization of protein aggregates by fluorescence microscopy
    • Demeule B, Gurny R, Arvinte T. 2007. Detection and characterization of protein aggregates by fluorescence microscopy. Int. J. Pharm. 329:37-45.
    • (2007) Int. J. Pharm. , vol.329 , pp. 37-45
    • Demeule, B.1    Gurny, R.2    Arvinte, T.3
  • 12
    • 38749099519 scopus 로고    scopus 로고
    • PhaP is involved in the formation of a network on the surface of polyhydroxyalkanoate inclusions in Cupriavidus necator H16
    • Dennis D, Sein V, Martinez E, Augustine B. 2008. PhaP is involved in the formation of a network on the surface of polyhydroxyalkanoate inclusions in Cupriavidus necator H16. J. Bacteriol. 190:555-563.
    • (2008) J. Bacteriol. , vol.190 , pp. 555-563
    • Dennis, D.1    Sein, V.2    Martinez, E.3    Augustine, B.4
  • 13
    • 78651085417 scopus 로고    scopus 로고
    • Nucleoid-associated PhaF phasin drives intracellular location and segregation of polyhydroxyalkanoate granules in Pseudomonas putida KT2442
    • Galán B, et al. 2011. Nucleoid-associated PhaF phasin drives intracellular location and segregation of polyhydroxyalkanoate granules in Pseudomonas putida KT2442. Mol. Microbiol. 79:402-418.
    • (2011) Mol. Microbiol. , vol.79 , pp. 402-418
    • Galán, B.1
  • 14
    • 0029049968 scopus 로고
    • Enzyme-catalyzed synthesis of poly[(R)-(-)-3-hydroxybutyrate]: formation of macroscopic granules in vitro
    • Gerngross TU, Martin DP. 1995. Enzyme-catalyzed synthesis of poly[(R)-(-)-3-hydroxybutyrate]: formation of macroscopic granules in vitro. Proc. Natl. Acad. Sci. U. S. A. 92:6279-6283.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6279-6283
    • Gerngross, T.U.1    Martin, D.P.2
  • 15
    • 0027297201 scopus 로고
    • Immunocytochemical analysis of poly-beta-hydroxybutyrate (PHB) synthase in Alcaligenes eutrophus H16: localization of the synthase enzyme at the surface of PHB granules
    • Gerngross TU, Reilly P, Stubbe J, Sinskey AJ, Peoples OP. 1993. Immunocytochemical analysis of poly-beta-hydroxybutyrate (PHB) synthase in Alcaligenes eutrophus H16: localization of the synthase enzyme at the surface of PHB granules. J. Bacteriol. 175:5289-5293.
    • (1993) J. Bacteriol. , vol.175 , pp. 5289-5293
    • Gerngross, T.U.1    Reilly, P.2    Stubbe, J.3    Sinskey, A.J.4    Peoples, O.P.5
  • 16
    • 0027933456 scopus 로고
    • Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity
    • Gerngross TU, et al. 1994. Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity. Biochemistry 33:9311-9320.
    • (1994) Biochemistry , vol.33 , pp. 9311-9320
    • Gerngross, T.U.1
  • 17
    • 0014340156 scopus 로고
    • Metabolism of poly-betahydroxybutyrate. I. Purification, composition, and properties of native poly-beta-hydroxybutyrate granules from Bacillus megaterium
    • Griebel R, Smith Z, Merrick JM. 1968. Metabolism of poly-betahydroxybutyrate. I. Purification, composition, and properties of native poly-beta-hydroxybutyrate granules from Bacillus megaterium. Biochemistry 7:3676-3681.
    • (1968) Biochemistry , vol.7 , pp. 3676-3681
    • Griebel, R.1    Smith, Z.2    Merrick, J.M.3
  • 18
    • 33845537229 scopus 로고    scopus 로고
    • Microscopical investigation of poly(3-hydroxybutyrate) granule formation in Azotobacter vinelandii
    • Hermawan S, Jendrossek D. 2007. Microscopical investigation of poly(3-hydroxybutyrate) granule formation in Azotobacter vinelandii. FEMS Microbiol. Lett. 266:60-64.
