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Volumn 23, Issue 1, 2015, Pages 22-34

Bacterial microcompartments and the modular construction of microbial metabolism

Author keywords

Bacterial microcompartments; Bacterial organelles; Carboxysomes; Metabolosomes; Synthetic biology

Indexed keywords

AEROBIC CAPACITY; ANAEROBIC METABOLISM; BACTERIAL CELL; BACTERIAL METABOLISM; BACTERIAL MICROCOMPARTMENT; CARBON FIXATION; CARDIOVASCULAR DISEASE; CATABOLISM; CELL FUNCTION; CELL MEMBRANE PERMEABILITY; CELL ORGANELLE; CELL STRUCTURE; CYTOARCHITECTURE; ENDOCYTOBIOSIS; HOST PATHOGEN INTERACTION; METABOLIC REGULATION; MOLECULAR EVOLUTION; MOLECULAR PATHOLOGY; NONHUMAN; NUTRIENT CYCLING; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN INTERACTION; REVIEW; SYNTHETIC BIOLOGY; BACTERIUM; CELL COMPARTMENTALIZATION; CHEMISTRY; CYTOLOGY; PROTEIN CONFORMATION; PROTEIN ENGINEERING;

EID: 84920531816     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2014.10.003     Document Type: Review
Times cited : (136)

References (101)
  • 1
    • 79960939957 scopus 로고    scopus 로고
    • Ecosystems biology of microbial metabolism
    • Klitgord N., Segrè D. Ecosystems biology of microbial metabolism. Curr. Opin. Biotechnol. 2011, 22:541-546.
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 541-546
    • Klitgord, N.1    Segrè, D.2
  • 2
    • 0031725610 scopus 로고    scopus 로고
    • Thinking about bacterial populations as multicellular organisms
    • Shapiro J.A. Thinking about bacterial populations as multicellular organisms. Annu. Rev. Microbiol. 1998, 52:81-104.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 81-104
    • Shapiro, J.A.1
  • 3
    • 77957959732 scopus 로고    scopus 로고
    • Bacterial microcompartments
    • Kerfeld C.A., et al. Bacterial microcompartments. Annu. Rev. Microbiol. 2010, 64:391-408.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 391-408
    • Kerfeld, C.A.1
  • 4
    • 84884528591 scopus 로고    scopus 로고
    • Functions, compositions, and evolution of the two types of carboxysomes: polyhedral microcompartments that facilitate CO2 fixation in cyanobacteria and some proteobacteria
    • Rae B.D., et al. Functions, compositions, and evolution of the two types of carboxysomes: polyhedral microcompartments that facilitate CO2 fixation in cyanobacteria and some proteobacteria. Microbiol. Mol. Biol. Rev. 2013, 77:357-379.
    • (2013) Microbiol. Mol. Biol. Rev. , vol.77 , pp. 357-379
    • Rae, B.D.1
  • 5
    • 84871837954 scopus 로고    scopus 로고
    • Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme
    • Craciun S., Balskus E.P. Microbial conversion of choline to trimethylamine requires a glycyl radical enzyme. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:21307-21312.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 21307-21312
    • Craciun, S.1    Balskus, E.P.2
  • 6
    • 84903975403 scopus 로고    scopus 로고
    • Functional genomics with a comprehensive library of transposon mutants for the sulfate-reducing bacterium Desulfovibrio alaskensis
    • Kuehl J.V., et al. Functional genomics with a comprehensive library of transposon mutants for the sulfate-reducing bacterium Desulfovibrio alaskensis. MBio 2014, 5:e01041-e1114.
    • (2014) MBio , vol.5 , pp. e01041-e1114
    • Kuehl, J.V.1
  • 7
    • 84873819450 scopus 로고    scopus 로고
    • Involvement of a bacterial microcompartment in the metabolism of fucose and rhamnose by Clostridium phytofermentans
    • Petit E., et al. Involvement of a bacterial microcompartment in the metabolism of fucose and rhamnose by Clostridium phytofermentans. PLoS ONE 2013, 8:e54337.
    • (2013) PLoS ONE , vol.8 , pp. e54337
    • Petit, E.1
  • 8
    • 33745002519 scopus 로고    scopus 로고
    • Whole-genome transcription profiling reveals genes up-regulated by growth on fucose in the human gut bacterium "Roseburia inulinivorans"
    • Scott K.P., et al. Whole-genome transcription profiling reveals genes up-regulated by growth on fucose in the human gut bacterium "Roseburia inulinivorans". J. Bacteriol. 2006, 188:4340-4349.
    • (2006) J. Bacteriol. , vol.188 , pp. 4340-4349
    • Scott, K.P.1
  • 9
    • 84900070956 scopus 로고    scopus 로고
    • Characterization of a planctomycetal organelle: a novel bacterial microcompartment for the aerobic degradation of plant saccharides
    • Erbilgin O., et al. Characterization of a planctomycetal organelle: a novel bacterial microcompartment for the aerobic degradation of plant saccharides. Appl. Environ. Microbiol. 2014, 80:2193-2205.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 2193-2205
    • Erbilgin, O.1
  • 10
    • 23244439942 scopus 로고    scopus 로고
    • Protein structures forming the shell of primitive bacterial organelles
    • Kerfeld C.A., et al. Protein structures forming the shell of primitive bacterial organelles. Science 2005, 309:936-938.
