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Volumn 30, Issue 11-12, 2008, Pages 1084-1095

Bacterial microcompartments: Their properties and paradoxes

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE; BACTERIAL ENZYME; BACTERIAL PROTEIN; CARBON DIOXIDE; OXYGEN; POLYPEPTIDE; PROPYLENE GLYCOL; PROTEIN SUBUNIT; PEPTIDE; PROTEIN;

EID: 58149173410     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20830     Document Type: Review
Times cited : (139)

References (97)
  • 1
    • 33645723005 scopus 로고    scopus 로고
    • Polyhedral organelles compartmenting bacterial metabolic processes
    • Bobik TA. 2006. Polyhedral organelles compartmenting bacterial metabolic processes. Appl Microbiol Biotechnol 70:517-525.
    • (2006) Appl Microbiol Biotechnol , vol.70 , pp. 517-525
    • Bobik, T.A.1
  • 2
    • 35448982290 scopus 로고    scopus 로고
    • Bacterial microcompartments
    • Bobik TA. 2007. Bacterial microcompartments. Microbe 2:25-31.
    • (2007) Microbe , vol.2 , pp. 25-31
    • Bobik, T.A.1
  • 4
    • 0042389658 scopus 로고    scopus 로고
    • Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • Havemann GD, Bobik TA. 2003. Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J Bacteriol 185:5086-5095.
    • (2003) J Bacteriol , vol.185 , pp. 5086-5095
    • Havemann, G.D.1    Bobik, T.A.2
  • 5
    • 23244439942 scopus 로고    scopus 로고
    • Protein structures forming the shell of primitive bacterial organelles
    • Kerfeld CA, Sawaya MR, Tanaka S, Nguyen CV, Phillips M, et al. 2005. Protein structures forming the shell of primitive bacterial organelles. Science 309:936-938.
    • (2005) Science , vol.309 , pp. 936-938
    • Kerfeld, C.A.1    Sawaya, M.R.2    Tanaka, S.3    Nguyen, C.V.4    Phillips, M.5
  • 6
    • 0015816557 scopus 로고
    • Functional organelles in prokaryotes: Polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus
    • Shively JM, Ball F, Brown DH, Saunders RE. 1973. Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus. Science 182:584-586.
    • (1973) Science , vol.182 , pp. 584-586
    • Shively, J.M.1    Ball, F.2    Brown, D.H.3    Saunders, R.E.4
  • 7
    • 44649180011 scopus 로고    scopus 로고
    • Advances in understanding the cyanobacterial CO2-concentrating-mechanism (CCM): Functional components, Ci transporters, diversity, genetic regulation and prospects for engineering into plants
    • DOI: 10.1093/jxb/erm112
    • Price GD, Badger MR, Woodger FJ, Long BM. 2007. Advances in understanding the cyanobacterial CO2-concentrating-mechanism (CCM): functional components, Ci transporters, diversity, genetic regulation and prospects for engineering into plants. J Exper Bot Advance accesss DOI: 10.1093/jxb/erm112.
    • (2007) J Exper Bot Advance accesss
    • Price, G.D.1    Badger, M.R.2    Woodger, F.J.3    Long, B.M.4
  • 8
    • 34250968370 scopus 로고
    • Beiträge zur Cytologie der Blaualgen. II. Zentroplasma und18 granulare Einschlüsse von Phormidium uncinatum.
    • Drews G, Niklowitz W. 1956. Beiträge zur Cytologie der Blaualgen. II. Zentroplasma und18 granulare Einschlüsse von Phormidium uncinatum. Arch Mikrobiol 24:147-162.
    • (1956) Arch Mikrobiol , vol.24 , pp. 147-162
    • Drews, G.1    Niklowitz, W.2
  • 10
    • 0031752797 scopus 로고    scopus 로고
    • Something from almost nothing: Carbon dioxide fixation in chemoautotrophs
    • Shively JM, van Keulen G, Meijer WG. 1998. Something from almost nothing: carbon dioxide fixation in chemoautotrophs. Ann Rev Microbiol 52:191-230.
    • (1998) Ann Rev Microbiol , vol.52 , pp. 191-230
    • Shively, J.M.1    van Keulen, G.2    Meijer, W.G.3
  • 11
    • 34250838686 scopus 로고    scopus 로고
    • Self-assembly in the carboxysome: A viral capsid-like protein shell in bacterial cells
    • Yeates TO, Tsai Y, Tanaka S, Sawaya MR, Kerfeld CA. 2007. Self-assembly in the carboxysome: a viral capsid-like protein shell in bacterial cells. Biochem Soc Trans 35:508-511.
    • (2007) Biochem Soc Trans , vol.35 , pp. 508-511
    • Yeates, T.O.1    Tsai, Y.2    Tanaka, S.3    Sawaya, M.R.4    Kerfeld, C.A.5
  • 12
    • 39749132210 scopus 로고    scopus 로고
    • Atomic-level models of the bacterial carboxysome shell
    • Tanaka S, Kerfeld CA, Sawaya MR, Cai F, Heinhorst S, et al. 2008. Atomic-level models of the bacterial carboxysome shell. Science 319:1083-1086.