    • (2007) FEMS Microbiol. Lett. , vol.266 , pp. 60-64
    • Hermawan, S.1    Jendrossek, D.2
  • 19
    • 25844446691 scopus 로고    scopus 로고
    • Atomic force microscopic observation of in vitro polymerized poly[(R)-3-hydroxybutyrate]: insight into possible mechanism of granule formation
    • Hiraishi T, et al. 2005. Atomic force microscopic observation of in vitro polymerized poly[(R)-3-hydroxybutyrate]: insight into possible mechanism of granule formation. Biomacromolecules 6:2671-2677.
    • (2005) Biomacromolecules , vol.6 , pp. 2671-2677
    • Hiraishi, T.1
  • 20
    • 0028766335 scopus 로고
    • Amorphous, biomimetic granules of polyhydroxybutyrate: preparation, characterization, and biological implications
    • Horowitz DM, Sanders JKM. 1994. Amorphous, biomimetic granules of polyhydroxybutyrate: preparation, characterization, and biological implications. J. Am. Chem. Soc. 116:2695-2702.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2695-2702
    • Horowitz, D.M.1    Sanders, J.K.M.2
  • 21
    • 16344385988 scopus 로고    scopus 로고
    • Fluorescence microscopical investigation of poly(3-hydroxybutyrate) granule formation in bacteria
    • Jendrossek D. 2005. Fluorescence microscopical investigation of poly(3-hydroxybutyrate) granule formation in bacteria. Biomacromolecules 6:598-603.
    • (2005) Biomacromolecules , vol.6 , pp. 598-603
    • Jendrossek, D.1
  • 22
    • 65549156552 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes)
    • Jendrossek D. 2009. Polyhydroxyalkanoate granules are complex subcellular organelles (carbonosomes). J. Bacteriol. 191:3195-3202.
    • (2009) J. Bacteriol. , vol.191 , pp. 3195-3202
    • Jendrossek, D.1
  • 23
    • 33846404159 scopus 로고    scopus 로고
    • Poly(3-hydroxybutyrate) granules at the early stages of formation are localized close to the cytoplasmic membrane in Caryophanon latum
    • Jendrossek D, Selchow O, Hoppert M. 2007. Poly(3-hydroxybutyrate) granules at the early stages of formation are localized close to the cytoplasmic membrane in Caryophanon latum. Appl. Environ. Microbiol. 73: 586-593.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 586-593
    • Jendrossek, D.1    Selchow, O.2    Hoppert, M.3
  • 24
    • 77952955154 scopus 로고    scopus 로고
    • Polyhydroxyalkanoates: bioplastics with a green agenda
    • Keshavarz T, Roy I. 2010. Polyhydroxyalkanoates: bioplastics with a green agenda. Curr. Opin. Microbiol. 13:321-326.
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 321-326
    • Keshavarz, T.1    Roy, I.2
  • 25
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili A, Li Z, Newman DK, Jensen GJ. 2006. Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311:242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 26
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of three-dimensional image data using IMOD
    • Kremer J, Mastronarde D, McIntosh J. 1996. Computer visualization of three-dimensional image data using IMOD. J. Struct. Biol. 116:71-76.
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.1    Mastronarde, D.2    McIntosh, J.3
  • 27
    • 27644482690 scopus 로고    scopus 로고
    • Transcriptional analysis of Ralstonia eutropha genes related to poly-(R)-3-hydroxybutyrate homeostasis during batch fermentation
    • Lawrence AG, et al. 2005. Transcriptional analysis of Ralstonia eutropha genes related to poly-(R)-3-hydroxybutyrate homeostasis during batch fermentation. Appl. Microbiol. Biotechnol. 68:663-672.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 663-672
    • Lawrence, A.G.1
  • 28
    • 66349121016 scopus 로고    scopus 로고
    • Electron cryotomography: a new view into microbial ultrastructure
    • Li Z, Jensen GJ. 2009. Electron cryotomography: a new view into microbial ultrastructure. Curr. Opin. Microbiol. 12:333-340.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 333-340
    • Li, Z.1    Jensen, G.J.2
  • 29
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z, Trimble M, Brun Y, Jensen G. 2007. The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J. 26:4694-4708.