    • (2005) Science , vol.309 , pp. 936-938
    • Kerfeld, C.A.1
  • 11
    • 68949220061 scopus 로고    scopus 로고
    • Identification and structural analysis of a novel carboxysome shell protein with implications for metabolite transport
    • Klein M.G., et al. Identification and structural analysis of a novel carboxysome shell protein with implications for metabolite transport. J. Mol. Biol. 2009, 392:319-333.
    • (2009) J. Mol. Biol. , vol.392 , pp. 319-333
    • Klein, M.G.1
  • 12
    • 39749132210 scopus 로고    scopus 로고
    • Atomic-level models of the bacterial carboxysome shell
    • Tanaka S., et al. Atomic-level models of the bacterial carboxysome shell. Science 2008, 319:1083-1086.
    • (2008) Science , vol.319 , pp. 1083-1086
    • Tanaka, S.1
  • 13
    • 34250968370 scopus 로고
    • Beiträge zur Cytologie der Blaualgen II. Mitteilung Zentroplasma und granuläre Einschlüsse von Phormidium uneinatum
    • Drews G., Niklowitz W. Beiträge zur Cytologie der Blaualgen II. Mitteilung Zentroplasma und granuläre Einschlüsse von Phormidium uneinatum. Arch. Mikrobiol. 1956, 24:147-162.
    • (1956) Arch. Mikrobiol. , vol.24 , pp. 147-162
    • Drews, G.1    Niklowitz, W.2
  • 14
    • 84908350120 scopus 로고    scopus 로고
    • A taxonomy of bacterial microcompartment loci constructed by a novel scoring method
    • Axen S.D., et al. A taxonomy of bacterial microcompartment loci constructed by a novel scoring method. PLoS Comput. Biol 2014, 10:e1003898. 10.1371/journal.pcbi.1003898.
    • (2014) PLoS Comput. Biol , vol.10 , pp. e1003898
    • Axen, S.D.1
  • 15
    • 84861208627 scopus 로고    scopus 로고
    • Elucidating the essential role of the conserved carboxysomal protein CcmN reveals a common feature of bacterial microcompartment assembly
    • Kinney J.N., et al. Elucidating the essential role of the conserved carboxysomal protein CcmN reveals a common feature of bacterial microcompartment assembly. J. Biol. Chem. 2012, 287:17729-17736.
    • (2012) J. Biol. Chem. , vol.287 , pp. 17729-17736
    • Kinney, J.N.1
  • 16
    • 84901209724 scopus 로고    scopus 로고
    • The distribution of polyhedral bacterial microcompartments suggests frequent horizontal transfer and operon reassembly
    • Abdul-Rahman F., et al. The distribution of polyhedral bacterial microcompartments suggests frequent horizontal transfer and operon reassembly. Phylogenet. Evol. Biol. 2013, 1:1000118.
    • (2013) Phylogenet. Evol. Biol. , vol.1 , pp. 1000118
    • Abdul-Rahman, F.1
  • 17
    • 84874058227 scopus 로고    scopus 로고
    • Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria
    • Jorda J., et al. Using comparative genomics to uncover new kinds of protein-based metabolic organelles in bacteria. Protein Sci. 2012, 22:179-195.
    • (2012) Protein Sci. , vol.22 , pp. 179-195
    • Jorda, J.1
  • 18
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
    • Parsons J.B., et al. Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement. Mol. Cell 2010, 38:305-315.
    • (2010) Mol. Cell , vol.38 , pp. 305-315
    • Parsons, J.B.1
  • 19
    • 78049443356 scopus 로고    scopus 로고
    • The carboxysome shell is permeable to protons
    • Menon B.B., et al. The carboxysome shell is permeable to protons. J. Bacteriol. 2010, 192:5881-5886.
    • (2010) J. Bacteriol. , vol.192 , pp. 5881-5886
    • Menon, B.B.1
  • 20
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage D.F., et al. Spatially ordered dynamics of the bacterial carbon fixation machinery. Science 2010, 327:1258-1261.
    • (2010) Science , vol.327 , pp. 1258-1261
    • Savage, D.F.1
  • 21
    • 84872197140 scopus 로고    scopus 로고
    • Bacterial microcompartments moving into a synthetic biological world
    • Frank S., et al. Bacterial microcompartments moving into a synthetic biological world. J. Biotechnol. 2013, 163:273-279.
    • (2013) J. Biotechnol. , vol.163 , pp. 273-279
    • Frank, S.1
  • 22
    • 30744447972 scopus 로고    scopus 로고
    • Identification of Listeria monocytogenes genes contributing to intracellular replication by expression profiling and mutant screening
    • Joseph B., et al. Identification of Listeria monocytogenes genes contributing to intracellular replication by expression profiling and mutant screening. J. Bacteriol. 2006, 188:556-568.