    • (2008) Science , vol.319 , pp. 1083-1086
    • Tanaka, S.1    Kerfeld, C.A.2    Sawaya, M.R.3    Cai, F.4    Heinhorst, S.5
  • 13
    • 0026539278 scopus 로고
    • A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942
    • Fukuzawa H, Suzuki E, Komukai Y, Miyachi S. 1992. A gene homologous to chloroplast carbonic anhydrase (icfA) is essential to photosynthetic carbon dioxide fixation by Synechococcus PCC7942. Proc Natl Acad Sci USA 89:4437-4441.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4437-4441
    • Fukuzawa, H.1    Suzuki, E.2    Komukai, Y.3    Miyachi, S.4
  • 16
    • 33646583168 scopus 로고    scopus 로고
    • Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized
    • Tcherkez GG, Farquhar GD, Andrews TJ. 2006. Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized. Proc Natl Acad Sci USA 103:7246-7251.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7246-7251
    • Tcherkez, G.G.1    Farquhar, G.D.2    Andrews, T.J.3
  • 17
    • 20444389072 scopus 로고    scopus 로고
    • CO2 concentrating mechanisms in algae: Mechanisms, environmental modulation, and evolution
    • Giordano M, Beardall J, Raven JA. 2005. CO2 concentrating mechanisms in algae: mechanisms, environmental modulation, and evolution. Annu Rev Plant Biol 56:99-131.
    • (2005) Annu Rev Plant Biol , vol.56 , pp. 99-131
    • Giordano, M.1    Beardall, J.2    Raven, J.A.3
  • 18
    • 42049093465 scopus 로고    scopus 로고
    • A carboxysomal carbon-concentrating mechanism in the cyanelles of the 'coelacanth' of the algal world, Cyanophora paradoxa?
    • Fathinejad S, Steiner JM, Reipert S, Marchetti M, Allmaier G, et al. 2008. A carboxysomal carbon-concentrating mechanism in the cyanelles of the 'coelacanth' of the algal world, Cyanophora paradoxa? Physiologia Plantarum 133:27-32.
    • (2008) Physiologia Plantarum , vol.133 , pp. 27-32
    • Fathinejad, S.1    Steiner, J.M.2    Reipert, S.3    Marchetti, M.4    Allmaier, G.5
  • 19
    • 0001595227 scopus 로고
    • Expression of human carbonic-anhydrase in the cyanobacterium Synechococcus PCC7942 creates a high CO2-requiring phenotype-evidence for a central role for carboxysomes in the CO2 concentrating mechanism
    • Price GD, Badger MR. 1989. Expression of human carbonic-anhydrase in the cyanobacterium Synechococcus PCC7942 creates a high CO2-requiring phenotype-evidence for a central role for carboxysomes in the CO2 concentrating mechanism. Plant Physiology 91:505-513.
    • (1989) Plant Physiology , vol.91 , pp. 505-513
    • Price, G.D.1    Badger, M.R.2
  • 20
    • 0030067045 scopus 로고    scopus 로고
    • Quantitative evaluation of the role of a putative CO2-scavenging entity in the cyanobacterial CO2-concentrating mechanism
    • Fridlyand L, Kaplan A, Reinhold L. 1996. Quantitative evaluation of the role of a putative CO2-scavenging entity in the cyanobacterial CO2-concentrating mechanism. Biosystems 37:229-238.
    • (1996) Biosystems , vol.37 , pp. 229-238
    • Fridlyand, L.1    Kaplan, A.2    Reinhold, L.3
  • 21
    • 0029146875 scopus 로고
    • Use of electroporation to generate a Thiobacillus neapolitanus carboxysome mutant
    • English RS, Jin S, Shively JM. 1995. Use of electroporation to generate a Thiobacillus neapolitanus carboxysome mutant. Applied and Environ Microbiol 61:3256-3260.
    • (1995) Applied and Environ Microbiol , vol.61 , pp. 3256-3260
    • English, R.S.1    Jin, S.2    Shively, J.M.3
  • 22
    • 0006057548 scopus 로고
    • Analysis of high CO2 requiring mutants indicates a central role for the 5′ flanking region of Rbc and for the carboxysomes in cyanobacterial photosynthesis
    • Kaplan A. 1990. Analysis of high CO2 requiring mutants indicates a central role for the 5′ flanking region of Rbc and for the carboxysomes in cyanobacterial photosynthesis. Canadian Journal of Botany-Revue Canadienne De Botanique 68:1303-1310.
    • (1990) Canadian Journal of Botany-Revue Canadienne De Botanique , vol.68 , pp. 1303-1310
    • Kaplan, A.1
  • 23
    • 0024764016 scopus 로고
    • The 5′-flanking region of the gene encoding the large subunit of ribulose-1,5-biosphosphate carboxylase/oxygenase is crucial for growth of the cyanobacterium Synechococcus sp. strain PCC 7942 at the level of CO2 in air
    • Friedberg D, Kaplan A, Ariel R, Kessel M, Seijffers J. 1989. The 5′-flanking region of the gene encoding the large subunit of ribulose-1,5-biosphosphate carboxylase/oxygenase is crucial for growth of the cyanobacterium Synechococcus sp. strain PCC 7942 at the level of CO2 in air. J Bacteriol 171:6069-6076.
    • (1989) J Bacteriol , vol.171 , pp. 6069-6076
    • Friedberg, D.1    Kaplan, A.2    Ariel, R.3    Kessel, M.4    Seijffers, J.5
  • 25
    • 0002618178 scopus 로고
    • Isolation and characterization of high CO2-requiring-mutants of the cyanobacterium Synechococcus PCC 7942
    • Price GD, Badger MR. 1989. Isolation and characterization of high CO2-requiring-mutants of the cyanobacterium Synechococcus PCC 7942. Plant Physiol 91:514-525.
