메뉴 건너뛰기




Volumn 24, Issue 4, 2013, Pages 627-632

Engineering nanoscale protein compartments for synthetic organelles

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL PRODUCTION; METABOLIC PATHWAYS; MICRO-COMPARTMENTS; NANOSCALE PROTEINS; NOVEL FUELS; PROTEIN SHELLS; SMALL MOLECULES;

EID: 84880953448     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2012.11.012     Document Type: Review
Times cited : (52)

References (57)
  • 1
    • 77950863739 scopus 로고    scopus 로고
    • Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. coli
    • Moon T.S., Dueber J.E., Shiue E., Prather K.L.J. Use of modular, synthetic scaffolds for improved production of glucaric acid in engineered E. coli. Metab Eng 2010, 12:298-305.
    • (2010) Metab Eng , vol.12 , pp. 298-305
    • Moon, T.S.1    Dueber, J.E.2    Shiue, E.3    Prather, K.L.J.4
  • 4
    • 34547109848 scopus 로고    scopus 로고
    • Stochastic reaction-diffusion simulation of enzyme compartmentalization reveals improved catalytic efficiency for a synthetic metabolic pathway
    • Conrado R.J., Mansell T.J., Varner J.D., DeLisa M.P. Stochastic reaction-diffusion simulation of enzyme compartmentalization reveals improved catalytic efficiency for a synthetic metabolic pathway. Metab Eng 2007, 9:355-363.
    • (2007) Metab Eng , vol.9 , pp. 355-363
    • Conrado, R.J.1    Mansell, T.J.2    Varner, J.D.3    DeLisa, M.P.4
  • 7
  • 8
    • 77952754569 scopus 로고    scopus 로고
    • Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules
    • Minten I.J., Nolte R.J.M., Cornelissen J.J.L.M. Complex assembly behavior during the encapsulation of green fluorescent protein analogs in virus derived protein capsules. Macromol Biosci 2010, 10:539-545.
    • (2010) Macromol Biosci , vol.10 , pp. 539-545
    • Minten, I.J.1    Nolte, R.J.M.2    Cornelissen, J.J.L.M.3
  • 9
    • 79960923510 scopus 로고    scopus 로고
    • Genetically programmed in vivo packaging of protein cargo and its controlled release from bacteriophage P22
    • O'Neil A., Reichhardt C., Johnson B., Prevelige P.E., Douglas T. Genetically programmed in vivo packaging of protein cargo and its controlled release from bacteriophage P22. Angew Chem Int Ed 2011, 50:7425-7428.
    • (2011) Angew Chem Int Ed , vol.50 , pp. 7425-7428
    • O'Neil, A.1    Reichhardt, C.2    Johnson, B.3    Prevelige, P.E.4    Douglas, T.5
  • 12
    • 84855979791 scopus 로고    scopus 로고
    • Efficient in vitro encapsulation of protein cargo by an engineered protein container
    • Worsdorfer B., Pianowski Z., Hilvert D. Efficient in vitro encapsulation of protein cargo by an engineered protein container. J Am Chem Soc 2012, 134:909-911.
    • (2012) J Am Chem Soc , vol.134 , pp. 909-911
    • Worsdorfer, B.1    Pianowski, Z.2    Hilvert, D.3
  • 13
  • 14
    • 0033527924 scopus 로고    scopus 로고
    • Protein encapsulation within poly(ethylene glycol)-coated nanospheres. II. Controlled release properties
    • Quellec P., Gref R., Dellacherie E., Sommer F., Tran M.D., Alonso M.J. Protein encapsulation within poly(ethylene glycol)-coated nanospheres. II. Controlled release properties. J Biomed Mater Res 1999, 47:388-395.
    • (1999) J Biomed Mater Res , vol.47 , pp. 388-395
    • Quellec, P.1    Gref, R.2    Dellacherie, E.3    Sommer, F.4    Tran, M.D.5    Alonso, M.J.6
  • 16
    • 3042611512 scopus 로고    scopus 로고
    • Protein encapsulation in liposomes: efficiency depends on interactions between protein and phospholipid bilayer
    • Colletier J.P., Chaize B., Winterhalter M., Fournier D. Protein encapsulation in liposomes: efficiency depends on interactions between protein and phospholipid bilayer. BMC Biotechnol 2002, 2:9.
