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Volumn 6, Issue JUN, 2015, Pages

Multi-color imaging of the bacterial nucleoid and division proteins with blue, orange, and near-infrared fluorescent proteins

Author keywords

Bacterial cell division; Bacterial chromosome; Fluorescent proteins; FtsZ; HU; MinD; TagBFP; TagRFP T

Indexed keywords

BLUE FLUORESCENT PROTEIN; CHLORAMPHENICOL; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; INFRARED FLUORESCENT PROTEIN; KANAMYCIN; MIND PROTEIN; ORANGE FLUORESCENT PROTEIN; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG;

EID: 84937002120     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2015.00607     Document Type: Article
Times cited : (21)

References (65)
  • 1
    • 34249007166 scopus 로고    scopus 로고
    • Exploration of new chromophore structures leads to the identification of improved blue fluorescent proteins
    • Ai, H.-W., Shaner, N. C., Cheng, Z., Tsien, R. Y., and Campbell, R. E. (2007). Exploration of new chromophore structures leads to the identification of improved blue fluorescent proteins. Biochemistry 46, 5904-5910. doi: 10.1021/bi700199g
    • (2007) Biochemistry , vol.46 , pp. 5904-5910
    • Ai, H.-W.1    Shaner, N.C.2    Cheng, Z.3    Tsien, R.Y.4    Campbell, R.E.5
  • 2
    • 77954376358 scopus 로고    scopus 로고
    • Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET
    • Alexeeva, S., Gadella, T. W. J., Verheul, J., Verhoeven, G. S., and Den Blaauwen, T. (2010). Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET. Mol. Microbiol. 77, 384-398. doi: 10.1111/j.1365-2958.2010.07211.x
    • (2010) Mol. Microbiol , vol.77 , pp. 384-398
    • Alexeeva, S.1    Gadella, T.W.J.2    Verheul, J.3    Verhoeven, G.S.4    Den Blaauwen, T.5
  • 3
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam, T., Iwata, A., Nishimura, A., Ueda, S., and Ishihama, A. (1999). Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J. Bacteriol. 181, 6361-6370.
    • (1999) J. Bacteriol. , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 4
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: an intermediate filament-like function in cell shape
    • Ausmees, N., Kuhn, J. R., and Jacobs-Wagner, C. (2003). The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell 115, 705-713. doi: 10.1016/S0092-8674(03)00935-8
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 5
    • 84908362766 scopus 로고    scopus 로고
    • Evidence for divisome localization mechanisms independent of the min system and SlmA in Escherichia coli
    • Bailey, M. W., Bisicchia, P., Warren, B. T., Sherratt, D. J., and Männik, J. (2014). Evidence for divisome localization mechanisms independent of the min system and SlmA in Escherichia coli. PLoS Genet. 10:e1004504. doi: 10.1371/journal.pgen.1004504
    • (2014) PLoS Genet , vol.10
    • Bailey, M.W.1    Bisicchia, P.2    Warren, B.T.3    Sherratt, D.J.4    Männik, J.5
  • 6
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezú, F. O., and de Boer, P. A. J. (2008). Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J. Bacteriol. 190, 1792-1811. doi: 10.1128/jb.01322-07
    • (2008) J. Bacteriol , vol.190 , pp. 1792-1811
    • Bendezú, F.O.1    de Boer, P.A.J.2
  • 7
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E
    • Bendezú, F. O., Hale, C. A., Bernhardt, T. G., and De Boer, P. A. J. (2009). RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli. EMBO J. 28, 193-204. doi: 10.1038/emboj.2008.264
    • (2009) coli. EMBO J , vol.28 , pp. 193-204
    • Bendezú, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    De Boer, P.A.J.4
  • 8
    • 84880133681 scopus 로고    scopus 로고
    • A flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo
    • Buske, P. J., and Levin, P. A. (2013). A flexible C-terminal linker is required for proper FtsZ assembly in vitro and cytokinetic ring formation in vivo. Mol. Microbiol. 89, 249-263. doi: 10.1111/mmi.12272
    • (2013) Mol. Microbiol , vol.89 , pp. 249-263
    • Buske, P.J.1    Levin, P.A.2
  • 9
    • 23444431611 scopus 로고
    • Green fluorescent protein as a marker for gene expression
    • Chalfie, M., Tu, Y., Euskirchen, G., Ward, W., and Prasher, D. (1994). Green fluorescent protein as a marker for gene expression. Science 263, 802-805. doi: 10.1126/science.8303295
    • (1994) Science , vol.263 , pp. 802-805
    • Chalfie, M.1    Tu, Y.2    Euskirchen, G.3    Ward, W.4    Prasher, D.5
  • 10
    • 0035859884 scopus 로고    scopus 로고
    • Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio
    • Charles, M., Pérez, M., Kobil, J. H., and Goldberg, M. B. (2001). Polar targeting of Shigella virulence factor IcsA in Enterobacteriacae and Vibrio. Proc. Natl. Acad. Sci. U.S.A. 98, 9871-9876. doi: 10.1073/pnas.171310498
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 9871-9876
    • Charles, M.1    Pérez, M.2    Kobil, J.H.3    Goldberg, M.B.4
  • 11
    • 0025733254 scopus 로고
    • ftsZ is an essential cell division gene in Escherichia coli
    • Dai, K., and Lutkenhaus, J. (1991). ftsZ is an essential cell division gene in Escherichia coli. J. Bacteriol. 173, 3500-3506.
    • (1991) J. Bacteriol. , vol.173 , pp. 3500-3506
    • Dai, K.1    Lutkenhaus, J.2
  • 12
    • 0026697767 scopus 로고
    • The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli
    • Dai, K., and Lutkenhaus, J. (1992). The proper ratio of FtsZ to FtsA is required for cell division to occur in Escherichia coli. J. Bacteriol. 174, 6145-6151.
    • (1992) J. Bacteriol. , vol.174 , pp. 6145-6151
    • Dai, K.1    Lutkenhaus, J.2
  • 13
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and Wanner, B. L. (2000). One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. U.S.A. 97, 6640-6645. doi: 10.1073/pnas.120163297
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 14
    • 0024977391 scopus 로고
    • A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E
    • de Boer, P. A. J., Crossley, R. E., and Rothfield, L. I. (1989). A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli. Cell 56, 641-649. doi: 10.1016/0092-8674(89)90586-2
    • (1989) coli. Cell , vol.56 , pp. 641-649
    • de Boer, P.A.J.1    Crossley, R.E.2    Rothfield, L.I.3
  • 15
    • 80052551898 scopus 로고    scopus 로고
    • Using superfolder green fluorescent protein for periplasmic protein localization studies
    • Dinh, T., and Bernhardt, T. G. (2011). Using superfolder green fluorescent protein for periplasmic protein localization studies. J. Bacteriol. 193, 4984-4987. doi: 10.1128/jb.00315-311
    • (2011) J. Bacteriol , vol.193 , pp. 4984-4987
    • Dinh, T.1    Bernhardt, T.G.2
  • 17
    • 84905483299 scopus 로고    scopus 로고
    • SlmA antagonism of FtsZ assembly employs a Two-pronged mechanism like MinCD
    • Du, S., and Lutkenhaus, J. (2014). SlmA antagonism of FtsZ assembly employs a Two-pronged mechanism like MinCD. PLoS Genet. 10:e1004460. doi: 10.1371/journal.pgen.1004460
    • (2014) PLoS Genet , vol.10
    • Du, S.1    Lutkenhaus, J.2
  • 18
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one
    • Erickson, H. P., Anderson, D. E., and Osawa, M. (2010). FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 74, 504-528. doi: 10.1128/MMBR.00021-10
    • (2010) Microbiol. Mol. Biol. Rev , vol.74 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 19
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B subtilis
    • Garner, E. C., Bernard, R., Wang, W., Zhuang, X., Rudner, D. Z., and Mitchison, T. (2011). Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333, 222-225. doi: 10.1126/science.1203285