    • (1989) Plant Physiol , vol.91 , pp. 514-525
    • Price, G.D.1    Badger, M.R.2
  • 26
    • 0020589050 scopus 로고
    • Characterization of a homogenous preparation of carboxysomes from Thiobacillus neapolitanus
    • Cannon GC, Shively JM. 1983. Characterization of a homogenous preparation of carboxysomes from Thiobacillus neapolitanus. Arch Microbiol 134:52-59.
    • (1983) Arch Microbiol , vol.134 , pp. 52-59
    • Cannon, G.C.1    Shively, J.M.2
  • 27
    • 0023250899 scopus 로고
    • Activity of ribulose-1,5-bisphosphate carboxylase in intact and disrupted carboxysomes of Thiobacillus neapolitanus
    • Holthuijzen YA, Kuenen JG, Konings WN. 1987. Activity of ribulose-1,5-bisphosphate carboxylase in intact and disrupted carboxysomes of Thiobacillus neapolitanus. FEMS Microbiol Lett 42:121-124.
    • (1987) FEMS Microbiol Lett , vol.42 , pp. 121-124
    • Holthuijzen, Y.A.1    Kuenen, J.G.2    Konings, W.N.3
  • 28
    • 1642500161 scopus 로고    scopus 로고
    • A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell
    • So AK, Espie GS, Williams EB, Shively JM, Heinhorst S, et al. 2004. A novel evolutionary lineage of carbonic anhydrase (epsilon class) is a component of the carboxysome shell. J Bacteriol 186:623-630.
    • (2004) J Bacteriol , vol.186 , pp. 623-630
    • So, A.K.1    Espie, G.S.2    Williams, E.B.3    Shively, J.M.4    Heinhorst, S.5
  • 29
    • 0036941660 scopus 로고    scopus 로고
    • Characterization of a mutant lacking carboxysomal carbonic anhydrase from the cyanobacterium Synechocystis PCC6803
    • So AK, John-McKay M, Espie GS. 2002. Characterization of a mutant lacking carboxysomal carbonic anhydrase from the cyanobacterium Synechocystis PCC6803. Planta 214:456-467.
    • (2002) Planta , vol.214 , pp. 456-467
    • So, A.K.1    John-McKay, M.2    Espie, G.S.3
  • 30
    • 0001202065 scopus 로고
    • Isolation of a putative carboxysomal carbonic-anhydrase gene from the cyanobacterium Synechococcus Pcc7942
    • Yu JW, Price GD, Song L, Badger MR. 1992. Isolation of a putative carboxysomal carbonic-anhydrase gene from the cyanobacterium Synechococcus Pcc7942. Plant Physiology 100:794-800.
    • (1992) Plant Physiology , vol.100 , pp. 794-800
    • Yu, J.W.1    Price, G.D.2    Song, L.3    Badger, M.R.4
  • 31
    • 44849136273 scopus 로고    scopus 로고
    • CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes lacking carbonic anhydrase suggest the shell acts as a diffusional barrier for CO2
    • Dou Z, Heinhorst S, Williams EB, Murin CD, Shively JM, et al. 2008. CO2 fixation kinetics of Halothiobacillus neapolitanus mutant carboxysomes lacking carbonic anhydrase suggest the shell acts as a diffusional barrier for CO2. J Biol Chem 283:10377-10384.
    • (2008) J Biol Chem , vol.283 , pp. 10377-10384
    • Dou, Z.1    Heinhorst, S.2    Williams, E.B.3    Murin, C.D.4    Shively, J.M.5
  • 32
    • 0000096307 scopus 로고
    • Photosynthesis and photorespiration in a mutant of the cyanobacterium Synechocystis PCC-6803 lacking carboxysomes
    • Marcus Y, Berry JA, Pierce J. 1992. Photosynthesis and photorespiration in a mutant of the cyanobacterium Synechocystis PCC-6803 lacking carboxysomes. Planta 187:511-516.
    • (1992) Planta , vol.187 , pp. 511-516
    • Marcus, Y.1    Berry, J.A.2    Pierce, J.3
  • 33
    • 38049145935 scopus 로고    scopus 로고
    • Transcript analysis of the Halothiobacillus neapolitanus cso operon
    • Cai F, Heinhorst S, Shively JM, Cannon GC. 2008. Transcript analysis of the Halothiobacillus neapolitanus cso operon. Arch Microbiol 189:141-150.
    • (2008) Arch Microbiol , vol.189 , pp. 141-150
    • Cai, F.1    Heinhorst, S.2    Shively, J.M.3    Cannon, G.C.4
  • 35
    • 0032886650 scopus 로고    scopus 로고
    • The correlation of the gene csoS2 of the carboxysome operon with two polypeptides of the carboxysome in Thiobacillus neapolitanus
    • Baker SH, Lorbach SC, Rodriguez-Buey M, Williams DS, Aldrich HC, et al. 1999. The correlation of the gene csoS2 of the carboxysome operon with two polypeptides of the carboxysome in Thiobacillus neapolitanus. Arch Microbiol 172:233-239.