    • (2007) EMBO J. , vol.26 , pp. 4694-4708
    • Li, Z.1    Trimble, M.2    Brun, Y.3    Jensen, G.4
  • 30
    • 0030995086 scopus 로고    scopus 로고
    • Determination of the thickness of the boundary layer surrounding bacterial PHA inclusion bodies, and implications for models describing the molecular architecture of this layer
    • Mayer F, Hoppert M. 1997. Determination of the thickness of the boundary layer surrounding bacterial PHA inclusion bodies, and implications for models describing the molecular architecture of this layer. J. Basic Microbiol. 37:45-52.
    • (1997) J. Basic Microbiol. , vol.37 , pp. 45-52
    • Mayer, F.1    Hoppert, M.2
  • 31
    • 41949101592 scopus 로고    scopus 로고
    • Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules
    • Neumann L, et al. 2008. Binding of the major phasin, PhaP1, from Ralstonia eutropha H16 to poly(3-hydroxybutyrate) granules. J. Bacteriol. 190:2911-2919.
    • (2008) J. Bacteriol. , vol.190 , pp. 2911-2919
    • Neumann, L.1
  • 32
    • 0024425823 scopus 로고
    • Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC)
    • 32. Peoples OP, Sinskey AJ. 1989. Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J. Biol. Chem. 264:15298-15303.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15298-15303
    • Peoples, O.P.1    Sinskey, A.J.2
  • 33
    • 35448964302 scopus 로고    scopus 로고
    • The inherent property of polyhydroxyalkanoate synthase to form spherical PHA granules at the cell poles: the core region is required for polar localization
    • Peters V, Becher D, Rehm B. 2007. The inherent property of polyhydroxyalkanoate synthase to form spherical PHA granules at the cell poles: the core region is required for polar localization. J. Biotechnol. 132:238-245.
    • (2007) J. Biotechnol. , vol.132 , pp. 238-245
    • Peters, V.1    Becher, D.2    Rehm, B.3
  • 34
    • 20444498924 scopus 로고    scopus 로고
    • In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases
    • Peters V, Rehm B. 2005. In vivo monitoring of PHA granule formation using GFP-labeled PHA synthases. FEMS Microbiol. Lett. 248:93-100.
    • (2005) FEMS Microbiol. Lett. , vol.248 , pp. 93-100
    • Peters, V.1    Rehm, B.2
  • 35
    • 80053443148 scopus 로고    scopus 로고
    • Interaction between poly(3-hydroxybutyrate) granule-associated proteins as revealed by two-hybrid analysis and identification of a new phasin in Ralstonia eutropha H16
    • Pfeiffer D, Jendrossek D. 2011. Interaction between poly(3-hydroxybutyrate) granule-associated proteins as revealed by two-hybrid analysis and identification of a new phasin in Ralstonia eutropha H16. Microbiology (Reading, Engl.) 157:2795-2807.
    • (2011) Microbiology (Reading, Engl.) , vol.157 , pp. 2795-2807
    • Pfeiffer, D.1    Jendrossek, D.2
  • 36
    • 80855132840 scopus 로고    scopus 로고
    • Identification of a multifunctional protein, PhaM, that determines number, surface to volume ratio, subcellular localization and distribution to daughter cells of poly(3-hydroxybutyrate), PHB, granules in Ralstonia eutropha H16
    • Pfeiffer D, Wahl A, Jendrossek D. 2011. Identification of a multifunctional protein, PhaM, that determines number, surface to volume ratio, subcellular localization and distribution to daughter cells of poly(3-hydroxybutyrate), PHB, granules in Ralstonia eutropha H16. Mol. Microbiol. 82:936-951.
    • (2011) Mol. Microbiol. , vol.82 , pp. 936-951
    • Pfeiffer, D.1    Wahl, A.2    Jendrossek, D.3
  • 38
    • 0036667428 scopus 로고    scopus 로고
    • Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16
    • Pötter M, Madkour M, Mayer F, Steinbüchel A. 2002. Regulation of phasin expression and polyhydroxyalkanoate (PHA) granule formation in Ralstonia eutropha H16. Microbiology (Reading, Engl.) 148:2413-2426.