    • (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
  • 20
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998). Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272. doi: 10.1126/science.281.5374.269
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 21
    • 31544438578 scopus 로고    scopus 로고
    • Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110
    • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., et al. (2006). Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol. Syst. Biol. 2, 2006.0007. doi: 10.1038/msb4100049
    • (2006) Mol. Syst. Biol , vol.2
    • Hayashi, K.1    Morooka, N.2    Yamamoto, Y.3    Fujita, K.4    Isono, K.5    Choi, S.6
  • 22
    • 84908254231 scopus 로고    scopus 로고
    • Zooming in to see the bigger picture: microfluidic and nanofabrication tools to study bacteria
    • Hol, F. J. H., and Dekker, C. (2014). Zooming in to see the bigger picture: microfluidic and nanofabrication tools to study bacteria. Science 346:1251821. doi: 10.1126/science.1251821
    • (2014) Science , vol.346 , pp. 1251821
    • Hol, F.J.H.1    Dekker, C.2
  • 23
    • 0032846485 scopus 로고    scopus 로고
    • Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE
    • Hu, Z., and Lutkenhaus, J. (1999). Topological regulation of cell division in Escherichia coli involves rapid pole to pole oscillation of the division inhibitor MinC under the control of MinD and MinE. Mol. Microbiol. 34, 82-90. doi: 10.1046/j.1365-2958.1999.01575.x
    • (1999) Mol. Microbiol , vol.34 , pp. 82-90
    • Hu, Z.1    Lutkenhaus, J.2
  • 24
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones, L. J. F., Carballido-López, R., and Errington, J. (2001). Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104, 913-922. doi: 10.1016/S0092-8674(01)00287-2
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.F.1    Carballido-López, R.2    Errington, J.3
  • 25
    • 33646568438 scopus 로고    scopus 로고
    • Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E coli K-12 ORF archive): unique resources for biological research
    • Kitagawa, M., Ara, T., Arifuzzaman, M., Ioka-Nakamichi, T., Inamoto, E., Toyonaga, H., et al. (2006). Complete set of ORF clones of Escherichia coli ASKA library (a complete set of E. coli K-12 ORF archive): unique resources for biological research. DNA Res. 12, 291-299. doi: 10.1093/dnares/dsi012
    • (2006) DNA Res , vol.12 , pp. 291-299
    • Kitagawa, M.1    Ara, T.2    Arifuzzaman, M.3    Ioka-Nakamichi, T.4    Inamoto, E.5    Toyonaga, H.6
  • 26
    • 33947704150 scopus 로고    scopus 로고
    • Improved green and blue fluorescent proteins for expression in bacteria and mammalian cells
    • Kremers, G.-J., Goedhart, J., Van Den Heuvel, D. J., Gerritsen, H. C., and Gadella, T. W. J. (2007). Improved green and blue fluorescent proteins for expression in bacteria and mammalian cells. Biochemistry 46, 3775-3783. doi: 10.1021/bi0622874
    • (2007) Biochemistry , vol.46 , pp. 3775-3783
    • Kremers, G.-J.1    Goedhart, J.2    Van Den Heuvel, D.J.3    Gerritsen, H.C.4    Gadella, T.W.J.5
  • 27
    • 33744779420 scopus 로고    scopus 로고
    • Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET förster radius
    • Kremers, G.-J., Goedhart, J., Van Munster, E. B., and Gadella, T. W. J. (2006). Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET förster radius. Biochemistry 45, 6570-6580. doi: 10.1021/bi0516273
    • (2006) Biochemistry , vol.45 , pp. 6570-6580
    • Kremers, G.-J.1    Goedhart, J.2    Van Munster, E.B.3    Gadella, T.W.J.4
  • 28
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in Escherichia coli