    • (1999) Arch Microbiol , vol.172 , pp. 233-239
    • Baker, S.H.1    Lorbach, S.C.2    Rodriguez-Buey, M.3    Williams, D.S.4    Aldrich, H.C.5
  • 36
    • 0036326931 scopus 로고    scopus 로고
    • Evolution and diversity of CO2 concentrating mechanisms in cyanobacteria
    • Badger MR, Hanson D, Price GD. 2002. Evolution and diversity of CO2 concentrating mechanisms in cyanobacteria. Functional Plant Biology 29:161-173.
    • (2002) Functional Plant Biology , vol.29 , pp. 161-173
    • Badger, M.R.1    Hanson, D.2    Price, G.D.3
  • 37
    • 0037318701 scopus 로고    scopus 로고
    • CO2 concentrating mechanisms in cyanobacteria: Molecular components, their diversity and evolution
    • Badger MR, Price GD. 2003. CO2 concentrating mechanisms in cyanobacteria: molecular components, their diversity and evolution. J Exp Bot 54:609-622.
    • (2003) J Exp Bot , vol.54 , pp. 609-622
    • Badger, M.R.1    Price, G.D.2
  • 40
    • 33646365079 scopus 로고    scopus 로고
    • The structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two
    • Sawaya MR, Cannon GC, Heinhorst S, Tanaka S, Williams EB, et al. 2006. The structure of beta-carbonic anhydrase from the carboxysomal shell reveals a distinct subclass with one active site for the price of two. J Biol Chem 281:7546-7555.
    • (2006) J Biol Chem , vol.281 , pp. 7546-7555
    • Sawaya, M.R.1    Cannon, G.C.2    Heinhorst, S.3    Tanaka, S.4    Williams, E.B.5
  • 41
    • 0028301484 scopus 로고
    • Isolation and characterization of a carboxysome shell gene from Thiobacillus neapolitanus
    • English RS, Lorbach SC, Qin X, Shively JM. 1994. Isolation and characterization of a carboxysome shell gene from Thiobacillus neapolitanus. Mol Microbiol 12:647-654.
    • (1994) Mol Microbiol , vol.12 , pp. 647-654
    • English, R.S.1    Lorbach, S.C.2    Qin, X.3    Shively, J.M.4
  • 42
    • 38649141503 scopus 로고    scopus 로고
    • A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria
    • Cot SS, So AK, Espie GS. 2008. A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria. J Bacteriol 190:936-945.
    • (2008) J Bacteriol , vol.190 , pp. 936-945
    • Cot, S.S.1    So, A.K.2    Espie, G.S.3
  • 43
    • 35748946615 scopus 로고    scopus 로고
    • Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple Rubisco complexes with carboxysomal proteins CcmM and CcaA
    • Long BM, Badger MR, Whitney SM, Price GD. 2007. Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple Rubisco complexes with carboxysomal proteins CcmM and CcaA. J Biol Chem 282:29323-29335.
    • (2007) J Biol Chem , vol.282 , pp. 29323-29335
    • Long, B.M.1    Badger, M.R.2    Whitney, S.M.3    Price, G.D.4
  • 44
    • 59349106139 scopus 로고    scopus 로고
    • Unpublished
    • Bobik TA. Unpublished. 2008.
    • (2008)
    • Bobik, T.A.1
  • 46
    • 0016250430 scopus 로고
    • Characterization of a phage-like particle from cells of Nitrobacter. II. Structure and size (author's transl)]
    • Peters KR. 1974. [Characterization of a phage-like particle from cells of Nitrobacter. II. Structure and size (author's transl)]. Arch Microbiol 97:129-140.
    • (1974) Arch Microbiol , vol.97 , pp. 129-140
    • Peters, K.R.1
  • 47
    • 34548276117 scopus 로고    scopus 로고
    • The structure of isolated Synechococcus strain WH8102 carboxysomes as revealed by electron cryotomography
    • Iancu CV, Ding HJ, Morris DM, Dias DP, Gonzales AD, et al. 2007. The structure of isolated Synechococcus strain WH8102 carboxysomes as revealed by electron cryotomography. J Mol Biol 372:764-773.
    • (2007) J Mol Biol , vol.372 , pp. 764-773
    • Iancu, C.V.1    Ding, H.J.2    Morris, D.M.3    Dias, D.P.4    Gonzales, A.D.5
  • 48
    • 33750822769 scopus 로고    scopus 로고
    • Structure of Halothiobacillus neapolitanus carboxysomes by cryoelectron tomography
    • Schmid MF, Paredes AM, Khant HA, Soyer F, Aldrich HC, et al. 2006. Structure of Halothiobacillus neapolitanus carboxysomes by cryoelectron tomography. J Mol Biol 364:526-535.
    • (2006) J Mol Biol , vol.364 , pp. 526-535
    • Schmid, M.F.1    Paredes, A.M.2    Khant, H.A.3    Soyer, F.4    Aldrich, H.C.5
  • 49
    • 30744456312 scopus 로고    scopus 로고
    • Intact carboxysomes in a cyanobacterial cell visualized by hilbert differential contrast transmission electron microscopy
    • Kaneko Y, Danev R, Nagayama K, Nakamoto H. 2006. Intact carboxysomes in a cyanobacterial cell visualized by hilbert differential contrast transmission electron microscopy. J Bacteriol 188:805-818.
    • (2006) J Bacteriol , vol.188 , pp. 805-818
    • Kaneko, Y.1    Danev, R.2    Nagayama, K.3    Nakamoto, H.4
  • 50
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar DL, Klug A. 1962. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol 27:1-24.