    • (2002) BMC Biotechnol , vol.2 , pp. 9
    • Colletier, J.P.1    Chaize, B.2    Winterhalter, M.3    Fournier, D.4
  • 19
    • 58149173410 scopus 로고    scopus 로고
    • Bacterial microcompartments: their properties and paradoxes
    • Cheng S., Liu Y., Crowley C.S., Yeates T.O., Bobik T.A. Bacterial microcompartments: their properties and paradoxes. Bioessays 2008, 30:1084-1095.
    • (2008) Bioessays , vol.30 , pp. 1084-1095
    • Cheng, S.1    Liu, Y.2    Crowley, C.S.3    Yeates, T.O.4    Bobik, T.A.5
  • 20
    • 77952945226 scopus 로고    scopus 로고
    • Bacterial microcompartment organelles: protein shell structure and evolution
    • Yeates T.O., Crowley C.S., Tanaka S. Bacterial microcompartment organelles: protein shell structure and evolution. Annu Rev Biophys 2010, 39:185-205.
    • (2010) Annu Rev Biophys , vol.39 , pp. 185-205
    • Yeates, T.O.1    Crowley, C.S.2    Tanaka, S.3
  • 21
    • 50849120064 scopus 로고    scopus 로고
    • Structure of the PduU shell protein from the Pdu microcompartment of Salmonella
    • Crowley C.S., Sawaya M.R., Bobik T.A., Yeates T.O. 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    Sawaya, M.R.2    Bobik, T.A.3    Yeates, T.O.4
  • 22
    • 78549246253 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of transport across the Salmonella enterica Pdu microcompartment shell
    • Crowley C.S., Cascio D., Sawaya M.R., Kopstein J.S., Bobik T.A., Yeates T.O. 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    Cascio, D.2    Sawaya, M.R.3    Kopstein, J.S.4    Bobik, T.A.5    Yeates, T.O.6
  • 23
    • 79952178155 scopus 로고    scopus 로고
    • Structure of PduT, a trimeric bacterial microcompartment protein with a 4Fe-4S cluster-binding site
    • Pang A., Warren M.J., Pickersgill R.W. 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    Warren, M.J.2    Pickersgill, R.W.3
  • 24
    • 67049117718 scopus 로고    scopus 로고
    • Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment
    • Sagermann M., Ohtaki A., Nikolakakis K. Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proc Natl Acad Sci USA 2009, 106:8883-8887.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8883-8887
    • Sagermann, M.1    Ohtaki, A.2    Nikolakakis, K.3
  • 25
    • 74849140487 scopus 로고    scopus 로고
    • Structure and mechanisms of a protein-based organelle in Escherichia coli
    • Tanaka S., Sawaya M.R., Yeates T.O. 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    Sawaya, M.R.2    Yeates, T.O.3
  • 29
    • 69949153137 scopus 로고    scopus 로고
    • Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C
    • Tsai Y., Sawaya M.R., Yeates T.O. Analysis of lattice-translocation disorder in the layered hexagonal structure of carboxysome shell protein CsoS1C. Acta Crystallogr D Biol Crystallogr 2009, 65:980-988.