    • (2006) J. Bacteriol. , vol.188 , pp. 556-568
    • Joseph, B.1
  • 23
    • 34247237333 scopus 로고    scopus 로고
    • Identification of novel genes in genomic islands that contribute to Salmonella typhimurium replication in macrophages
    • Klumpp J., Fuchs T.M. Identification of novel genes in genomic islands that contribute to Salmonella typhimurium replication in macrophages. Microbiology 2007, 2:1207-1220.
    • (2007) Microbiology , vol.2 , pp. 1207-1220
    • Klumpp, J.1    Fuchs, T.M.2
  • 24
    • 84863449360 scopus 로고    scopus 로고
    • Ethanolamine controls expression of genes encoding components involved in interkingdom signaling and virulence in enterohemorrhagic Escherichia coli O157:H7
    • Kendall M.M., et al. Ethanolamine controls expression of genes encoding components involved in interkingdom signaling and virulence in enterohemorrhagic Escherichia coli O157:H7. MBio 2012, 3:1-10.
    • (2012) MBio , vol.3 , pp. 1-10
    • Kendall, M.M.1
  • 25
    • 80855136572 scopus 로고    scopus 로고
    • Salmonella enterica typhimurium colonizing the lumen of the chicken intestine grows slowly and upregulates a unique set of virulence and metabolism genes
    • Harvey P.C., et al. Salmonella enterica typhimurium colonizing the lumen of the chicken intestine grows slowly and upregulates a unique set of virulence and metabolism genes. Infect. Immun. 2011, 79:4105-4121.
    • (2011) Infect. Immun. , vol.79 , pp. 4105-4121
    • Harvey, P.C.1
  • 26
    • 34248386490 scopus 로고    scopus 로고
    • Enterococcus faecalis mutations affecting virulence in the Caenorhabditis elegans model host
    • Maadani A., et al. Enterococcus faecalis mutations affecting virulence in the Caenorhabditis elegans model host. Infect. Immun. 2007, 75:2634-2637.
    • (2007) Infect. Immun. , vol.75 , pp. 2634-2637
    • Maadani, A.1
  • 27
    • 84876563088 scopus 로고    scopus 로고
    • Intestinal microbial metabolism of phosphatidylcholine and cardiovascular risk
    • Tang W.H.W., et al. Intestinal microbial metabolism of phosphatidylcholine and cardiovascular risk. N. Engl. J. Med. 2013, 368:1575-1584.
    • (2013) N. Engl. J. Med. , vol.368 , pp. 1575-1584
    • Tang, W.H.W.1
  • 28
    • 79953733693 scopus 로고    scopus 로고
    • Gut flora metabolism of phosphatidylcholine promotes cardiovascular disease
    • Wang Z., et al. Gut flora metabolism of phosphatidylcholine promotes cardiovascular disease. Nature 2011, 472:57-63.
    • (2011) Nature , vol.472 , pp. 57-63
    • Wang, Z.1
  • 29
    • 84905198664 scopus 로고    scopus 로고
    • Planctomycetes and macroalgae, a striking association
    • Lage O.M., Bondoso J. Planctomycetes and macroalgae, a striking association. Front. Microbiol. 2014, 5:1-9.
    • (2014) Front. Microbiol. , vol.5 , pp. 1-9
    • Lage, O.M.1    Bondoso, J.2
  • 30
    • 84905867273 scopus 로고    scopus 로고
    • Structural insights into higher-order assembly and function of the bacterial microcompartment protein PduA
    • Pang A., et al. Structural insights into higher-order assembly and function of the bacterial microcompartment protein PduA. J. Biol. Chem. 2014, 289:22377-22384.
    • (2014) J. Biol. Chem. , vol.289 , pp. 22377-22384
    • Pang, A.1
  • 31
    • 84901239311 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment
    • Sinha S., et al. Alanine scanning mutagenesis identifies an asparagine-arginine-lysine triad essential to assembly of the shell of the Pdu microcompartment. J. Mol. Biol. 2014, 426:2328-2345.
    • (2014) J. Mol. Biol. , vol.426 , pp. 2328-2345
    • Sinha, S.1
  • 32
    • 84892402637 scopus 로고    scopus 로고
    • A challenging interpretation of a hexagonally layered protein structure
    • Thompson M.C., Yeates T.O. A challenging interpretation of a hexagonally layered protein structure. Acta Crystallogr. D: Biol. Crystallogr. 2014, 70:203-208.
    • (2014) Acta Crystallogr. D: Biol. Crystallogr. , vol.70 , pp. 203-208
    • Thompson, M.C.1    Yeates, T.O.2
  • 33
    • 84868087161 scopus 로고    scopus 로고
    • Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment
    • Pitts A.C., et al. Structural insight into the Clostridium difficile ethanolamine utilisation microcompartment. PLoS ONE 2012, 7:e48360.
    • (2012) PLoS ONE , vol.7 , pp. e48360
    • Pitts, A.C.1
  • 34
    • 79952178155 scopus 로고    scopus 로고
    • Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site
    • Pang A., et al. Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site. Acta Crystallogr. D: Biol. Crystallogr. 2011, 67:91-96.