    • (1962) Cold Spring Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Caspar, D.L.1    Klug, A.2
  • 51
    • 0031588020 scopus 로고    scopus 로고
    • Quasi-equivalent viruses: A paradigm for protein assemblies
    • Johnson JE, Speir JA. 1997. Quasi-equivalent viruses: a paradigm for protein assemblies. J Mol Biol 269:665-675.
    • (1997) J Mol Biol , vol.269 , pp. 665-675
    • Johnson, J.E.1    Speir, J.A.2
  • 52
    • 34250347772 scopus 로고    scopus 로고
    • Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome
    • Tsai Y, Sawaya MR, Cannon GC, Cai F, Williams EB, et al. 2007. Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome. PLoS Biol 5:e144.
    • (2007) PLoS Biol , vol.5
    • Tsai, Y.1    Sawaya, M.R.2    Cannon, G.C.3    Cai, F.4    Williams, E.B.5
  • 53
    • 59349108809 scopus 로고    scopus 로고
    • Tanaka S, Yeates TO. unpublished results.
    • Tanaka S, Yeates TO. unpublished results.
  • 55
    • 0027934799 scopus 로고
    • The control region of the pdu/cob regulon in Salmonella typhimurium
    • Chen P, Andersson D, Roth JR. 1994. The control region of the pdu/cob regulon in Salmonella typhimurium. J Bacteriol 176:5474-5482.
    • (1994) J Bacteriol , vol.176 , pp. 5474-5482
    • Chen, P.1    Andersson, D.2    Roth, J.R.3
  • 56
    • 0036178889 scopus 로고    scopus 로고
    • PduA is a shell protein of polyhedral organelles involved in the coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2
    • Havemann GD, Sampson EM, Bobik TA. 2002. PduA is a shell protein of polyhedral organelles involved in the coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J Bacteriol 184:1253-1261.
    • (2002) J Bacteriol , vol.184 , pp. 1253-1261
    • Havemann, G.D.1    Sampson, E.M.2    Bobik, T.A.3
  • 57
    • 0028944586 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium: Nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster
    • Stojiljkovic I, Baeumler AJ, Heffron F. 1995. Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster. J Bacteriol 177:1357-1366.
    • (1995) J Bacteriol , vol.177 , pp. 1357-1366
    • Stojiljkovic, I.1    Baeumler, A.J.2    Heffron, F.3
  • 58
    • 0242492282 scopus 로고    scopus 로고
    • PduP is a coenzyme-A-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2
    • Leal NA, Havemann GD, Bobik TA. 2003. PduP is a coenzyme-A-acylating propionaldehyde dehydrogenase associated with the polyhedral bodies involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2. Arch Microbiol 180:353-361.
    • (2003) Arch Microbiol , vol.180 , pp. 353-361
    • Leal, N.A.1    Havemann, G.D.2    Bobik, T.A.3
  • 59
    • 0032882589 scopus 로고    scopus 로고
    • Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle
    • Horswill AR, Escalante-Semerena JC. 1999. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J Bacteriol 181:5615-5623.
    • (1999) J Bacteriol , vol.181 , pp. 5615-5623
    • Horswill, A.R.1    Escalante-Semerena, J.C.2
  • 60
    • 0023819084 scopus 로고
    • Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium
    • Obradors N, Badia J, Baldoma L, Aguilar J. 1988. Anaerobic metabolism of the L-rhamnose fermentation product 1,2-propanediol in Salmonella typhimurium. J Bacteriol 170:2159-2162.
    • (1988) J Bacteriol , vol.170 , pp. 2159-2162
    • Obradors, N.1    Badia, J.2    Baldoma, L.3    Aguilar, J.4
  • 61
    • 0018423604 scopus 로고
    • Fermentation of 1,2-propanediol and 1,2-ethanediol by some genera of Enterobacteriaceae, involving coenzyme B12-dependent diol dehydratase
    • Toraya T, Honda S, Fukui S. 1979. Fermentation of 1,2-propanediol and 1,2-ethanediol by some genera of Enterobacteriaceae, involving coenzyme B12-dependent diol dehydratase. J Bacteriol 139:39-47.
    • (1979) J Bacteriol , vol.139 , pp. 39-47
    • Toraya, T.1    Honda, S.2    Fukui, S.3
  • 62
    • 41949137665 scopus 로고    scopus 로고
    • Microcompartments for B12-dependent 1,2-propanediol degradation provide protection from DNA and cellular damage by a reactive metabolic intermediate
    • Sampson EM, Bobik TA. 2008. Microcompartments for B12-dependent 1,2-propanediol degradation provide protection from DNA and cellular damage by a reactive metabolic intermediate. J Bacteriol 190:2966-2971.
    • (2008) J Bacteriol , vol.190 , pp. 2966-2971
    • Sampson, E.M.1    Bobik, T.A.2
  • 63
    • 0035110798 scopus 로고    scopus 로고
    • Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene
    • Johnson CLVJ, Pechonick E, Park SD, Havemann GD, Leal NA, et al. 2001. Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene. J Bacteriol 183:1577-1584.
    • (2001) J Bacteriol , vol.183 , pp. 1577-1584
    • Johnson, C.L.V.J.1    Pechonick, E.2    Park, S.D.3    Havemann, G.D.4    Leal, N.A.5
  • 64
    • 0031464312 scopus 로고    scopus 로고
    • Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase
    • Mori K, Tobimatsu T, Hara T, Toraya T. 1997. Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase. J Biol Chem 272:32034-32041.
