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Volumn 36, Issue 5, 2012, Pages 1005-1022

Compartmentalization and spatiotemporal organization of macromolecules in bacteria

Author keywords

Cell compartmentalization; Cell polarity; Localized translation; Polar cues; RNA targeting; Subcellular organization

Indexed keywords

BACTERIAL DNA; BACTERIAL PROTEIN; BACTERIAL RNA; MEMBRANE LIPID; MESSENGER RNA;

EID: 84864408193     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1111/j.1574-6976.2012.00348.x     Document Type: Review
Times cited : (45)

References (155)
  • 1
    • 0026628961 scopus 로고
    • Polar localization of a bacterial chemoreceptor
    • Alley MR, Maddock JR & Shapiro L (1992) Polar localization of a bacterial chemoreceptor. Genes Dev 6: 825-836.
    • (1992) Genes Dev , vol.6 , pp. 825-836
    • Alley, M.R.1    Maddock, J.R.2    Shapiro, L.3
  • 3
    • 84862505674 scopus 로고    scopus 로고
    • The compartmentalized vessel: the bacterial cell as a model for subcellular organization (a tale of two studies)
    • Amster-Choder O (2011) The compartmentalized vessel: the bacterial cell as a model for subcellular organization (a tale of two studies). Cell Logist 1: 77-81.
    • (2011) Cell Logist , vol.1 , pp. 77-81
    • Amster-Choder, O.1
  • 4
    • 84862765893 scopus 로고    scopus 로고
    • Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells
    • Bakshi S, Siryaporn A, Goulian M & Weisshaar JC (2012) Superresolution imaging of ribosomes and RNA polymerase in live Escherichia coli cells. Mol Microbiol 85: 21-38.
    • (2012) Mol Microbiol , vol.85 , pp. 21-38
    • Bakshi, S.1    Siryaporn, A.2    Goulian, M.3    Weisshaar, J.C.4
  • 6
    • 0033519623 scopus 로고    scopus 로고
    • Localization and anchoring of mRNA in budding yeast
    • Beach DL, Salmon ED & Bloom K (1999) Localization and anchoring of mRNA in budding yeast. Curr Biol 9: 569-578.
    • (1999) Curr Biol , vol.9 , pp. 569-578
    • Beach, D.L.1    Salmon, E.D.2    Bloom, K.3
  • 7
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • Bendezu FO, Hale CA, Bernhardt TG & de Boer PA (2009) RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J 28: 193-204.
    • (2009) EMBO J , vol.28 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    de Boer, P.A.4
  • 8
    • 0037462540 scopus 로고    scopus 로고
    • RacA, a bacterial protein that anchors chromosomes to the cell poles
    • Ben-Yehuda S, Rudner DZ & Losick R (2003) RacA, a bacterial protein that anchors chromosomes to the cell poles. Science 299: 532-536.
    • (2003) Science , vol.299 , pp. 532-536
    • Ben-Yehuda, S.1    Rudner, D.Z.2    Losick, R.3
  • 9
    • 0024966540 scopus 로고
    • Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
    • Bernstein HD, Poritz MA, Strub K, Hoben PJ, Brenner S & Walter P (1989) Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle. Nature 340: 482-486.
    • (1989) Nature , vol.340 , pp. 482-486
    • Bernstein, H.D.1    Poritz, M.A.2    Strub, K.3    Hoben, P.J.4    Brenner, S.5    Walter, P.6
  • 10
    • 0037162469 scopus 로고    scopus 로고
    • Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays
    • Bernstein JA, Khodursky AB, Lin PH, Lin-Chao S & Cohen SN (2002) Global analysis of mRNA decay and abundance in Escherichia coli at single-gene resolution using two-color fluorescent DNA microarrays. P Natl Acad Sci USA 99: 9697-9702.
    • (2002) P Natl Acad Sci USA , vol.99 , pp. 9697-9702
    • Bernstein, J.A.1    Khodursky, A.B.2    Lin, P.H.3    Lin-Chao, S.4    Cohen, S.N.5
  • 12
    • 0026059127 scopus 로고
    • FtsZ ring structure associated with division in Escherichia coli
    • Bi EF & Lutkenhaus J (1991) FtsZ ring structure associated with division in Escherichia coli. Nature 354: 161-164.
    • (1991) Nature , vol.354 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 13
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork P, Sander C & Valencia A (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. P Natl Acad Sci USA 89: 7290-7294.
    • (1992) P Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 15
    • 56749185690 scopus 로고    scopus 로고
    • A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD
    • Bramkamp M, Emmins R, Weston L, Donovan C, Daniel RA & Errington J (2008) A novel component of the division-site selection system of Bacillus subtilis and a new mode of action for the division inhibitor MinCD. Mol Microbiol 70: 1556-1569.
    • (2008) Mol Microbiol , vol.70 , pp. 1556-1569
    • Bramkamp, M.1    Emmins, R.2    Weston, L.3    Donovan, C.4    Daniel, R.A.5    Errington, J.6
  • 16
    • 79957469880 scopus 로고    scopus 로고
    • Analysis of RNA localization and metabolism in single live bacterial cells: achievements and challenges
    • Broude NE (2011) Analysis of RNA localization and metabolism in single live bacterial cells: achievements and challenges. Mol Microbiol 80: 1137-1147.
    • (2011) Mol Microbiol , vol.80 , pp. 1137-1147
    • Broude, N.E.1
  • 18
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez R, Formstone A, Li Y, Ehrlich SD, Noirot P & Errington J (2006) Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell 11: 399-409.
    • (2006) Dev Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5    Errington, J.6
  • 19
    • 59249088584 scopus 로고    scopus 로고
    • Polar localization of virulence-related Esx-1 secretion in mycobacteria
    • Carlsson F, Joshi SA, Rangell L & Brown EJ (2009) Polar localization of virulence-related Esx-1 secretion in mycobacteria. PLoS Pathog 5: e1000285.
    • (2009) PLoS Pathog , vol.5
    • Carlsson, F.1    Joshi, S.A.2    Rangell, L.3    Brown, E.J.4
  • 20
    • 34548524489 scopus 로고    scopus 로고
    • Spatial complexity and control of a bacterial cell cycle
    • Collier J & Shapiro L (2007) Spatial complexity and control of a bacterial cell cycle. Curr Opin Biotechnol 18: 333-340.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 333-340
    • Collier, J.1    Shapiro, L.2
  • 21
    • 77953509169 scopus 로고    scopus 로고
    • Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa
    • Cowles KN & Gitai Z (2010) Surface association and the MreB cytoskeleton regulate pilus production, localization and function in Pseudomonas aeruginosa. Mol Microbiol 76: 1411-1426.