    • (2002) Microbiology (Reading, Engl.) , vol.148 , pp. 2413-2426
    • Pötter, M.1    Madkour, M.2    Mayer, F.3    Steinbüchel, A.4
  • 39
    • 69549118308 scopus 로고    scopus 로고
    • E. coli transports aggregated proteins to the poles by a specific and energy-dependent process
    • Rokney A, et al. 2009. E. coli transports aggregated proteins to the poles by a specific and energy-dependent process. J. Mol. Biol. 392:589-601.
    • (2009) J. Mol. Biol. , vol.392 , pp. 589-601
    • Rokney, A.1
  • 40
    • 0035190694 scopus 로고    scopus 로고
    • Cloning of an intracellular poly[D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product
    • Saegusa H, Shiraki M, Kanai C, Saito T. 2001. Cloning of an intracellular poly[D(-)-3-hydroxybutyrate] depolymerase gene from Ralstonia eutropha H16 and characterization of the gene product. J. Bacteriol. 183:94-100.
    • (2001) J. Bacteriol. , vol.183 , pp. 94-100
    • Saegusa, H.1    Shiraki, M.2    Kanai, C.3    Saito, T.4
  • 41
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage D, Afonso B, Chen A, Silver P. 2010. Spatially ordered dynamics of the bacterial carbon fixation machinery. Science 327:1258-1261.
    • (2010) Science , vol.327 , pp. 1258-1261
    • Savage, D.1    Afonso, B.2    Chen, A.3    Silver, P.4
  • 42
    • 0028349313 scopus 로고
    • Nuclear magnetic resonance relaxation studies of poly(hydroxybutyrate) in whole cells and in artificial granules
    • Shaw GL, Melby MK, Horowitz DM, Keeler J, Sanders JK. 1994. Nuclear magnetic resonance relaxation studies of poly(hydroxybutyrate) in whole cells and in artificial granules. Int. J. Biol. Macromol. 16:59-63.
    • (1994) Int. J. Biol. Macromol. , vol.16 , pp. 59-63
    • Shaw, G.L.1    Melby, M.K.2    Horowitz, D.M.3    Keeler, J.4    Sanders, J.K.5
  • 43
    • 67650714662 scopus 로고    scopus 로고
    • PHA bioplastic: a value added coproduct for biomass biorefineries
    • Snell KD, Peoples OP. 2009. PHA bioplastic: a value added coproduct for biomass biorefineries. Biofuels Bioproducts Biorefining 3:456-467.
    • (2009) Biofuels Bioproducts Biorefining , vol.3 , pp. 456-467
    • Snell, K.D.1    Peoples, O.P.2
  • 44
    • 0029018968 scopus 로고
    • Diversity of bacterial polyhydroxyalkanoic acids
    • Steinbüchel A, Valentin HE. 1995. Diversity of bacterial polyhydroxyalkanoic acids. FEMS Microbiol. Lett. 128:219-228.
    • (1995) FEMS Microbiol. Lett. , vol.128 , pp. 219-228
    • Steinbüchel, A.1    Valentin, H.E.2
  • 45
    • 0142059593 scopus 로고    scopus 로고
    • Polyhydroxyalkanoate (PHA) homeostasis: the role of PHA synthase
    • Stubbe J, Tian J. 2003. Polyhydroxyalkanoate (PHA) homeostasis: the role of PHA synthase. Nat. Prod. Rep. 20:445-457.
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 445-457
    • Stubbe, J.1    Tian, J.2
  • 46
    • 22244459223 scopus 로고    scopus 로고
    • Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm
    • Stubbe J, et al. 2005. Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm. Annu. Rev. Biochem. 74: 433-480.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 433-480
    • Stubbe, J.1
  • 47
    • 67349173210 scopus 로고    scopus 로고
    • Fully automated, sequential tilt-series acquisition with Leginon
    • Suloway C, et al. 2009. Fully automated, sequential tilt-series acquisition with Leginon. J. Struct. Biol. 167:11-18.
    • (2009) J. Struct. Biol. , vol.167 , pp. 11-18
    • Suloway, C.1
  • 48
    • 18944368050 scopus 로고    scopus 로고
    • Analysis of transient polyhydroxybutyrate production in Wautersia eutropha H16 by quantitative Western analysis and transmission electron microscopy
    • Tian J, et al. 2005. Analysis of transient polyhydroxybutyrate production in Wautersia eutropha H16 by quantitative Western analysis and transmission electron microscopy. J. Bacteriol. 187:3825-3832.