    • (1997) J Biol Chem , vol.272 , pp. 32034-32041
    • Mori, K.1    Tobimatsu, T.2    Hara, T.3    Toraya, T.4
  • 65
    • 0030668674 scopus 로고    scopus 로고
    • Propanediol utilization genes (pdu) of Salmonella typhimurium: Three genes for the propanediol dehydratase
    • Bobik TA, Xu Y, Jeter RM, Otto KE, Roth JR. 1997. Propanediol utilization genes (pdu) of Salmonella typhimurium: three genes for the propanediol dehydratase. J Bacteriol 179:6633-6639.
    • (1997) J Bacteriol , vol.179 , pp. 6633-6639
    • Bobik, T.A.1    Xu, Y.2    Jeter, R.M.3    Otto, K.E.4    Roth, J.R.5
  • 66
    • 33947401932 scopus 로고    scopus 로고
    • PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2
    • Liu Y, Leal NA, Sampson EM, Johnson CL, Havemann GD, et al. 2007. PduL is an evolutionarily distinct phosphotransacylase involved in B12-dependent 1,2-propanediol degradation by Salmonella enterica serovar Typhimurium LT2. J Bacteriol 189:1589-1596.
    • (2007) J Bacteriol , vol.189 , pp. 1589-1596
    • Liu, Y.1    Leal, N.A.2    Sampson, E.M.3    Johnson, C.L.4    Havemann, G.D.5
  • 67
    • 0037406882 scopus 로고    scopus 로고
    • Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol
    • Palacios S, Starai VJ, Escalante-Semerena JC. 2003. Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol. J Bacteriol 185:2802-2810.
    • (2003) J Bacteriol , vol.185 , pp. 2802-2810
    • Palacios, S.1    Starai, V.J.2    Escalante-Semerena, J.C.3
  • 68
    • 0032822281 scopus 로고    scopus 로고
    • The propanediol utilization (pdu) operon of Salmonella enterica Serovar Typhimurium LT2 includes genes necessary for the formation of polyhedral organelles involved in coenzyme B12-dependent 1,2-propanediol degradation
    • Bobik TA, Havemann GD, Busch RJ, Williams DS, Aldrich HC. 1999. The propanediol utilization (pdu) operon of Salmonella enterica Serovar Typhimurium LT2 includes genes necessary for the formation of polyhedral organelles involved in coenzyme B12-dependent 1,2-propanediol degradation. J Bacteriol 181:5967-5975.
    • (1999) J Bacteriol , vol.181 , pp. 5967-5975
    • Bobik, T.A.1    Havemann, G.D.2    Busch, R.J.3    Williams, D.S.4    Aldrich, H.C.5
  • 69
    • 0025306896 scopus 로고
    • Cobalamin-dependent 1,2-propanediol utilization by Salmonella typhimurium
    • Jeter RM. 1990. Cobalamin-dependent 1,2-propanediol utilization by Salmonella typhimurium. J Gen Microbiol 136:887-896.
    • (1990) J Gen Microbiol , vol.136 , pp. 887-896
    • Jeter, R.M.1
  • 70
    • 9244262460 scopus 로고    scopus 로고
    • Purification and initial characterization of the Salmonella enterica PduO ATP:Cob(I)alamin adenosyltransferase
    • Johnson CL, Buszko ML, Bobik TA. 2004. Purification and initial characterization of the Salmonella enterica PduO ATP:Cob(I)alamin adenosyltransferase. J Bacteriol 186:7881-7887.
    • (2004) J Bacteriol , vol.186 , pp. 7881-7887
    • Johnson, C.L.1    Buszko, M.L.2    Bobik, T.A.3
  • 71
    • 0031240468 scopus 로고    scopus 로고
    • A protein factor is essential for in situ reactivation of glycerol-inactivated adenosylcobalamin-dependent diol dehydratase
    • Mori K, Tobimatsu T, Toraya T. 1997. A protein factor is essential for in situ reactivation of glycerol-inactivated adenosylcobalamin-dependent diol dehydratase. Biosci Biotechnol Biochem 61:1729-1733.
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 1729-1733
    • Mori, K.1    Tobimatsu, T.2    Toraya, T.3
  • 72
    • 0032855711 scopus 로고    scopus 로고
    • Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor
    • Mori K, Toraya T. 1999. Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor. Biochemistry 38:13170-13178.
    • (1999) Biochemistry , vol.38 , pp. 13170-13178
    • Mori, K.1    Toraya, T.2
  • 73
    • 0026503401 scopus 로고
    • A single regulatory gene integrates control of vitamin B12 synthesis and propanediol degradation
    • Bobik TA, Ailion ME, Roth JR. 1992. A single regulatory gene integrates control of vitamin B12 synthesis and propanediol degradation. J Bacteriol 174:2253-2266.
    • (1992) J Bacteriol , vol.174 , pp. 2253-2266
    • Bobik, T.A.1    Ailion, M.E.2    Roth, J.R.3
  • 74
    • 17644393113 scopus 로고    scopus 로고
    • Biochemical evidence that the pduS gene encodes a bifunctional cobalamin reductase
    • Sampson EM, Johnson CL, Bobik TA. 2005. Biochemical evidence that the pduS gene encodes a bifunctional cobalamin reductase. Microbiology 151:1169-1177.