    • (2010) Mol Microbiol , vol.76 , pp. 1411-1426
    • Cowles, K.N.1    Gitai, Z.2
  • 22
    • 33751213557 scopus 로고    scopus 로고
    • Pathways for mRNA localization in the cytoplasm
    • Czaplinski K & Singer RH (2006) Pathways for mRNA localization in the cytoplasm. Trends Biochem Sci 31: 687-693.
    • (2006) Trends Biochem Sci , vol.31 , pp. 687-693
    • Czaplinski, K.1    Singer, R.H.2
  • 23
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell
    • Daniel RA & Errington J (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113: 767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 24
    • 0037379474 scopus 로고    scopus 로고
    • Localization of rRNA synthesis in Bacillus subtilis: characterization of loci involved in transcription focus formation
    • Davies KM & Lewis PJ (2003) Localization of rRNA synthesis in Bacillus subtilis: characterization of loci involved in transcription focus formation. J Bacteriol 185: 2346-2353.
    • (2003) J Bacteriol , vol.185 , pp. 2346-2353
    • Davies, K.M.1    Lewis, P.J.2
  • 25
    • 78649646536 scopus 로고    scopus 로고
    • Advances in understanding E. coli cell fission
    • de Boer PA (2010) Advances in understanding E. coli cell fission. Curr Opin Microbiol 13: 730-737.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 730-737
    • de Boer, P.A.1
  • 26
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • Defeu Soufo HJ & Graumann PL (2004) Dynamic movement of actin-like proteins within bacterial cells. EMBO Rep 5: 789-794.
    • (2004) EMBO Rep , vol.5 , pp. 789-794
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 27
    • 42049092081 scopus 로고    scopus 로고
    • The mechanisms of carbon catabolite repression in bacteria
    • Deutscher J (2008) The mechanisms of carbon catabolite repression in bacteria. Curr Opin Microbiol 11: 87-93.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 87-93
    • Deutscher, J.1
  • 28
    • 77949512479 scopus 로고    scopus 로고
    • Cellular electron microscopy imaging reveals the localization of the Hfq protein close to the bacterial membrane
    • Diestra E, Cayrol B, Arluison V & Risco C (2009) Cellular electron microscopy imaging reveals the localization of the Hfq protein close to the bacterial membrane. PLoS ONE 4: e8301.
    • (2009) PLoS ONE , vol.4
    • Diestra, E.1    Cayrol, B.2    Arluison, V.3    Risco, C.4
  • 29
    • 29344476196 scopus 로고    scopus 로고
    • The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus
    • Divakaruni AV, Loo RR, Xie Y, Loo JA & Gober JW (2005) The cell-shape protein MreC interacts with extracytoplasmic proteins including cell wall assembly complexes in Caulobacter crescentus. P Natl Acad Sci USA 102: 18602-18607.
    • (2005) P Natl Acad Sci USA , vol.102 , pp. 18602-18607
    • Divakaruni, A.V.1    Loo, R.R.2    Xie, Y.3    Loo, J.A.4    Gober, J.W.5
  • 30
    • 34548677525 scopus 로고    scopus 로고
    • The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes
    • Divakaruni AV, Baida C, White CL & Gober JW (2007) The cell shape proteins MreB and MreC control cell morphogenesis by positioning cell wall synthetic complexes. Mol Microbiol 66: 174-188.
    • (2007) Mol Microbiol , vol.66 , pp. 174-188
    • Divakaruni, A.V.1    Baida, C.2    White, C.L.3    Gober, J.W.4
  • 32
    • 78349254943 scopus 로고    scopus 로고
    • Subcellular communication through RNA transport and localized protein synthesis
    • Donnelly CJ, Fainzilber M & Twiss JL (2010) Subcellular communication through RNA transport and localized protein synthesis. Traffic 11: 1498-1505.
    • (2010) Traffic , vol.11 , pp. 1498-1505
    • Donnelly, C.J.1    Fainzilber, M.2    Twiss, J.L.3
  • 33
    • 67650708496 scopus 로고    scopus 로고
    • Characterization and subcellular localization of a bacterial flotillin homologue
    • Donovan C & Bramkamp M (2009) Characterization and subcellular localization of a bacterial flotillin homologue. Microbiology 155: 1786-1799.
    • (2009) Microbiology , vol.155 , pp. 1786-1799
    • Donovan, C.1    Bramkamp, M.2
  • 34
    • 84864021780 scopus 로고    scopus 로고
    • DivIVA-mediated polar localization of ComN, a post-transcriptional regulator of B. subtilis
    • Dos Santos VT, Bisson-Filho AW & Gueiros-Filho FJ (2012) DivIVA-mediated polar localization of ComN, a post-transcriptional regulator of B. subtilis. J Bacteriol, 194: 3661-3669.
    • (2012) J Bacteriol , vol.194 , pp. 3661-3669
    • Dos Santos, V.T.1    Bisson-Filho, A.W.2    Gueiros-Filho, F.J.3
  • 35
    • 77955867901 scopus 로고    scopus 로고
    • Cellular polarity in prokaryotic organisms
    • Dworkin J (2009) Cellular polarity in prokaryotic organisms. Cold Spring Harb Perspect Biol 1: a003368.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Dworkin, J.1
  • 36
  • 37
    • 33847674876 scopus 로고    scopus 로고
    • Exploration into the spatial and temporal mechanisms of bacterial polarity
    • Ebersbach G & Jacobs-Wagner C (2007) Exploration into the spatial and temporal mechanisms of bacterial polarity. Trends Microbiol 15: 101-108.
    • (2007) Trends Microbiol , vol.15 , pp. 101-108
    • Ebersbach, G.1    Jacobs-Wagner, C.2
  • 38
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE & Osawa M (2010) FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol Mol Biol Rev 74: 504-528.
    • (2010) Microbiol Mol Biol Rev , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 40
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge RM, Divakaruni AV & Gober JW (2004) MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus. Mol Microbiol 51: 1321-1332.
    • (2004) Mol Microbiol , vol.51 , pp. 1321-1332
    • Figge, R.M.1    Divakaruni, A.V.2    Gober, J.W.3
  • 41
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis
    • Garner EC, Bernard R, Wang W, Zhuang X, Rudner DZ & Mitchison T (2011) Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333: 222-225.
    • (2011) Science , vol.333 , pp. 222-225
    • Garner, E.C.1    Bernard, R.2    Wang, W.3    Zhuang, X.4    Rudner, D.Z.5    Mitchison, T.6
  • 42
    • 0020413603 scopus 로고
    • Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
    • Gilmore R, Walter P & Blobel G (1982) Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J Cell Biol 95: 470-477.
    • (1982) J Cell Biol , vol.95 , pp. 470-477
    • Gilmore, R.1    Walter, P.2    Blobel, G.3
  • 43
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine cell polarity in bacteria
    • Gitai Z, Dye N & Shapiro L (2004) An actin-like gene can determine cell polarity in bacteria. P Natl Acad Sci USA 101: 8643-8648.