    • (2011) Acta Crystallogr. D: Biol. Crystallogr. , vol.67 , pp. 91-96
    • Pang, A.1
  • 35
    • 78549246253 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell
    • Crowley C.S., et al. Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell. J. Biol. Chem. 2010, 285:37838-37846.
    • (2010) J. Biol. Chem. , vol.285 , pp. 37838-37846
    • Crowley, C.S.1
  • 36
    • 74849140487 scopus 로고    scopus 로고
    • Structure and mechanisms of a protein-based organelle in Escherichia coli
    • Tanaka S., et al. Structure and mechanisms of a protein-based organelle in Escherichia coli. Science 2010, 327:81-84.
    • (2010) Science , vol.327 , pp. 81-84
    • Tanaka, S.1
  • 37
    • 70350096554 scopus 로고    scopus 로고
    • Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri
    • Heldt D., et al. Structure of a trimeric bacterial microcompartment shell protein, EtuB, associated with ethanol utilization in Clostridium kluyveri. Biochem. J. 2009, 423:199-207.
    • (2009) Biochem. J. , vol.423 , pp. 199-207
    • Heldt, D.1
  • 38
    • 67049117718 scopus 로고    scopus 로고
    • Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment
    • Sagermann M., et al. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:8883-8887.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 8883-8887
    • Sagermann, M.1
  • 39
    • 58149456903 scopus 로고    scopus 로고
    • Insights from multiple structures of the shell proteins from the beta-carboxysome
    • Tanaka S., et al. Insights from multiple structures of the shell proteins from the beta-carboxysome. Protein Sci. 2009, 18:108-120.
    • (2009) Protein Sci. , vol.18 , pp. 108-120
    • Tanaka, S.1
  • 40
    • 50849120064 scopus 로고    scopus 로고
    • Structure of the PduU shell protein from the Pdu microcompartment of Salmonella
    • Crowley C.S., et al. Structure of the PduU shell protein from the Pdu microcompartment of Salmonella. Structure 2008, 16:1324-1332.
    • (2008) Structure , vol.16 , pp. 1324-1332
    • Crowley, C.S.1
  • 41
    • 34250347772 scopus 로고    scopus 로고
    • Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome
    • Tsai Y., et al. Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome. PLoS Biol. 2007, 5:e144.
    • (2007) PLoS Biol. , vol.5 , pp. e144
    • Tsai, Y.1
  • 42
    • 84856963458 scopus 로고    scopus 로고
    • Comparative analysis of carboxysome shell proteins
    • Kinney J.N., et al. Comparative analysis of carboxysome shell proteins. Photosynth. Res. 2011, 109:21-32.
    • (2011) Photosynth. Res. , vol.109 , pp. 21-32
    • Kinney, J.N.1
  • 43
    • 84878391635 scopus 로고    scopus 로고
    • The structure of CcmP, a tandem bacterial microcompartment domain protein from the β-carboxysome, forms a subcompartment within a microcompartment
    • Cai F., et al. The structure of CcmP, a tandem bacterial microcompartment domain protein from the β-carboxysome, forms a subcompartment within a microcompartment. J. Biol. Chem. 2013, 288:16055-16063.
    • (2013) J. Biol. Chem. , vol.288 , pp. 16055-16063
    • Cai, F.1
  • 44
    • 84889097184 scopus 로고    scopus 로고
    • Two new high-resolution crystal structures of carboxysome pentamer proteins reveal high structural conservation of CcmL orthologs among distantly related cyanobacterial species
    • Sutter M., et al. Two new high-resolution crystal structures of carboxysome pentamer proteins reveal high structural conservation of CcmL orthologs among distantly related cyanobacterial species. Photosynth. Res. 2013, 118:9-16.
    • (2013) Photosynth. Res. , vol.118 , pp. 9-16
    • Sutter, M.1
  • 45
    • 84928138623 scopus 로고    scopus 로고
    • Engineering bacterial microcompartment shells: chimeric shell proteins and chimeric carboxysome shells
    • Cai F., et al. Engineering bacterial microcompartment shells: chimeric shell proteins and chimeric carboxysome shells. ACS Synth. Biol. 2014, 10.1021/sb500226j.
    • (2014) ACS Synth. Biol.
    • Cai, F.1
  • 46
    • 84865191456 scopus 로고    scopus 로고
    • Structural determinants of the outer shell of β-carboxysomes in Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL
    • Rae B.D., et al. Structural determinants of the outer shell of β-carboxysomes in Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL. PLoS ONE 2012, 7:e43871.
    • (2012) PLoS ONE , vol.7 , pp. e43871
    • Rae, B.D.1
  • 47
    • 78049415865 scopus 로고    scopus 로고
    • Crystallographic insights into the pore structures and mechanisms of the EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment of Escherichia coli
    • Takenoya M., et al. Crystallographic insights into the pore structures and mechanisms of the EutL and EutM shell proteins of the ethanolamine-utilizing microcompartment of Escherichia coli. J. Bacteriol. 2010, 192:6056-6063.