    • (2009) Acta Crystallogr D Biol Crystallogr , vol.65 , pp. 980-988
    • Tsai, Y.1    Sawaya, M.R.2    Yeates, T.O.3
  • 30
    • 68949220061 scopus 로고    scopus 로고
    • Identification and structural analysis of a novel carboxysome shell protein with implications for metabolite transport
    • Klein M.G., Zwart P., Bagby S.C., Cai F., Chisholm S.W., Heinhorst S., Cannon G.C., Kerfeld C.A. 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    Zwart, P.2    Bagby, S.C.3    Cai, F.4    Chisholm, S.W.5    Heinhorst, S.6    Cannon, G.C.7    Kerfeld, C.A.8
  • 31
    • 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., Nikolakakis K., Sagermann M. 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    Nikolakakis, K.2    Sagermann, M.3
  • 33
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
    • Parsons J.B., Frank S., Bhella D., Liang M.Z., Prentice M.B., Mulvihill D.P., Warren M.J. 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    Frank, S.2    Bhella, D.3    Liang, M.Z.4    Prentice, M.B.5    Mulvihill, D.P.6    Warren, M.J.7
  • 34
    • 84861217493 scopus 로고    scopus 로고
    • The PduM protein is a structural component of the microcompartments involved in coenzyme B(12)-dependent 1,2-propanediol degradation by Salmonella enterica
    • Sinha S., Cheng S., Fan C., Bobik T.A. The PduM protein is a structural component of the microcompartments involved in coenzyme B(12)-dependent 1,2-propanediol degradation by Salmonella enterica. J Bacteriol 2012, 194:1912-1918.
    • (2012) J Bacteriol , vol.194 , pp. 1912-1918
    • Sinha, S.1    Cheng, S.2    Fan, C.3    Bobik, T.A.4
  • 35
    • 79952367508 scopus 로고    scopus 로고
    • Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella
    • Cheng S., Sinha S., Fan C., Liu Y., Bobik T.A. Genetic analysis of the protein shell of the microcompartments involved in coenzyme B12-dependent 1,2-propanediol degradation by Salmonella. J Bacteriol 2011, 193:1385-1392.
    • (2011) J Bacteriol , vol.193 , pp. 1385-1392
    • Cheng, S.1    Sinha, S.2    Fan, C.3    Liu, Y.4    Bobik, T.A.5
  • 38
    • 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
  • 39
    • 84861208627 scopus 로고    scopus 로고
    • Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly
    • Kinney J.N., Salmeen A., Cai F., Kerfeld C.A. Elucidating essential role of conserved carboxysomal protein CcmN reveals 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    Salmeen, A.2    Cai, F.3    Kerfeld, C.A.4
  • 40
    • 84866280237 scopus 로고    scopus 로고
    • Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments
    • Fan C., Cheng S., Sinha S., Bobik T.A. Interactions between the termini of lumen enzymes and shell proteins mediate enzyme encapsulation into bacterial microcompartments. Proc Natl Acad Sci USA 2012, 109:14995-15000.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 14995-15000
    • Fan, C.1    Cheng, S.2    Sinha, S.3    Bobik, T.A.4
  • 41
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage D.F., Afonso B., Chen A.H., Silver P.A. 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    Afonso, B.2    Chen, A.H.3    Silver, P.A.4
  • 42
    • 84856963458 scopus 로고    scopus 로고
    • Comparative analysis of carboxysome shell proteins
    • Kinney J.N., Axen S.D., Kerfeld C.A. Comparative analysis of carboxysome shell proteins. Photosynth Res 2011, 109:21-32.
    • (2011) Photosynth Res , vol.109 , pp. 21-32
    • Kinney, J.N.1    Axen, S.D.2    Kerfeld, C.A.3
  • 43
    • 58149456903 scopus 로고    scopus 로고
    • Insights from multiple structures of the shell proteins from the β-carboxysome
    • Tanaka S., Sawaya M.R., Phillips M., Yeates T.O. Insights from multiple structures of the shell proteins from the β-carboxysome. Protein Science 2009, 18:108-120.
    • (2009) Protein Science , vol.18 , pp. 108-120
    • Tanaka, S.1    Sawaya, M.R.2    Phillips, M.3    Yeates, T.O.4
  • 44
    • 0036178889 scopus 로고    scopus 로고
    • PduA is a shell protein of polyhedral organelles involved in coenzyme B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica serovar typhimurium LT2
    • Havemann G.D., Sampson E.M., Bobik T.A. PduA is a shell protein of polyhedral organelles involved in coenzyme B(12)-dependent degradation of 1,2-propanediol in Salmonella enterica serovar typhimurium LT2. J Bacteriol 2002, 184:1253-1261.