    • (2004) P Natl Acad Sci USA , vol.101 , pp. 8643-8648
    • Gitai, Z.1    Dye, N.2    Shapiro, L.3
  • 45
    • 0027191844 scopus 로고
    • Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement
    • Goldberg MB, Barzu O, Parsot C & Sansonetti PJ (1993) Unipolar localization and ATPase activity of IcsA, a Shigella flexneri protein involved in intracellular movement. J Bacteriol 175: 2189-2196.
    • (1993) J Bacteriol , vol.175 , pp. 2189-2196
    • Goldberg, M.B.1    Barzu, O.2    Parsot, C.3    Sansonetti, P.J.4
  • 46
    • 3843126332 scopus 로고    scopus 로고
    • RNA dynamics in live Escherichia coli cells
    • Golding I & Cox EC (2004) RNA dynamics in live Escherichia coli cells. P Natl Acad Sci USA 101: 11310-11315.
    • (2004) P Natl Acad Sci USA , vol.101 , pp. 11310-11315
    • Golding, I.1    Cox, E.C.2
  • 49
    • 0030597337 scopus 로고    scopus 로고
    • Plasmids for ectopic integration in Bacillus subtilis
    • Guerout-Fleury AM, Frandsen N & Stragier P (1996) Plasmids for ectopic integration in Bacillus subtilis. Gene 180: 57-61.
    • (1996) Gene , vol.180 , pp. 57-61
    • Guerout-Fleury, A.M.1    Frandsen, N.2    Stragier, P.3
  • 50
    • 85041133119 scopus 로고    scopus 로고
    • Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle
    • Herskovits AA & Bibi E (2000) Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle. P Natl Acad Sci USA 97: 4621-4626.
    • (2000) P Natl Acad Sci USA , vol.97 , pp. 4621-4626
    • Herskovits, A.A.1    Bibi, E.2
  • 51
    • 74349123957 scopus 로고    scopus 로고
    • Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli
    • Hsieh CW, Lin TY, Lai HM, Lin CC, Hsieh TS & Shih YL (2010) Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli. Mol Microbiol 75: 499-512.
    • (2010) Mol Microbiol , vol.75 , pp. 499-512
    • Hsieh, C.W.1    Lin, T.Y.2    Lai, H.M.3    Lin, C.C.4    Hsieh, T.S.5    Shih, Y.L.6
  • 52
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu CD, Chinenov Y & Kerppola TK (2002) Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol Cell 9: 789-798.
    • (2002) Mol Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 53
    • 83355166257 scopus 로고    scopus 로고
    • A growing family: the expanding universe of the bacterial cytoskeleton
    • Ingerson-Mahar M & Gitai Z (2012) A growing family: the expanding universe of the bacterial cytoskeleton. FEMS Microbiol Rev 36: 256-267.
    • (2012) FEMS Microbiol Rev , vol.36 , pp. 256-267
    • Ingerson-Mahar, M.1    Gitai, Z.2
  • 54
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • Ingledew WJ & Poole RK (1984) The respiratory chains of Escherichia coli. Microbiol Rev 48: 222-271.
    • (1984) Microbiol Rev , vol.48 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2
  • 56
    • 5644264779 scopus 로고    scopus 로고
    • Recent advances on the development of bacterial poles
    • Janakiraman A & Goldberg MB (2004) Recent advances on the development of bacterial poles. Trends Microbiol 12: 518-525.
    • (2004) Trends Microbiol , vol.12 , pp. 518-525
    • Janakiraman, A.1    Goldberg, M.B.2
  • 57
    • 38549164727 scopus 로고    scopus 로고
    • Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella
    • Jaumouille V, Francetic O, Sansonetti PJ & Tran Van Nhieu G (2008) Cytoplasmic targeting of IpaC to the bacterial pole directs polar type III secretion in Shigella. EMBO J 27: 447-457.
    • (2008) EMBO J , vol.27 , pp. 447-457
    • Jaumouille, V.1    Francetic, O.2    Sansonetti, P.J.3    Tran Van Nhieu, G.4
  • 58
    • 0021066596 scopus 로고
    • Localization of actin messenger RNA during early ascidian development
    • Jeffery WR, Tomlinson CR & Brodeur RD (1983) Localization of actin messenger RNA during early ascidian development. Dev Biol 99: 408-417.
    • (1983) Dev Biol , vol.99 , pp. 408-417
    • Jeffery, W.R.1    Tomlinson, C.R.2    Brodeur, R.D.3
  • 59
    • 80455131023 scopus 로고    scopus 로고
    • The long journey: actin on the road to pro- and eukaryotic cells
    • Jockusch BM & Graumann PL (2011) The long journey: actin on the road to pro- and eukaryotic cells. Rev Physiol Biochem Pharmacol 161: 67-85.
    • (2011) Rev Physiol Biochem Pharmacol , vol.161 , pp. 67-85
    • Jockusch, B.M.1    Graumann, P.L.2
  • 60
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones LJ, Carballido-Lopez R & Errington J (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104: 913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 61
    • 23844435922 scopus 로고    scopus 로고
    • Spatial location and requirements for the assembly of the Agrobacterium tumefaciens type IV secretion apparatus
    • Judd PK, Kumar RB & Das A (2005) Spatial location and requirements for the assembly of the Agrobacterium tumefaciens type IV secretion apparatus. P Natl Acad Sci USA 102: 11498-11503.
    • (2005) P Natl Acad Sci USA , vol.102 , pp. 11498-11503
    • Judd, P.K.1    Kumar, R.B.2    Das, A.3
  • 62
    • 0025813137 scopus 로고
    • Universal promoter for gene expression without cloning: expression-PCR
    • Kain KC, Orlandi PA & Lanar DE (1991) Universal promoter for gene expression without cloning: expression-PCR. Biotechniques 10: 366-374.
    • (1991) Biotechniques , vol.10 , pp. 366-374
    • Kain, K.C.1    Orlandi, P.A.2    Lanar, D.E.3
  • 63
    • 0021766488 scopus 로고
    • Dissipation of membrane potential of Escherichia coli cells induced by macromolecular polylysine
    • Katsu T, Tsuchiya T & Fujita Y (1984) Dissipation of membrane potential of Escherichia coli cells induced by macromolecular polylysine. Biochem Biophys Res Commun 122: 401-406.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 401-406
    • Katsu, T.1    Tsuchiya, T.2    Fujita, Y.3
  • 64
    • 54249138245 scopus 로고    scopus 로고
    • The RNase E of Escherichia coli is a membrane-binding protein
    • Khemici V, Poljak L, Luisi BF & Carpousis AJ (2008) The RNase E of Escherichia coli is a membrane-binding protein. Mol Microbiol 70: 799-813.