    • (2010) J. Bacteriol. , vol.192 , pp. 6056-6063
    • Takenoya, M.1
  • 48
    • 84869431601 scopus 로고    scopus 로고
    • Substrate channels revealed in the trimeric Lactobacillus reuteri bacterial microcompartment shell protein PduB
    • Pang A., et al. Substrate channels revealed in the trimeric Lactobacillus reuteri bacterial microcompartment shell protein PduB. Acta Crystallogr. D: Biol. Crystallogr. 2012, 68:1642-1652.
    • (2012) Acta Crystallogr. D: Biol. Crystallogr. , vol.68 , pp. 1642-1652
    • Pang, A.1
  • 49
    • 84864863698 scopus 로고    scopus 로고
    • A dodecameric CcmK2 structure suggests β-carboxysomal shell facets have a double-layered organization
    • Samborska B., Kimber M.S. A dodecameric CcmK2 structure suggests β-carboxysomal shell facets have a double-layered organization. Structure 2012, 20:1353-1362.
    • (2012) Structure , vol.20 , pp. 1353-1362
    • Samborska, B.1    Kimber, M.S.2
  • 50
    • 84899945180 scopus 로고    scopus 로고
    • Assembly of robust bacterial microcompartment shells using building blocks from an organelle of unknown function
    • Lassila J.K., et al. Assembly of robust bacterial microcompartment shells using building blocks from an organelle of unknown function. J. Mol. Biol. 2014, 426:2217-2228.
    • (2014) J. Mol. Biol. , vol.426 , pp. 2217-2228
    • Lassila, J.K.1
  • 51
    • 47249117924 scopus 로고    scopus 로고
    • Biochemical and structural insights into bacterial organelle form and biogenesis
    • Parsons J.B., et al. Biochemical and structural insights into bacterial organelle form and biogenesis. J. Biol. Chem. 2008, 283:14366-14375.
    • (2008) J. Biol. Chem. , vol.283 , pp. 14366-14375
    • Parsons, J.B.1
  • 52
    • 78649494879 scopus 로고    scopus 로고
    • Characterisation of PduS, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment
    • Parsons J.B., et al. Characterisation of PduS, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment. PLoS ONE 2010, 5:e14009.
    • (2010) PLoS ONE , vol.5 , pp. e14009
    • Parsons, J.B.1
  • 53
    • 77957353322 scopus 로고    scopus 로고
    • Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment
    • Cheng S., Bobik T. Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment. J. Bacteriol. 2010, 192:5071-5080.
    • (2010) J. Bacteriol. , vol.192 , pp. 5071-5080
    • Cheng, S.1    Bobik, T.2
  • 54
    • 70449558136 scopus 로고    scopus 로고
    • The pentameric vertex proteins are necessary for the icosahedral carboxysome shell to function as a CO2 leakage barrier
    • Cai F., et al. The pentameric vertex proteins are necessary for the icosahedral carboxysome shell to function as a CO2 leakage barrier. PLoS ONE 2009, 4:e7521.
    • (2009) PLoS ONE , vol.4 , pp. e7521
    • Cai, F.1
  • 55
    • 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 E.M., Bobik T.A. Microcompartments for B12-dependent 1,2-propanediol degradation provide protection from DNA and cellular damage by a reactive metabolic intermediate. J. Bacteriol. 2008, 190:2966-2971.
    • (2008) J. Bacteriol. , vol.190 , pp. 2966-2971
    • Sampson, E.M.1    Bobik, T.A.2
  • 56
    • 33645964606 scopus 로고    scopus 로고
    • Conserving a volatile metabolite: a role for carboxysome-like organelles in Salmonella enterica
    • Penrod J.T., Roth J.R. Conserving a volatile metabolite: a role for carboxysome-like organelles in Salmonella enterica. J. Bacteriol. 2006, 188:2865-2874.
    • (2006) J. Bacteriol. , vol.188 , pp. 2865-2874
    • Penrod, J.T.1    Roth, J.R.2
  • 57
    • 84867515386 scopus 로고    scopus 로고
    • The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdu microcompartment of Salmonella enterica
    • Cheng S., et al. The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdu microcompartment of Salmonella enterica. PLoS ONE 2012, 7:e47144.
    • (2012) PLoS ONE , vol.7 , pp. e47144
    • Cheng, S.1
  • 58
    • 84880017088 scopus 로고    scopus 로고
    • Evidence that a metabolic microcompartment contains and recycles private cofactor pools
    • Huseby D.L., Roth J.R. Evidence that a metabolic microcompartment contains and recycles private cofactor pools. J. Bacteriol. 2013, 195:2864-2879.
    • (2013) J. Bacteriol. , vol.195 , pp. 2864-2879
    • Huseby, D.L.1    Roth, J.R.2
  • 59
    • 84883333320 scopus 로고    scopus 로고
    • The bacterial carbon-fixing organelle is formed by shell envelopment of preassembled cargo
    • Chen A.H., et al. The bacterial carbon-fixing organelle is formed by shell envelopment of preassembled cargo. PLoS ONE 2013, 8:e76127.