    • (2005) J. Bacteriol. , vol.187 , pp. 3825-3832
    • Tian, J.1
  • 49
    • 20444429432 scopus 로고    scopus 로고
    • Class III polyhydroxybutyrate synthase: involvement in chain termination and reinitiation
    • Tian J, Sinskey AJ, Stubbe J. 2005. Class III polyhydroxybutyrate synthase: involvement in chain termination and reinitiation. Biochemistry 44:8369-8377.
    • (2005) Biochemistry , vol.44 , pp. 8369-8377
    • Tian, J.1    Sinskey, A.J.2    Stubbe, J.3
  • 50
    • 18944405650 scopus 로고    scopus 로고
    • Kinetic studies of polyhydroxybutyrate granule formation in Wautersia eutropha H16 by transmission electron microscopy
    • Tian J, Sinskey A, Stubbe J. 2005. Kinetic studies of polyhydroxybutyrate granule formation in Wautersia eutropha H16 by transmission electron microscopy. J. Bacteriol. 187:3814-3824.
    • (2005) J. Bacteriol. , vol.187 , pp. 3814-3824
    • Tian, J.1    Sinskey, A.2    Stubbe, J.3
  • 52
    • 66049157868 scopus 로고    scopus 로고
    • Quantitative genome-scale analysis of protein localization in an asymmetric bacterium
    • Werner J, et al. 2009. Quantitative genome-scale analysis of protein localization in an asymmetric bacterium. Proc. Natl. Acad. Sci. U. S. A. 106:7858-7863.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 7858-7863
    • Werner, J.1
  • 53
    • 0029039870 scopus 로고
    • Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus
    • Wieczorek R, Pries A, Steinbüchel A, Mayer F. 1995. Analysis of a 24-kilodalton protein associated with the polyhydroxyalkanoic acid granules in Alcaligenes eutrophus. J. Bacteriol. 177:2425-2435.
    • (1995) J. Bacteriol. , vol.177 , pp. 2425-2435
    • Wieczorek, R.1    Pries, A.2    Steinbüchel, A.3    Mayer, F.4
  • 54
    • 0030059466 scopus 로고    scopus 로고
    • Polyhydroxybutyrate synthase: evidence for covalent catalysis
    • Wodzinska J, et al. 1996. Polyhydroxybutyrate synthase: evidence for covalent catalysis. J. Am. Chem. Soc. 118:6319-6320.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6319-6320
    • Wodzinska, J.1
  • 55
    • 0034977798 scopus 로고    scopus 로고
    • Accumulation of the PhaP phasin of Ralstonia eutropha is dependent on production of polyhydroxybutyrate in cells
    • York G, Junker B, Stubbe J, Sinskey A. 2001. Accumulation of the PhaP phasin of Ralstonia eutropha is dependent on production of polyhydroxybutyrate in cells. J. Bacteriol. 183:4217-4226.
    • (2001) J. Bacteriol. , vol.183 , pp. 4217-4226
    • York, G.1    Junker, B.2    Stubbe, J.3    Sinskey, A.4
  • 56
    • 0035078527 scopus 로고    scopus 로고
    • New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrate
    • York G, Stubbe J, Sinskey A. 2001. New insight into the role of the PhaP phasin of Ralstonia eutropha in promoting synthesis of polyhydroxybutyrate. J. Bacteriol. 183:2394-2397.
    • (2001) J. Bacteriol. , vol.183 , pp. 2394-2397
    • York, G.1    Stubbe, J.2    Sinskey, A.3
  • 57
    • 0036136119 scopus 로고    scopus 로고
    • The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production
    • York GM, Stubbe J, Sinskey AJ. 2002. The Ralstonia eutropha PhaR protein couples synthesis of the PhaP phasin to the presence of polyhydroxybutyrate in cells and promotes polyhydroxybutyrate production. J. Bacteriol. 184:59-66.
    • (2002) J. Bacteriol. , vol.184 , pp. 59-66
    • York, G.M.1    Stubbe, J.2    Sinskey, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.