    • (2008) Mol Microbiol , vol.70 , pp. 799-813
    • Khemici, V.1    Poljak, L.2    Luisi, B.F.3    Carpousis, A.J.4
  • 65
    • 80054892595 scopus 로고    scopus 로고
    • Poles apart: prokaryotic polar organelles and their spatial regulation
    • Kirkpatrick CL & Viollier PH (2010) Poles apart: prokaryotic polar organelles and their spatial regulation. Cold Spring Harb Perspect Biol 3: a006809.
    • (2010) Cold Spring Harb Perspect Biol , vol.3
    • Kirkpatrick, C.L.1    Viollier, P.H.2
  • 66
    • 0027362779 scopus 로고
    • Isoform-specific 3′-untranslated sequences sort alpha-cardiac and beta-cytoplasmic actin messenger RNAs to different cytoplasmic compartments
    • Kislauskis EH, Li Z, Singer RH & Taneja KL (1993) Isoform-specific 3′-untranslated sequences sort alpha-cardiac and beta-cytoplasmic actin messenger RNAs to different cytoplasmic compartments. J Cell Biol 123: 165-172.
    • (1993) J Cell Biol , vol.123 , pp. 165-172
    • Kislauskis, E.H.1    Li, Z.2    Singer, R.H.3    Taneja, K.L.4
  • 67
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK
    • Komeili A, Li Z, Newman DK & Jensen GJ (2006) Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311: 242-245.
    • (2006) Science , vol.311 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 68
    • 0032473890 scopus 로고    scopus 로고
    • LNA (locked nucleic acids): synthesis of the adenine, cytosine, guanine, 5-methylcytosine, thymine and uracil bicyclonucleoside monomers, oligomerisation, and unprecedented nucleic acid recognition
    • Koshkin AA, Singh SK, Nielsen P, Rajwanshi VK, Kumar R, Meldgaard M, Olsen CE & Wengel J (1998) LNA (locked nucleic acids): synthesis of the adenine, cytosine, guanine, 5-methylcytosine, thymine and uracil bicyclonucleoside monomers, oligomerisation, and unprecedented nucleic acid recognition. Tetrahedron 54: 3607-3630.
    • (1998) Tetrahedron , vol.54 , pp. 3607-3630
    • Koshkin, A.A.1    Singh, S.K.2    Nielsen, P.3    Rajwanshi, V.K.4    Kumar, R.5    Meldgaard, M.6    Olsen, C.E.7    Wengel, J.8
  • 69
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse T, Bork-Jensen J & Gerdes K (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol 55: 78-89.
    • (2005) Mol Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 70
    • 0016760859 scopus 로고
    • Direct association of messenger RNA with microsomal membranes in human diploid fibroblasts
    • Lande MA, Adesnik M, Sumida M, Tashiro Y & Sabatini DD (1975) Direct association of messenger RNA with microsomal membranes in human diploid fibroblasts. J Cell Biol 65: 513-528.
    • (1975) J Cell Biol , vol.65 , pp. 513-528
    • Lande, M.A.1    Adesnik, M.2    Sumida, M.3    Tashiro, Y.4    Sabatini, D.D.5
  • 71
    • 68249141791 scopus 로고    scopus 로고
    • Localisation of DivIVA by targeting to negatively curved membranes
    • Lenarcic R, Halbedel S, Visser L et al. (2009) Localisation of DivIVA by targeting to negatively curved membranes. EMBO J 28: 2272-2282.
    • (2009) EMBO J , vol.28 , pp. 2272-2282
    • Lenarcic, R.1    Halbedel, S.2    Visser, L.3
  • 72
    • 79960396323 scopus 로고    scopus 로고
    • Temporal and spatial oscillations in bacteria
    • Lenz P & Sogaard-Andersen L (2011) Temporal and spatial oscillations in bacteria. Nat Rev Microbiol 9: 565-577.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 565-577
    • Lenz, P.1    Sogaard-Andersen, L.2
  • 73
    • 0034651795 scopus 로고    scopus 로고
    • Compartmentalization of transcription and translation in Bacillus subtilis
    • Lewis PJ, Thaker SD & Errington J (2000) Compartmentalization of transcription and translation in Bacillus subtilis. EMBO J 19: 710-718.
    • (2000) EMBO J , vol.19 , pp. 710-718
    • Lewis, P.J.1    Thaker, S.D.2    Errington, J.3
  • 74
    • 0036340805 scopus 로고    scopus 로고
    • Hydrodynamic coupling in diffusion of quasi-one-dimensional Brownian particles
    • Lin BH, Cui BX, Lee JH & Yu J (2002) Hydrodynamic coupling in diffusion of quasi-one-dimensional Brownian particles. Europhys Lett 57: 724-730.
    • (2002) Europhys Lett , vol.57 , pp. 724-730
    • Lin, B.H.1    Cui, B.X.2    Lee, J.H.3    Yu, J.4
  • 75
    • 77956292192 scopus 로고    scopus 로고
    • Functional microdomains in bacterial membranes
    • Lopez D & Kolter R (2010) Functional microdomains in bacterial membranes. Genes Dev 24: 1893-1902.
    • (2010) Genes Dev , vol.24 , pp. 1893-1902
    • Lopez, D.1    Kolter, R.2
  • 76
    • 78149280885 scopus 로고    scopus 로고
    • Spatial and temporal organization of the E. coli PTS components
    • Lopian L, Elisha Y, Nussbaum-Shochat A & Amster-Choder O (2010) Spatial and temporal organization of the E. coli PTS components. EMBO J 29: 3630-3645.
    • (2010) EMBO J , vol.29 , pp. 3630-3645
    • Lopian, L.1    Elisha, Y.2    Nussbaum-Shochat, A.3    Amster-Choder, O.4
  • 77
    • 0029616573 scopus 로고
    • Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli
    • Lux R, Jahreis K, Bettenbrock K, Parkinson JS & Lengeler JW (1995) Coupling the phosphotransferase system and the methyl-accepting chemotaxis protein-dependent chemotaxis signaling pathways of Escherichia coli. P Natl Acad Sci USA 92: 11583-11587.
    • (1995) P Natl Acad Sci USA , vol.92 , pp. 11583-11587
    • Lux, R.1    Jahreis, K.2    Bettenbrock, K.3    Parkinson, J.S.4    Lengeler, J.W.5
  • 78
    • 0029851154 scopus 로고    scopus 로고
    • Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein
    • Ma X, Ehrhardt DW & Margolin W (1996) Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. P Natl Acad Sci USA 93: 12998-13003.
    • (1996) P Natl Acad Sci USA , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 80
    • 78649658087 scopus 로고    scopus 로고
    • Bridging cell wall biosynthesis and bacterial morphogenesis
    • Mattei PJ, Neves D & Dessen A (2010) Bridging cell wall biosynthesis and bacterial morphogenesis. Curr Opin Struct Biol 20: 749-755.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 749-755
    • Mattei, P.J.1    Neves, D.2    Dessen, A.3
  • 81
    • 75049084936 scopus 로고    scopus 로고
    • Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA
    • Mauriello EM, Mouhamar F, Nan B, Ducret A, Dai D, Zusman DR & Mignot T (2010) Bacterial motility complexes require the actin-like protein, MreB and the Ras homologue, MglA. EMBO J 29: 315-326.