    • (2013) PLoS ONE , vol.8 , pp. e76127
    • Chen, A.H.1
  • 60
    • 77249103054 scopus 로고    scopus 로고
    • Structural basis of the oxidative activation of the carboxysomal gamma-carbonic anhydrase, CcmM
    • Peña K.L., et al. Structural basis of the oxidative activation of the carboxysomal gamma-carbonic anhydrase, CcmM. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:2455-2460.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2455-2460
    • Peña, K.L.1
  • 61
    • 84875723302 scopus 로고    scopus 로고
    • Cyanobacterial-based approaches to improving photosynthesis in plants
    • Zarzycki J., et al. Cyanobacterial-based approaches to improving photosynthesis in plants. J. Exp. Bot. 2013, 64:787-798.
    • (2013) J. Exp. Bot. , vol.64 , pp. 787-798
    • Zarzycki, J.1
  • 62
    • 84857065808 scopus 로고    scopus 로고
    • Isolation and characterization of the Prochlorococcus carboxysome reveal the presence of the novel shell protein CsoS1D
    • Roberts E.W., et al. Isolation and characterization of the Prochlorococcus carboxysome reveal the presence of the novel shell protein CsoS1D. J. Bacteriol. 2012, 194:787-795.
    • (2012) J. Bacteriol. , vol.194 , pp. 787-795
    • Roberts, E.W.1
  • 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 C.L., et al. Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:Cob(I)alamin adenosyltransferase gene. J. Bacteriol. 2001, 183:1577-1584.
    • (2001) J. Bacteriol. , vol.183 , pp. 1577-1584
    • Johnson, C.L.1
  • 64
    • 4344682568 scopus 로고    scopus 로고
    • The eutT gene of Salmonella enterica encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme
    • Buan N.R., et al. The eutT gene of Salmonella enterica encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme. J. Bacteriol. 2004, 186:5708-5714.
    • (2004) J. Bacteriol. , vol.186 , pp. 5708-5714
    • Buan, N.R.1
  • 65
    • 84898712690 scopus 로고    scopus 로고
    • Can the cyanobacterial carbon-concentrating mechanism increase photosynthesis in crop species? A theoretical analysis
    • McGrath J.M., Long S.P. Can the cyanobacterial carbon-concentrating mechanism increase photosynthesis in crop species? A theoretical analysis. Plant Physiol. 2014, 164:2247-2261.
    • (2014) Plant Physiol. , vol.164 , pp. 2247-2261
    • McGrath, J.M.1    Long, S.P.2
  • 66
    • 55849129963 scopus 로고    scopus 로고
    • Halothiobacillus neapolitanus carboxysomes sequester heterologous and chimeric RuBisCO species
    • Menon B.B., et al. Halothiobacillus neapolitanus carboxysomes sequester heterologous and chimeric RuBisCO species. PLoS ONE 2008, 3:e3570.
    • (2008) PLoS ONE , vol.3 , pp. e3570
    • Menon, B.B.1
  • 67
    • 0031856506 scopus 로고    scopus 로고
    • Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth
    • Baker S.H., et al. Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth. J. Bacteriol. 1998, 180:4133-4139.
    • (1998) J. Bacteriol. , vol.180 , pp. 4133-4139
    • Baker, S.H.1
  • 68
    • 84858009996 scopus 로고    scopus 로고
    • Engineered protein nano-compartments for targeted enzyme localization
    • Choudhary S., et al. Engineered protein nano-compartments for targeted enzyme localization. PLoS ONE 2012, 7:e33342.
    • (2012) PLoS ONE , vol.7 , pp. e33342
    • Choudhary, S.1
  • 69
    • 19844373000 scopus 로고    scopus 로고
    • Control of virus assembly: HK97 "Whiffleball" mutant capsids without pentons
    • Li Y., et al. Control of virus assembly: HK97 "Whiffleball" mutant capsids without pentons. J. Mol. Biol. 2005, 348:167-182.
    • (2005) J. Mol. Biol. , vol.348 , pp. 167-182
    • Li, Y.1
  • 70
    • 0026098298 scopus 로고
    • Structure of the herpes simplex virus capsid: effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids
    • Newcomb W., Brown J. Structure of the herpes simplex virus capsid: effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsids. J. Virol. 1991, 65:613-620.
    • (1991) J. Virol. , vol.65 , pp. 613-620
    • Newcomb, W.1    Brown, J.2
  • 71
    • 77952135283 scopus 로고    scopus 로고
    • Short N-terminal sequences package proteins into bacterial microcompartments
    • Fan C., et al. Short N-terminal sequences package proteins into bacterial microcompartments. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:7509-7514.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7509-7514
    • Fan, C.1
  • 72
    • 80053580487 scopus 로고    scopus 로고
    • The N-terminal region of the medium subunit (PduD) packages adenosylcobalamin-dependent diol dehydratase (PduCDE) into the Pdu microcompartment
    • Fan C., Bobik T.A. The N-terminal region of the medium subunit (PduD) packages adenosylcobalamin-dependent diol dehydratase (PduCDE) into the Pdu microcompartment. J. Bacteriol. 2011, 193:5623-5628.