    • Kudla, G., Murray, A. W., Tollervey, D., and Plotkin, J. B. (2009). Coding-sequence determinants of gene expression in Escherichia coli. Science 324, 255-258. doi: 10.1126/science.1170160
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 29
    • 84919360122 scopus 로고    scopus 로고
    • Genome-scale quantitative characterization of bacterial protein localization dynamics throughout the cell cycle
    • Kuwada, N. J., Traxler, B., and Wiggins, P. A. (2015). Genome-scale quantitative characterization of bacterial protein localization dynamics throughout the cell cycle. Mol. Microbiol. 95, 64-79. doi: 10.1111/mmi.12841
    • (2015) Mol. Microbiol , vol.95 , pp. 64-79
    • Kuwada, N.J.1    Traxler, B.2    Wiggins, P.A.3
  • 30
    • 84860361727 scopus 로고    scopus 로고
    • Segregation of molecules at cell division reveals native protein localization
    • Landgraf, D., Okumus, B., Chien, P., Baker, T. A., and Paulsson, J. (2012). Segregation of molecules at cell division reveals native protein localization. Nat Meth. 9, 480-482. doi: 10.1038/nmeth.1955
    • (2012) Nat Meth , vol.9 , pp. 480-482
    • Landgraf, D.1    Okumus, B.2    Chien, P.3    Baker, T.A.4    Paulsson, J.5
  • 31
    • 0041853780 scopus 로고    scopus 로고
    • Spatial and temporal organization of replicating Escherichia coli chromosomes
    • Lau, I. F., Filipe, S. R., Søballe, B., Økstad, O.-A., Barre, F.-X., and Sherratt, D. J. (2003). Spatial and temporal organization of replicating Escherichia coli chromosomes. Mol. Microbiol. 49, 731-743. doi: 10.1046/j.1365-2958.2003.03640.x
    • (2003) Mol. Microbiol , vol.49 , pp. 731-743
    • Lau, I.F.1    Filipe, S.R.2    Søballe, B.3    Økstad, O.-A.4    Barre, F.-X.5    Sherratt, D.J.6
  • 32
    • 84879761045 scopus 로고    scopus 로고
    • Improved blue, green, and red fluorescent protein tagging vectors for S cerevisiae
    • Lee, S., Lim, W. A., and Thorn, K. S. (2013). Improved blue, green, and red fluorescent protein tagging vectors for S. cerevisiae. PLoS ONE 8:e67902. doi: 10.1371/journal.pone.0067902
    • (2013) PLoS ONE , vol.8
    • Lee, S.1    Lim, W.A.2    Thorn, K.S.3
  • 33
    • 84862815508 scopus 로고    scopus 로고
    • Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli
    • Li, G., and Young, K. D. (2012). Isolation and identification of new inner membrane-associated proteins that localize to cell poles in Escherichia coli. Mol. Microbiol. 84, 276-295. doi: 10.1111/j.1365-2958.2012.08021.x
    • (2012) Mol. Microbiol , vol.84 , pp. 276-295
    • Li, G.1    Young, K.D.2
  • 34
    • 42949100420 scopus 로고    scopus 로고
    • Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation
    • Lindner, A. B., Madden, R., Demarez, A., Stewart, E. J., and Taddei, F. (2008). Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation. Proc. Natl. Acad. Sci. U.S.A. 105, 3076-3081. doi: 10.1073/pnas.0708931105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 3076-3081
    • Lindner, A.B.1    Madden, R.2    Demarez, A.3    Stewart, E.J.4    Taddei, F.5
  • 35
    • 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, D. W., and Margolin, W. (1996). Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein. Proc. Natl. Acad. Sci. U.S.A. 93, 12998-13003. doi: 10.1073/pnas.93.23.12998
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 36
    • 84860822838 scopus 로고    scopus 로고
    • Robustness and accuracy of cell division in Escherichia coli in diverse cell shapes
    • Männik, J., Wu, F., Hol, F. J. H., Bisicchia, P., Sherratt, D. J., Keymer, J. E., et al. (2012). Robustness and accuracy of cell division in Escherichia coli in diverse cell shapes. Proc. Natl. Acad. Sci. U.S.A. 109, 6957-6962. doi: 10.1073/pnas.1120854109
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 6957-6962
    • Männik, J.1    Wu, F.2    Hol, F.J.H.3    Bisicchia, P.4    Sherratt, D.J.5    Keymer, J.E.6