    • (2010) EMBO J , vol.29 , pp. 315-326
    • Mauriello, E.M.1    Mouhamar, F.2    Nan, B.3    Ducret, A.4    Dai, D.5    Zusman, D.R.6    Mignot, T.7
  • 82
    • 54049136408 scopus 로고    scopus 로고
    • Mutual effects of MinD-membrane interaction: I. Changes in the membrane properties induced by MinD binding
    • Mazor S, Regev T, Mileykovskaya E, Margolin W, Dowhan W & Fishov I (2008a) Mutual effects of MinD-membrane interaction: I. Changes in the membrane properties induced by MinD binding. Biochim Biophys Acta 1778: 2496-2504.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2496-2504
    • Mazor, S.1    Regev, T.2    Mileykovskaya, E.3    Margolin, W.4    Dowhan, W.5    Fishov, I.6
  • 83
    • 54049088085 scopus 로고    scopus 로고
    • Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding
    • Mazor S, Regev T, Mileykovskaya E, Margolin W, Dowhan W & Fishov I (2008b) Mutual effects of MinD-membrane interaction: II. Domain structure of the membrane enhances MinD binding. Biochim Biophys Acta 1778: 2505-2511.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 2505-2511
    • Mazor, S.1    Regev, T.2    Mileykovskaya, E.3    Margolin, W.4    Dowhan, W.5    Fishov, I.6
  • 84
    • 0344687406 scopus 로고    scopus 로고
    • Protein fragment complementation strategies for biochemical network mapping
    • Michnick SW (2003) Protein fragment complementation strategies for biochemical network mapping. Curr Opin Biotechnol 14: 610-617.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 610-617
    • Michnick, S.W.1
  • 85
    • 70349523247 scopus 로고    scopus 로고
    • Cardiolipin membrane domains in prokaryotes and eukaryotes
    • Mileykovskaya E & Dowhan W (2009) Cardiolipin membrane domains in prokaryotes and eukaryotes. Biochim Biophys Acta 1788: 2084-2091.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2084-2091
    • Mileykovskaya, E.1    Dowhan, W.2
  • 86
    • 0037929218 scopus 로고    scopus 로고
    • Effects of phospholipid composition on MinD-membrane interactions in vitro and in vivo
    • Mileykovskaya E, Fishov I, Fu X, Corbin BD, Margolin W & Dowhan W (2003) Effects of phospholipid composition on MinD-membrane interactions in vitro and in vivo. J Biol Chem 278: 22193-22198.
    • (2003) J Biol Chem , vol.278 , pp. 22193-22198
    • Mileykovskaya, E.1    Fishov, I.2    Fu, X.3    Corbin, B.D.4    Margolin, W.5    Dowhan, W.6
  • 87
    • 80052299858 scopus 로고    scopus 로고
    • RodZ regulates the post-transcriptional processing of the Shigella sonnei type III secretion system
    • Mitobe J, Yanagihara I, Ohnishi K, Yamamoto S, Ohnishi M, Ishihama A & Watanabe H (2011) RodZ regulates the post-transcriptional processing of the Shigella sonnei type III secretion system. EMBO Rep 12: 911-916.
    • (2011) EMBO Rep , vol.12 , pp. 911-916
    • Mitobe, J.1    Yanagihara, I.2    Ohnishi, K.3    Yamamoto, S.4    Ohnishi, M.5    Ishihama, A.6    Watanabe, H.7
  • 90
    • 0030862285 scopus 로고    scopus 로고
    • Synthesis of 2′-O,4′-C-methyleneuridine and -cytidine. Novel bicyclic nucleosides having a fixed C3′-endo sugar puckering
    • Obika S, Nanbu N, Hari Y, Morio K-I, In Y, Ishida T & Imanishi T (1997) Synthesis of 2′-O, 4′-C-methyleneuridine and -cytidine. Novel bicyclic nucleosides having a fixed C3′-endo sugar puckering. Tetrahedron Lett 38: 8735-8738.
    • (1997) Tetrahedron Lett , vol.38 , pp. 8735-8738
    • Obika, S.1    Nanbu, N.2    Hari, Y.3    Morio, K.-I.4    In, Y.5    Ishida, T.6    Imanishi, T.7
  • 91
    • 79960959180 scopus 로고    scopus 로고
    • RNA mimics of green fluorescent protein
    • Paige JS, Wu KY & Jaffrey SR (2011) RNA mimics of green fluorescent protein. Science 333: 642-646.
    • (2011) Science , vol.333 , pp. 642-646
    • Paige, J.S.1    Wu, K.Y.2    Jaffrey, S.R.3
  • 92
    • 34248589077 scopus 로고    scopus 로고
    • How does an mRNA find its way? Intracellular localisation of transcripts
    • Palacios IM (2007) How does an mRNA find its way? Intracellular localisation of transcripts. Semin Cell Dev Biol 18: 163-170.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 163-170
    • Palacios, I.M.1
  • 94
    • 77950906711 scopus 로고    scopus 로고
    • Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement
    • Parsons JB, Frank S, Bhella D, Liang M, Prentice MB, Mulvihill DP & Warren MJ (2010) Synthesis of empty bacterial microcompartments, directed organelle protein incorporation, and evidence of filament-associated organelle movement. Mol Cell 38: 305-315.
    • (2010) Mol Cell , vol.38 , pp. 305-315
    • Parsons, J.B.1    Frank, S.2    Bhella, D.3    Liang, M.4    Prentice, M.B.5    Mulvihill, D.P.6    Warren, M.J.7
  • 96
    • 0036900521 scopus 로고    scopus 로고
    • Dynamic cellular location of bacterial plasmids
    • Pogliano J (2002) Dynamic cellular location of bacterial plasmids. Curr Opin Microbiol 5: 586-590.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 586-590
    • Pogliano, J.1
  • 97
    • 0023692827 scopus 로고
    • Small ribonucleoproteins in Schizosaccharomyces pombe and Yarrowia lipolytica homologous to signal recognition particle
    • Poritz MA, Siegel V, Hansen W & Walter P (1988) Small ribonucleoproteins in Schizosaccharomyces pombe and Yarrowia lipolytica homologous to signal recognition particle. P Natl Acad Sci USA 85: 4315-4319.