    • (2005) Microbiology , vol.151 , pp. 1169-1177
    • Sampson, E.M.1    Johnson, C.L.2    Bobik, T.A.3
  • 75
    • 0026582188 scopus 로고
    • The poc locus is required for 1,2-propanediol-dependent transcription of the cobalamin biosynthetic (cob) and propanediol utilization (pdu) genes of Salmonella typhimurium
    • Rondon MR, Escalante-Semerena JC. 1992. The poc locus is required for 1,2-propanediol-dependent transcription of the cobalamin biosynthetic (cob) and propanediol utilization (pdu) genes of Salmonella typhimurium. J Bacteriol 174:2267-2272.
    • (1992) J Bacteriol , vol.174 , pp. 2267-2272
    • Rondon, M.R.1    Escalante-Semerena, J.C.2
  • 76
    • 0028808541 scopus 로고
    • DNA polymerase I function is required for the utilization of ethanolamine, 1,2-propanediol, and propionate by Salmonella typhimurium LT2
    • Rondon MR, Horswill RA, Escalante-Semerena KC. 1995. DNA polymerase I function is required for the utilization of ethanolamine, 1,2-propanediol, and propionate by Salmonella typhimurium LT2. J Bacteriol 177:7119-7124.
    • (1995) J Bacteriol , vol.177 , pp. 7119-7124
    • Rondon, M.R.1    Horswill, R.A.2    Escalante-Semerena, K.C.3
  • 77
    • 0029563686 scopus 로고
    • Glutathione is required for maximal transcription of the cobalamin biosynthetic and 1,2-propanediol utilization (cob/pdu) regulon and for the catabolism of ethanolamine, 1,2-propanediol, and propionate in Salmonella typhimurium
    • Rondon MR, Kazmierczak R, Escalante-Semerena JC. 1995. Glutathione is required for maximal transcription of the cobalamin biosynthetic and 1,2-propanediol utilization (cob/pdu) regulon and for the catabolism of ethanolamine, 1,2-propanediol, and propionate in Salmonella typhimurium. J Bacteriol 177:5434-5439.
    • (1995) J Bacteriol , vol.177 , pp. 5434-5439
    • Rondon, M.R.1    Kazmierczak, R.2    Escalante-Semerena, J.C.3
  • 78
    • 33645964606 scopus 로고    scopus 로고
    • Conserving a volatile metabolite: A role for carboxysome-like organelles in Salmonella enterica
    • Penrod JT, Roth JR. 2006. Conserving a volatile metabolite: a role for carboxysome-like organelles in Salmonella enterica. J Bacteriol 188: 2865-2874.
    • (2006) J Bacteriol , vol.188 , pp. 2865-2874
    • Penrod, J.T.1    Roth, J.R.2
  • 79
    • 0018166846 scopus 로고
    • Evolution of propanediol utilization in Escherichia coli mutants with improved substrate scavenging power
    • Hacking AJ, Aguilar J, Lin ECC. 1978. Evolution of propanediol utilization in Escherichia coli mutants with improved substrate scavenging power. J Bacteriol 136:522-530.
    • (1978) J Bacteriol , vol.136 , pp. 522-530
    • Hacking, A.J.1    Aguilar, J.2    Lin, E.C.C.3
  • 80
    • 59349116470 scopus 로고    scopus 로고
    • Crowley CS, Sawaya MR, Bobik TA, Yeates TO. unpublished results 2008.
    • Crowley CS, Sawaya MR, Bobik TA, Yeates TO. unpublished results 2008.
  • 82
    • 0032851358 scopus 로고    scopus 로고
    • The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins
    • Kofoid E, Rappleye C, Stojiljkovic I, Roth J. 1999. The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. J Bacteriol 181:5317-5329.
    • (1999) J Bacteriol , vol.181 , pp. 5317-5329
    • Kofoid, E.1    Rappleye, C.2    Stojiljkovic, I.3    Roth, J.4
  • 83
    • 0016593454 scopus 로고
    • Evidence for the B12-dependent enzyme ethanolamine deaminase in Salmonella
    • Chang GW, Chang JT. 1975. Evidence for the B12-dependent enzyme ethanolamine deaminase in Salmonella. Nature (London) 254:150-151.
    • (1975) Nature (London) , vol.254 , pp. 150-151
    • Chang, G.W.1    Chang, J.T.2
  • 84
    • 0024075956 scopus 로고
    • Ethanolamine utilization in Salmonella typhimurium
    • Roof DM, Roth JR. 1988. Ethanolamine utilization in Salmonella typhimurium. J Bacteriol 170:3855-3863.
    • (1988) J Bacteriol , vol.170 , pp. 3855-3863
    • Roof, D.M.1    Roth, J.R.2
  • 85
    • 0035094993 scopus 로고    scopus 로고
    • The alternative electron acceptor tetrathionate supports B12-dependent anaerobic growth of Salmonella enterica serovar Typhimurium on ethanolamine or 1,2-propanediol
    • Price-Carter M, Tingey J, Bobik TA, Roth JR. 2001. The alternative electron acceptor tetrathionate supports B12-dependent anaerobic growth of Salmonella enterica serovar Typhimurium on ethanolamine or 1,2-propanediol. J Bacteriol 183:2463-2475.
    • (2001) J Bacteriol , vol.183 , pp. 2463-2475
    • Price-Carter, M.1    Tingey, J.2    Bobik, T.A.3    Roth, J.R.4
  • 86
    • 28044459168 scopus 로고    scopus 로고
    • Minimal functions and physiological conditions required for growth of Salmonella enterica on ethanolamine in the absence of the metabolosome
    • Brinsmade SR, Paldon T, Escalante-Semerena JC. 2005. Minimal functions and physiological conditions required for growth of Salmonella enterica on ethanolamine in the absence of the metabolosome. J Bacteriol 187:8039-8046.