    • (2011) J. Bacteriol. , vol.193 , pp. 5623-5628
    • Fan, C.1    Bobik, T.A.2
  • 73
    • 84866280237 scopus 로고    scopus 로고
    • Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments
    • Fan C., et al. Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:14995-15000.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 14995-15000
    • Fan, C.1
  • 74
    • 84886693636 scopus 로고    scopus 로고
    • A synthetic system for expression of components of a bacterial microcompartment
    • Sargent F., et al. A synthetic system for expression of components of a bacterial microcompartment. Microbiology 2013, 159:2427-2436.
    • (2013) Microbiology , vol.159 , pp. 2427-2436
    • Sargent, F.1
  • 75
    • 0028919805 scopus 로고
    • In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA
    • Zhao X., et al. In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA. Virology 1995, 207:486-494.
    • (1995) Virology , vol.207 , pp. 486-494
    • Zhao, X.1
  • 76
    • 84889604825 scopus 로고    scopus 로고
    • Biogenesis of a bacterial organelle: the carboxysome assembly pathway
    • Cameron J.C., et al. Biogenesis of a bacterial organelle: the carboxysome assembly pathway. Cell 2013, 155:1131-1140.
    • (2013) Cell , vol.155 , pp. 1131-1140
    • Cameron, J.C.1
  • 77
    • 38649141503 scopus 로고    scopus 로고
    • A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria
    • Cot S.S-W., et al. A multiprotein bicarbonate dehydration complex essential to carboxysome function in cyanobacteria. J. Bacteriol. 2008, 190:936-945.
    • (2008) J. Bacteriol. , vol.190 , pp. 936-945
    • Cot, S.S.-W.1
  • 79
    • 47649098600 scopus 로고    scopus 로고
    • Cooperativity and biological complexity
    • Whitty A. Cooperativity and biological complexity. Nature 2008, 4:435-439.
    • (2008) Nature , vol.4 , pp. 435-439
    • Whitty, A.1
  • 80
    • 6344260294 scopus 로고    scopus 로고
    • The power of two: protein dimerization in biology
    • Marianayagam N.J., et al. The power of two: protein dimerization in biology. Trends Biochem. Sci. 2004, 29:618-625.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 618-625
    • Marianayagam, N.J.1
  • 81
    • 84876272531 scopus 로고    scopus 로고
    • Protein complexes are under evolutionary selection to assemble via ordered pathways
    • Marsh J., et al. Protein complexes are under evolutionary selection to assemble via ordered pathways. Cell 2013, 153:461-470.
    • (2013) Cell , vol.153 , pp. 461-470
    • Marsh, J.1
  • 82
    • 17844373301 scopus 로고    scopus 로고
    • The N-terminal regions of β and γ subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase
    • Tobimatsu T., et al. The N-terminal regions of β and γ subunits lower the solubility of adenosylcobalamin-dependent diol dehydratase. Biosci. Biotechnol. Biochem. 2005, 69:455-462.
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 455-462
    • Tobimatsu, T.1
  • 83
    • 77956220623 scopus 로고    scopus 로고
    • Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates
    • Shibata N., et al. Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates. J. Biol. Chem. 2010, 285:26484-26493.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26484-26493
    • Shibata, N.1
  • 84
    • 0036436891 scopus 로고    scopus 로고
    • Purification, characterization and subunits identification of the diol dehydratase of Lactobacillus collinoides
    • Sauvageot N., et al. Purification, characterization and subunits identification of the diol dehydratase of Lactobacillus collinoides. Eur. J. Biochem. 2002, 269:5731-5737.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5731-5737
    • Sauvageot, N.1
  • 85
    • 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 N.A., et al. 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. 2003, 180:353-361.
    • (2003) Arch. Microbiol. , vol.180 , pp. 353-361
    • Leal, N.A.1
  • 86
    • 0033523989 scopus 로고    scopus 로고
    • Protein interaction maps for complete genomes based on gene fusion events
    • Enright A.J., et al. Protein interaction maps for complete genomes based on gene fusion events. Nature 1999, 402:86-90.
    • (1999) Nature , vol.402 , pp. 86-90
    • Enright, A.J.1
  • 87
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte E.M. Detecting protein function and protein-protein interactions from genome sequences. Science 1999, 285:751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1
  • 88
    • 74649083831 scopus 로고    scopus 로고
    • Organization, structure, and assembly of α-carboxysomes determined by electron cryotomography of intact cells
    • Iancu C.V., et al. Organization, structure, and assembly of α-carboxysomes determined by electron cryotomography of intact cells. J. Mol. Biol. 2010, 396:105-117.
    • (2010) J. Mol. Biol. , vol.396 , pp. 105-117
    • Iancu, C.V.1
  • 89
    • 0029847554 scopus 로고    scopus 로고
    • Selfish operons: horizontal transfer may drive the evolution of gene clusters
    • Lawrence J.G., Roth J.R. Selfish operons: horizontal transfer may drive the evolution of gene clusters. Genetics 1996, 143:1843-1860.