    • (1988) P Natl Acad Sci USA , vol.85 , pp. 4315-4319
    • Poritz, M.A.1    Siegel, V.2    Hansen, W.3    Walter, P.4
  • 99
    • 66149134063 scopus 로고    scopus 로고
    • Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs
    • Prilusky J & Bibi E (2009) Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs. P Natl Acad Sci USA 106: 6662-6666.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 6662-6666
    • Prilusky, J.1    Bibi, E.2
  • 100
    • 4444285375 scopus 로고    scopus 로고
    • Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs
    • Rackham O & Brown CM (2004) Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs. EMBO J 23: 3346-3355.
    • (2004) EMBO J , vol.23 , pp. 3346-3355
    • Rackham, O.1    Brown, C.M.2
  • 101
    • 78649670793 scopus 로고    scopus 로고
    • Protein localization by recognition of membrane curvature
    • Ramamurthi KS (2010) Protein localization by recognition of membrane curvature. Curr Opin Microbiol 13: 753-757.
    • (2010) Curr Opin Microbiol , vol.13 , pp. 753-757
    • Ramamurthi, K.S.1
  • 102
    • 69449106111 scopus 로고    scopus 로고
    • Negative membrane curvature as a cue for subcellular localization of a bacterial protein
    • Ramamurthi KS & Losick R (2009) Negative membrane curvature as a cue for subcellular localization of a bacterial protein. P Natl Acad Sci USA 106: 13541-13545.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 13541-13545
    • Ramamurthi, K.S.1    Losick, R.2
  • 103
    • 33751355259 scopus 로고    scopus 로고
    • Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis
    • Ramamurthi KS, Clapham KR & Losick R (2006) Peptide anchoring spore coat assembly to the outer forespore membrane in Bacillus subtilis. Mol Microbiol 62: 1547-1557.
    • (2006) Mol Microbiol , vol.62 , pp. 1547-1557
    • Ramamurthi, K.S.1    Clapham, K.R.2    Losick, R.3
  • 104
    • 62149141206 scopus 로고    scopus 로고
    • Geometric cue for protein localization in a bacterium
    • Ramamurthi KS, Lecuyer S, Stone HA & Losick R (2009) Geometric cue for protein localization in a bacterium. Science 323: 1354-1357.
    • (2009) Science , vol.323 , pp. 1354-1357
    • Ramamurthi, K.S.1    Lecuyer, S.2    Stone, H.A.3    Losick, R.4
  • 106
    • 69549118308 scopus 로고    scopus 로고
    • E. coli transports aggregated proteins to the poles by a specific and energy-dependent process
    • Rokney A, Shagan M, Kessel M, Smith Y, Rosenshine I & Oppenheim AB (2009) E. coli transports aggregated proteins to the poles by a specific and energy-dependent process. J Mol Biol 392: 589-601.
    • (2009) J Mol Biol , vol.392 , pp. 589-601
    • Rokney, A.1    Shagan, M.2    Kessel, M.3    Smith, Y.4    Rosenshine, I.5    Oppenheim, A.B.6
  • 107
    • 34250016257 scopus 로고    scopus 로고
    • Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli
    • Romantsov T, Helbig S, Culham DE, Gill C, Stalker L & Wood JM (2007) Cardiolipin promotes polar localization of osmosensory transporter ProP in Escherichia coli. Mol Microbiol 64: 1455-1465.
    • (2007) Mol Microbiol , vol.64 , pp. 1455-1465
    • Romantsov, T.1    Helbig, S.2    Culham, D.E.3    Gill, C.4    Stalker, L.5    Wood, J.M.6
  • 108
    • 75749083324 scopus 로고    scopus 로고
    • Protein localization in Escherichia coli cells: comparison of the cytoplasmic membrane proteins ProP, LacY, ProW, AqpZ, MscS, and MscL
    • Romantsov T, Battle AR, Hendel JL, Martinac B & Wood JM (2010) Protein localization in Escherichia coli cells: comparison of the cytoplasmic membrane proteins ProP, LacY, ProW, AqpZ, MscS, and MscL. J Bacteriol 192: 912-924.
    • (2010) J Bacteriol , vol.192 , pp. 912-924
    • Romantsov, T.1    Battle, A.R.2    Hendel, J.L.3    Martinac, B.4    Wood, J.M.5
  • 109
    • 0024400708 scopus 로고
    • Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains
    • Romisch K, Webb J, Herz J, Prehn S, Frank R, Vingron M & Dobberstein B (1989) Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains. Nature 340: 478-482.
    • (1989) Nature , vol.340 , pp. 478-482
    • Romisch, K.1    Webb, J.2    Herz, J.3    Prehn, S.4    Frank, R.5    Vingron, M.6    Dobberstein, B.7
  • 111
    • 70349490822 scopus 로고    scopus 로고
    • Subcellular localization of a bacterial regulatory RNA
    • Russell JH & Keiler KC (2009) Subcellular localization of a bacterial regulatory RNA. P Natl Acad Sci USA 106: 16405-16409.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 16405-16409
    • Russell, J.H.1    Keiler, K.C.2
  • 112
    • 77749264485 scopus 로고    scopus 로고
    • Spatially ordered dynamics of the bacterial carbon fixation machinery
    • Savage DF, Afonso B, Chen AH & Silver PA (2010) Spatially ordered dynamics of the bacterial carbon fixation machinery. Science 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
  • 113
    • 4444348028 scopus 로고    scopus 로고
    • Dynamic domain formation in membranes: thickness-modulation-induced phase separation
    • Schaffer E & Thiele U (2004) Dynamic domain formation in membranes: thickness-modulation-induced phase separation. Eur Phys J E Soft Matter 14: 169-175.
    • (2004) Eur Phys J E Soft Matter , vol.14 , pp. 169-175
    • Schaffer, E.1    Thiele, U.2
  • 115
    • 0035923586 scopus 로고    scopus 로고
    • Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway
    • Scott ME, Dossani ZY & Sandkvist M (2001) Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway. P Natl Acad Sci USA 98: 13978-13983.
    • (2001) P Natl Acad Sci USA , vol.98 , pp. 13978-13983
    • Scott, M.E.1    Dossani, Z.Y.2    Sandkvist, M.3
  • 116
    • 0023904203 scopus 로고
    • Cardiolipin activation of dnaA protein, the initiation protein of replication in Escherichia coli
    • Sekimizu K & Kornberg A (1988) Cardiolipin activation of dnaA protein, the initiation protein of replication in Escherichia coli. J Biol Chem 263: 7131-7135.
    • (1988) J Biol Chem , vol.263 , pp. 7131-7135
    • Sekimizu, K.1    Kornberg, A.2
  • 118
    • 0037032826 scopus 로고    scopus 로고
    • Generating and exploiting polarity in bacteria
    • Shapiro L, McAdams HH & Losick R (2002) Generating and exploiting polarity in bacteria. Science 298: 1942-1946.
    • (2002) Science , vol.298 , pp. 1942-1946
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 119
    • 70849086538 scopus 로고    scopus 로고
    • Why and how bacteria localize proteins
    • Shapiro L, McAdams HH & Losick R (2009) Why and how bacteria localize proteins. Science 326: 1225-1228.