    • (2002) J Bacteriol , vol.184 , pp. 1253-1261
    • Havemann, G.D.1    Sampson, E.M.2    Bobik, T.A.3
  • 46
    • 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 S.H., Lorbach S.C., Rodriguez-Buey M., Williams D.S., Aldrich H.C., Shively J.M. The correlation of the gene csoS2 of the carboxysome operon with two polypeptides of the carboxysome in thiobacillus neapolitanus. Arch Microbiol 1999, 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    Shively, J.M.6
  • 47
    • 0034038419 scopus 로고    scopus 로고
    • Identification and localization of the carboxysome peptide Csos3 and its corresponding gene in Thiobacillus neapolitanus
    • Baker S.H., Williams D.S., Aldrich H.C., Gambrell A.C., Shively J.M. Identification and localization of the carboxysome peptide Csos3 and its corresponding gene in Thiobacillus neapolitanus. Arch Microbiol 2000, 173:278-283.
    • (2000) Arch Microbiol , vol.173 , pp. 278-283
    • Baker, S.H.1    Williams, D.S.2    Aldrich, H.C.3    Gambrell, A.C.4    Shively, J.M.5
  • 48
    • 84865191456 scopus 로고    scopus 로고
    • Structural determinants of the outer shell of beta-carboxysomes in Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL
    • Rae B.D., Long B.M., Badger M.R., Price G.D. Structural determinants of the outer shell of beta-carboxysomes in Synechococcus elongatus PCC 7942: roles for CcmK2, K3-K4, CcmO, and CcmL. PLoS One 2012, 7:e43871.
    • (2012) PLoS One , vol.7
    • Rae, B.D.1    Long, B.M.2    Badger, M.R.3    Price, G.D.4
  • 50
    • 0015816557 scopus 로고
    • Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus
    • Shively J.M., Ball F., Brown D.H., Saunders R.E. Functional organelles in prokaryotes: polyhedral inclusions (carboxysomes) of Thiobacillus neapolitanus. Science 1973, 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
  • 51
    • 0042993885 scopus 로고
    • Polyhedral Bodies and Ribulose 1,5-Diphosphate Carboxylase of Blue-Green-Alga Anabaena-Cylindrica
    • Codd G.A., Stewart W.D.P. Polyhedral Bodies and Ribulose 1,5-Diphosphate Carboxylase of Blue-Green-Alga Anabaena-Cylindrica. Planta 1976, 130:323-326.
    • (1976) Planta , vol.130 , pp. 323-326
    • Codd, G.A.1    Stewart, W.D.P.2
  • 52
    • 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
  • 53
    • 35748946615 scopus 로고    scopus 로고
    • Analysis of carboxysomes from Synechococcus PCC 7942 reveals multiple Rubisco complexes with carboxysomal proteins CcmM and CcaA
    • Long B.M., Badger M.R., Whitney S.M., Price G.D. Analysis of carboxysomes from Synechococcus PCC 7942 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    Badger, M.R.2    Whitney, S.M.3    Price, G.D.4
  • 54
    • 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 G.D., Bobik T.A. Protein content of polyhedral organelles involved in coenzyme B12-dependent degradation of 1,2-propanediol in Salmonella enterica serovar Typhimurium LT2. J Bacteriol 2003, 185:5086-5095.
    • (2003) J Bacteriol , vol.185 , pp. 5086-5095
    • Havemann, G.D.1    Bobik, T.A.2
  • 55
    • 77951980276 scopus 로고    scopus 로고
    • Functional cyanobacterial beta-carboxysomes have an absolute requirement for both long and short forms of the CcmM protein
    • Long B.M., Tucker L., Badger M.R., Price G.D. Functional cyanobacterial beta-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    Tucker, L.2    Badger, M.R.3    Price, G.D.4
  • 56
    • 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., Fan C., Sinha S., Bobik T.A. 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
    • Cheng, S.1    Fan, C.2    Sinha, S.3    Bobik, T.A.4
  • 57
    • 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.A. 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.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.