    • (1996) Genetics , vol.143 , pp. 1843-1860
    • Lawrence, J.G.1    Roth, J.R.2
  • 90
    • 0037173117 scopus 로고    scopus 로고
    • Evolutionary genomics of Salmonella: gene acquisitions revealed by microarray analysis
    • Porwollik S., et al. Evolutionary genomics of Salmonella: gene acquisitions revealed by microarray analysis. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:8956-8961.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 8956-8961
    • Porwollik, S.1
  • 91
    • 78049411009 scopus 로고    scopus 로고
    • Metabolomics of Mycobacterium tuberculosis reveals compartmentalized co-catabolism of carbon substrates
    • De Carvalho L.P.S., et al. Metabolomics of Mycobacterium tuberculosis reveals compartmentalized co-catabolism of carbon substrates. Chem. Biol. 2010, 17:1122-1131.
    • (2010) Chem. Biol. , vol.17 , pp. 1122-1131
    • De Carvalho, L.P.S.1
  • 92
    • 84855991265 scopus 로고    scopus 로고
    • Modularity of a carbon-fixing protein organelle
    • Bonacci W., et al. Modularity of a carbon-fixing protein organelle. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:478-483.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 478-483
    • Bonacci, W.1
  • 93
    • 84903317602 scopus 로고    scopus 로고
    • β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts
    • Lin M.T., et al. β-Carboxysomal proteins assemble into highly organized structures in Nicotiana chloroplasts. Plant J. 2014, 79:1-12.
    • (2014) Plant J. , vol.79 , pp. 1-12
    • Lin, M.T.1
  • 94
    • 35748946615 scopus 로고    scopus 로고
    • Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple RuBisCO complexes with carboxysomal proteins CcmM and CcaA
    • Long B.M., et al. Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple RuBisCO complexes with carboxysomal proteins CcmM and CcaA. J. Biol. Chem. 2007, 282:29323-29335.
    • (2007) J. Biol. Chem. , vol.282 , pp. 29323-29335
    • Long, B.M.1
  • 95
    • 77951980276 scopus 로고    scopus 로고
    • Functional cyanobacterial β-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein
    • Long B.M., et al. Functional cyanobacterial β-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein. Plant Physiol. 2010, 153:285-293.
    • (2010) Plant Physiol. , vol.153 , pp. 285-293
    • Long, B.M.1
  • 96
    • 84908510011 scopus 로고    scopus 로고
    • A faster RuBisCO with potential to increase photosynthesis in crops
    • Lin M.T., et al. A faster RuBisCO with potential to increase photosynthesis in crops. Nature 2014, 513:547-550.
    • (2014) Nature , vol.513 , pp. 547-550
    • Lin, M.T.1
  • 97
    • 79251599711 scopus 로고    scopus 로고
    • Identification and characterization of the propanediol utilization protein PduP of Lactobacillus reuteri for 3-hydroxypropionic acid production from glycerol
    • Luo L.H., et al. Identification and characterization of the propanediol utilization protein PduP of Lactobacillus reuteri for 3-hydroxypropionic acid production from glycerol. Appl. Microbiol. Biotechnol. 2011, 89:697-703.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 697-703
    • Luo, L.H.1
  • 98
    • 0037304408 scopus 로고    scopus 로고
    • Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins
    • Anantharaman V., et al. Emergence of diverse biochemical activities in evolutionarily conserved structural scaffolds of proteins. Curr. Opin. Chem. Biol. 2003, 7:12-20.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 12-20
    • Anantharaman, V.1
  • 99
    • 84881521788 scopus 로고    scopus 로고
    • The shells of BMC-type microcompartment organelles in bacteria
    • Yeates T.O., et al. The shells of BMC-type microcompartment organelles in bacteria. J. Mol. Microbiol. Biotechnol. 2013, 23:290-299.
    • (2013) J. Mol. Microbiol. Biotechnol. , vol.23 , pp. 290-299
    • Yeates, T.O.1
  • 100
    • 79251598466 scopus 로고    scopus 로고
    • Genetic analysis around aminoalcohol dehydrogenase gene of Rhodococcus erythropolis MAK154: a putative GntR transcription factor in transcriptional regulation
    • Urano N., et al. Genetic analysis around aminoalcohol dehydrogenase gene of Rhodococcus erythropolis MAK154: a putative GntR transcription factor in transcriptional regulation. Appl. Microbiol. Biotechnol. 2011, 89:739-746.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 739-746
    • Urano, N.1
  • 101
    • 33748632359 scopus 로고    scopus 로고
    • A novel NADP+-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols
    • Kataoka M., et al. A novel NADP+-dependent l-1-amino-2-propanol dehydrogenase from Rhodococcus erythropolis MAK154: a promising enzyme for the production of double chiral aminoalcohols. Lett. Appl. Microbiol. 2006, 43:430-435.
    • (2006) Lett. Appl. Microbiol. , vol.43 , pp. 430-435
    • Kataoka, M.1


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