    • (2009) Science , vol.326 , pp. 1225-1228
    • Shapiro, L.1    McAdams, H.H.2    Losick, R.3
  • 120
    • 33646408141 scopus 로고    scopus 로고
    • Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery
    • Shiomi D, Yoshimoto M, Homma M & Kawagishi I (2006) Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery. Mol Microbiol 60: 894-906.
    • (2006) Mol Microbiol , vol.60 , pp. 894-906
    • Shiomi, D.1    Yoshimoto, M.2    Homma, M.3    Kawagishi, I.4
  • 121
    • 57149120088 scopus 로고    scopus 로고
    • Determination of bacterial rod shape by a novel cytoskeletal membrane protein
    • Shiomi D, Sakai M & Niki H (2008) Determination of bacterial rod shape by a novel cytoskeletal membrane protein. EMBO J 27: 3081-3091.
    • (2008) EMBO J , vol.27 , pp. 3081-3091
    • Shiomi, D.1    Sakai, M.2    Niki, H.3
  • 122
    • 11144257131 scopus 로고    scopus 로고
    • Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure
    • Slovak PM, Wadhams GH & Armitage JP (2005) Localization of MreB in Rhodobacter sphaeroides under conditions causing changes in cell shape and membrane structure. J Bacteriol 187: 54-64.
    • (2005) J Bacteriol , vol.187 , pp. 54-64
    • Slovak, P.M.1    Wadhams, G.H.2    Armitage, J.P.3
  • 123
    • 7944221332 scopus 로고    scopus 로고
    • Receptor clustering and signal processing in E. coli chemotaxis
    • Sourjik V (2004) Receptor clustering and signal processing in E. coli chemotaxis. Trends Microbiol 12: 569-576.
    • (2004) Trends Microbiol , vol.12 , pp. 569-576
    • Sourjik, V.1
  • 124
    • 77955807391 scopus 로고    scopus 로고
    • Spatial organization in bacterial chemotaxis
    • Sourjik V & Armitage JP (2010) Spatial organization in bacterial chemotaxis. EMBO J 29: 2724-2733.
    • (2010) EMBO J , vol.29 , pp. 2724-2733
    • Sourjik, V.1    Armitage, J.P.2
  • 125
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions
    • Sourjik V & Berg HC (2000) Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol Microbiol 37: 740-751.
    • (2000) Mol Microbiol , vol.37 , pp. 740-751
    • Sourjik, V.1    Berg, H.C.2
  • 126
    • 77955449195 scopus 로고    scopus 로고
    • Membrane potential is important for bacterial cell division
    • Strahl H & Hamoen LW (2010) Membrane potential is important for bacterial cell division. P Natl Acad Sci USA 107: 12281-12286.
    • (2010) P Natl Acad Sci USA , vol.107 , pp. 12281-12286
    • Strahl, H.1    Hamoen, L.W.2
  • 127
    • 33846818898 scopus 로고    scopus 로고
    • RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton
    • Taghbalout A & Rothfield L (2007) RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton. P Natl Acad Sci USA 104: 1667-1672.
    • (2007) P Natl Acad Sci USA , vol.104 , pp. 1667-1672
    • Taghbalout, A.1    Rothfield, L.2
  • 128
    • 46649086171 scopus 로고    scopus 로고
    • RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome
    • Taghbalout A & Rothfield L (2008) RNaseE and RNA helicase B play central roles in the cytoskeletal organization of the RNA degradosome. J Biol Chem 283: 13850-13855.
    • (2008) J Biol Chem , vol.283 , pp. 13850-13855
    • Taghbalout, A.1    Rothfield, L.2
  • 129
    • 74849140487 scopus 로고    scopus 로고
    • Structure and mechanisms of a protein-based organelle in Escherichia coli
    • Tanaka S, Sawaya MR & Yeates TO (2010) Structure and mechanisms of a protein-based organelle in Escherichia coli. Science 327: 81-84.
    • (2010) Science , vol.327 , pp. 81-84
    • Tanaka, S.1    Sawaya, M.R.2    Yeates, T.O.3
  • 130
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi Y, Choi PJ, Li GW et al. (2010) Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 329: 533-538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3
  • 131
    • 37349036312 scopus 로고    scopus 로고
    • Getting organized-how bacterial cells move proteins and DNA
    • Thanbichler M & Shapiro L (2008) Getting organized-how bacterial cells move proteins and DNA. Nat Rev Microbiol 6: 28-40.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 28-40
    • Thanbichler, M.1    Shapiro, L.2
  • 132
    • 43449139401 scopus 로고    scopus 로고
    • Stochastic assembly of chemoreceptor clusters in Escherichia coli
    • Thiem S & Sourjik V (2008) Stochastic assembly of chemoreceptor clusters in Escherichia coli. Mol Microbiol 68: 1228-1236.
    • (2008) Mol Microbiol , vol.68 , pp. 1228-1236
    • Thiem, S.1    Sourjik, V.2
  • 133
    • 33947584609 scopus 로고    scopus 로고
    • Positioning of chemosensory clusters in E. coli and its relation to cell division
    • Thiem S, Kentner D & Sourjik V (2007) Positioning of chemosensory clusters in E. coli and its relation to cell division. EMBO J 26: 1615-1623.
    • (2007) EMBO J , vol.26 , pp. 1615-1623
    • Thiem, S.1    Kentner, D.2    Sourjik, V.3
  • 134
  • 135
    • 79952500685 scopus 로고    scopus 로고
    • A dynamic complex of signaling proteins uses polar localization to regulate cell-fate asymmetry in Caulobacter crescentus
    • Tsokos CG, Perchuk BS & Laub MT (2011) A dynamic complex of signaling proteins uses polar localization to regulate cell-fate asymmetry in Caulobacter crescentus. Dev Cell 20: 329-341.
    • (2011) Dev Cell , vol.20 , pp. 329-341
    • Tsokos, C.G.1    Perchuk, B.S.2    Laub, M.T.3
  • 136
    • 34250191761 scopus 로고    scopus 로고
    • RNA visualization in live bacterial cells using fluorescent protein complementation
    • Valencia-Burton M, McCullough RM, Cantor CR & Broude NE (2007) RNA visualization in live bacterial cells using fluorescent protein complementation. Nat Methods 4: 421-427.
    • (2007) Nat Methods , vol.4 , pp. 421-427
    • Valencia-Burton, M.1    McCullough, R.M.2    Cantor, C.R.3    Broude, N.E.4
  • 137
    • 70349515864 scopus 로고    scopus 로고
    • Spatiotemporal patterns and transcription kinetics of induced RNA in single bacterial cells
    • Valencia-Burton M, Shah A, Sutin J et al. (2009) Spatiotemporal patterns and transcription kinetics of induced RNA in single bacterial cells. P Natl Acad Sci USA 106: 16399-16404.