    • (2005) J Bacteriol , vol.187 , pp. 8039-8046
    • Brinsmade, S.R.1    Paldon, T.2    Escalante-Semerena, J.C.3
  • 87
    • 0038740503 scopus 로고    scopus 로고
    • Carbon sequestration in Synechococcus Sp.: From molecular machines to hierarchical modeling
    • Heffelfinger GS, Martino A, Gorin A, Xu Y, Rintoul MD 3rd, et al. 2002. Carbon sequestration in Synechococcus Sp.: from molecular machines to hierarchical modeling. Omics 6:305-330.
    • (2002) Omics , vol.6 , pp. 305-330
    • Heffelfinger, G.S.1    Martino, A.2    Gorin, A.3    Xu, Y.4    Rintoul 3rd, M.D.5
  • 88
    • 0027421793 scopus 로고
    • Two global regulatory systems (Crp and Arc) control the cobalamin/propanediol regulon of Salmonella typhimurium
    • Ailion M, Bobik TA, Roth JR. 1993. Two global regulatory systems (Crp and Arc) control the cobalamin/propanediol regulon of Salmonella typhimurium. J Bacteriol 175:7200-7208.
    • (1993) J Bacteriol , vol.175 , pp. 7200-7208
    • Ailion, M.1    Bobik, T.A.2    Roth, J.R.3
  • 89
    • 0024369388 scopus 로고
    • Redox regulation of the genes for cobinamide biosynthesis in Salmonella typhimurium
    • Andersson DI, Roth JR. 1989. Redox regulation of the genes for cobinamide biosynthesis in Salmonella typhimurium. J Bacteriol 171: 6734-6739.
    • (1989) J Bacteriol , vol.171 , pp. 6734-6739
    • Andersson, D.I.1    Roth, J.R.2
  • 92
    • 0032917462 scopus 로고    scopus 로고
    • Coordinate intracellular expression of Salmonella genes induced during infection
    • Heithoff DM, Conner CP, Hentschel U, Govantes F, Hanna PC, et al. 1999. Coordinate intracellular expression of Salmonella genes induced during infection. J Bacteriol 181:799-807.
    • (1999) J Bacteriol , vol.181 , pp. 799-807
    • Heithoff, D.M.1    Conner, C.P.2    Hentschel, U.3    Govantes, F.4    Hanna, P.C.5
  • 93
    • 34247237333 scopus 로고    scopus 로고
    • Identification of novel genes in genomic islands that contribute to Salmonella typhimurium replication in macrophages
    • Klumpp J, Fuchs TM. 2007. Identification of novel genes in genomic islands that contribute to Salmonella typhimurium replication in macrophages. Microbiology 153:1207-1220.
    • (2007) Microbiology , vol.153 , pp. 1207-1220
    • Klumpp, J.1    Fuchs, T.M.2
  • 94
    • 0037376106 scopus 로고    scopus 로고
    • Comparison of the genome sequences of Listeria monocytogenes and Listeria innocua: Clues for evolution and pathogenicity
    • Buchrieser C, Rusniok C, Kunst F, Cossart P, Glaser P. 2003. Comparison of the genome sequences of Listeria monocytogenes and Listeria innocua: clues for evolution and pathogenicity. FEMS. Immunol Med Microbiol 35:207-213.
    • (2003) FEMS. Immunol Med Microbiol , vol.35 , pp. 207-213
    • Buchrieser, C.1    Rusniok, C.2    Kunst, F.3    Cossart, P.4    Glaser, P.5
  • 95
    • 30744447972 scopus 로고    scopus 로고
    • Identification of Listeria monocytogenes genes contributing to intracellular replication by expression profiling and mutant screening
    • Joseph B, Przybilla K, Stuhler C, Schauer K, Slaghuis J, et al. 2006. Identification of Listeria monocytogenes genes contributing to intracellular replication by expression profiling and mutant screening. J Bacteriol 188:556-568.
    • (2006) J Bacteriol , vol.188 , pp. 556-568
    • Joseph, B.1    Przybilla, K.2    Stuhler, C.3    Schauer, K.4    Slaghuis, J.5
  • 96
    • 36649006253 scopus 로고    scopus 로고
    • Genomic and biochemical studies demonstrating the absence of an alkane-producing phenotype in Vibrio furnissii M1
    • Wackett LP, Frias JA, Seffernick JL, Sukovich DJ, Cameron SM. 2007. Genomic and biochemical studies demonstrating the absence of an alkane-producing phenotype in Vibrio furnissii M1. Appl Environ Microbiol 73:7192-7198.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 7192-7198
    • Wackett, L.P.1    Frias, J.A.2    Seffernick, J.L.3    Sukovich, D.J.4    Cameron, S.M.5
  • 97
    • 41149164162 scopus 로고    scopus 로고
    • The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features
    • Seedorf H, Fricke WF, Veith B, Bruggemann H, Liesegang H, et al. 2008. The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features. Proc Natl Acad Sci USA 105:2128-2133.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 2128-2133
    • Seedorf, H.1    Fricke, W.F.2    Veith, B.3    Bruggemann, H.4    Liesegang, H.5


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