    • (2009) P Natl Acad Sci USA , vol.106 , pp. 16399-16404
    • Valencia-Burton, M.1    Shah, A.2    Sutin, J.3
  • 138
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent F & Lowe J (2000) Crystal structure of the cell division protein FtsA from Thermotoga maritima. EMBO J 19: 5300-5307.
    • (2000) EMBO J , vol.19 , pp. 5300-5307
    • van den Ent, F.1    Lowe, J.2
  • 139
    • 77949567575 scopus 로고    scopus 로고
    • Bacterial actin MreB assembles in complex with cell shape protein RodZ
    • van den Ent F, Johnson CM, Persons L, de Boer P & Lowe J (2010) Bacterial actin MreB assembles in complex with cell shape protein RodZ. EMBO J 29: 1081-1090.
    • (2010) EMBO J , vol.29 , pp. 1081-1090
    • van den Ent, F.1    Johnson, C.M.2    Persons, L.3    de Boer, P.4    Lowe, J.5
  • 141
    • 36749016781 scopus 로고    scopus 로고
    • Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle
    • Vats P & Rothfield L (2007) Duplication and segregation of the actin (MreB) cytoskeleton during the prokaryotic cell cycle. P Natl Acad Sci USA 104: 17795-17800.
    • (2007) P Natl Acad Sci USA , vol.104 , pp. 17795-17800
    • Vats, P.1    Rothfield, L.2
  • 142
    • 70350493966 scopus 로고    scopus 로고
    • The dynamic nature of the bacterial cytoskeleton
    • Vats P, Yu J & Rothfield L (2009a) The dynamic nature of the bacterial cytoskeleton. Cell Mol Life Sci 66: 3353-3362.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3353-3362
    • Vats, P.1    Yu, J.2    Rothfield, L.3
  • 143
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
    • Vats P, Shih YL & Rothfield L (2009b) Assembly of the MreB-associated cytoskeletal ring of Escherichia coli. Mol Microbiol 72: 170-182.
    • (2009) Mol Microbiol , vol.72 , pp. 170-182
    • Vats, P.1    Shih, Y.L.2    Rothfield, L.3
  • 144
    • 0023638691 scopus 로고
    • Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli
    • Wachi M, Doi M, Tamaki S, Park W, Nakajima-Iijima S & Matsuhashi M (1987) Mutant isolation and molecular cloning of mre genes, which determine cell shape, sensitivity to mecillinam, and amount of penicillin-binding proteins in Escherichia coli. J Bacteriol 169: 4935-4940.
    • (1987) J Bacteriol , vol.169 , pp. 4935-4940
    • Wachi, M.1    Doi, M.2    Tamaki, S.3    Park, W.4    Nakajima-Iijima, S.5    Matsuhashi, M.6
  • 145
    • 11844281590 scopus 로고    scopus 로고
    • Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation
    • Wagner JK, Galvani CD & Brun YV (2005) Caulobacter crescentus requires RodA and MreB for stalk synthesis and prevention of ectopic pole formation. J Bacteriol 187: 544-553.
    • (2005) J Bacteriol , vol.187 , pp. 544-553
    • Wagner, J.K.1    Galvani, C.D.2    Brun, Y.V.3
  • 146
    • 0009499348 scopus 로고
    • Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum
    • Walter P & Blobel G (1980) Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum. P Natl Acad Sci USA 77: 7112-7116.
    • (1980) P Natl Acad Sci USA , vol.77 , pp. 7112-7116
    • Walter, P.1    Blobel, G.2
  • 147
    • 0019964240 scopus 로고
    • Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum
    • Walter P & Blobel G (1982) Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum. Nature 299: 691-698.
    • (1982) Nature , vol.299 , pp. 691-698
    • Walter, P.1    Blobel, G.2
  • 148
    • 77952727936 scopus 로고    scopus 로고
    • Actin-like cytoskeleton filaments contribute to cell mechanics in bacteria
    • Wang S, Arellano-Santoyo H, Combs PA & Shaevitz JW (2010) Actin-like cytoskeleton filaments contribute to cell mechanics in bacteria. P Natl Acad Sci USA 107: 9182-9185.
    • (2010) P Natl Acad Sci USA , vol.107 , pp. 9182-9185
    • Wang, S.1    Arellano-Santoyo, H.2    Combs, P.A.3    Shaevitz, J.W.4
  • 149
    • 84863229704 scopus 로고    scopus 로고
    • Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall
    • Wang S, Furchtgott L, Huang KC & Shaevitz JW (2012) Helical insertion of peptidoglycan produces chiral ordering of the bacterial cell wall. P Natl Acad Sci USA 109: E595-E604.
    • (2012) P Natl Acad Sci USA , vol.109
    • Wang, S.1    Furchtgott, L.2    Huang, K.C.3    Shaevitz, J.W.4
  • 151
    • 77951608842 scopus 로고    scopus 로고
    • Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD
    • White CL, Kitich A & Gober JW (2010) Positioning cell wall synthetic complexes by the bacterial morphogenetic proteins MreB and MreD. Mol Microbiol 76: 616-633.
    • (2010) Mol Microbiol , vol.76 , pp. 616-633
    • White, C.L.1    Kitich, A.2    Gober, J.W.3
  • 153
    • 79955577661 scopus 로고    scopus 로고
    • RNA detection in live bacterial cells using fluorescent protein complementation triggered by interaction of two RNA aptamers with two RNA-binding peptides
    • Yiu H-W, Demidov VV, Toran P, Cantor CR & Broude NE (2011) RNA detection in live bacterial cells using fluorescent protein complementation triggered by interaction of two RNA aptamers with two RNA-binding peptides. Pharmaceuticals 4: 494-508.
    • (2011) Pharmaceuticals , vol.4 , pp. 494-508
    • Yiu, H.-W.1    Demidov, V.V.2    Toran, P.3    Cantor, C.R.4    Broude, N.E.5
  • 154
    • 21044433322 scopus 로고    scopus 로고
    • An alkali-inducible flotillin-like protein from Bacillus halodurans C-125
    • Zhang HM, Li Z, Tsudome M, Ito S, Takami H & Horikoshi K (2005) An alkali-inducible flotillin-like protein from Bacillus halodurans C-125. Protein J 24: 125-131.
    • (2005) Protein J , vol.24 , pp. 125-131
    • Zhang, H.M.1    Li, Z.2    Tsudome, M.3    Ito, S.4    Takami, H.5    Horikoshi, K.6
  • 155
    • 0026344818 scopus 로고
    • Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli
    • Zimmerman SB & Trach SO (1991) Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli. J Mol Biol 222: 599-620.
    • (1991) J Mol Biol , vol.222 , pp. 599-620
    • Zimmerman, S.B.1    Trach, S.O.2


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