  • 37
    • 77955211891 scopus 로고    scopus 로고
    • Far-Red fluorescent protein excitable with red lasers for flow cytometry and superresolution STED nanoscopy
    • Morozova, K. S., Piatkevich, K. D., Gould, T. J., Zhang, J., Bewersdorf, J., and Verkhusha, V. V. (2010). Far-Red fluorescent protein excitable with red lasers for flow cytometry and superresolution STED nanoscopy. Biophys. J. 99, L13-L15. doi: 10.1016/j.bpj.2010.04.025
    • (2010) Biophys. J , vol.99 , pp. L13-L15
    • Morozova, K.S.1    Piatkevich, K.D.2    Gould, T.J.3    Zhang, J.4    Bewersdorf, J.5    Verkhusha, V.V.6
  • 38
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • Nguyen, A. W., and Daugherty, P. S. (2005). Evolutionary optimization of fluorescent proteins for intracellular FRET. Nat. Biotechnol. 23, 355-360. doi: 10.1038/nbt1066
    • (2005) Nat. Biotechnol , vol.23 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 39
    • 13444274140 scopus 로고    scopus 로고
    • Structural insights into FtsZ protofilament formation
    • Oliva, M. A., Cordell, S. C., and Lowe, J. (2004). Structural insights into FtsZ protofilament formation. Nat. Struct. Mol. Biol. 11, 1243-1250. doi: 10.1038/nsmb855
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 1243-1250
    • Oliva, M.A.1    Cordell, S.C.2    Lowe, J.3
  • 40
    • 29244436874 scopus 로고    scopus 로고
    • Probing the domain structure of FtsZ by random truncation and insertion of GFP
    • Osawa, M., and Erickson, H. P. (2005). Probing the domain structure of FtsZ by random truncation and insertion of GFP. Microbiology 151, 4033-4043. doi: 10.1099/mic.0.28219-0
    • (2005) Microbiology , vol.151 , pp. 4033-4043
    • Osawa, M.1    Erickson, H.P.2
  • 41
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • Pedelacq, J.-D., Cabantous, S., Tran, T., Terwilliger, T. C., and Waldo, G. S. (2006). Engineering and characterization of a superfolder green fluorescent protein. Nat. Biotechnol. 24, 79-88. doi: 10.1038/nbt1172
    • (2006) Nat. Biotechnol , vol.24 , pp. 79-88
    • Pedelacq, J.-D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 42
    • 0026578325 scopus 로고
    • Primary structure of the Aequorea victoria green-fluorescent protein
    • Prasher, D. C., Eckenrode, V. K., Ward, W. W., Prendergast, F. G., and Cormier, M. J. (1992). Primary structure of the Aequorea victoria green-fluorescent protein. Gene 111, 229-233. doi: 10.1016/0378-1119(92)90691-H
    • (1992) Gene , vol.111 , pp. 229-233
    • Prasher, D.C.1    Eckenrode, V.K.2    Ward, W.W.3    Prendergast, F.G.4    Cormier, M.J.5
  • 43
    • 0030780085 scopus 로고    scopus 로고
    • The MinE ring: an FtsZ-Independent cell structure required for selection of the correct division site in E coli
    • Raskin, D. M., and de Boer, P. A. J. (1997). The MinE ring: an FtsZ-Independent cell structure required for selection of the correct division site in E. coli. Cell 91, 685-694. doi: 10.1016/S0092-8674(00)80455-9
    • (1997) Cell , vol.91 , pp. 685-694
    • Raskin, D.M.1    de Boer, P.A.J.2
  • 44
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli
    • Raskin, D. M., and de Boer, P. A. J. (1999). Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 96, 4971-4976. doi: 10.1073/pnas.96.9.4971
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    de Boer, P.A.J.2
  • 45
    • 41149121779 scopus 로고    scopus 로고
    • Independent positioning and action of Escherichia coli replisomes in live cells
    • Reyes-Lamothe, R., Possoz, C., Danilova, O., and Sherratt, D. J. (2008). Independent positioning and action of Escherichia coli replisomes in live cells. Cell 133, 90-102. doi: 10.1016/j.cell.2008.01.044
    • (2008) Cell , vol.133 , pp. 90-102
    • Reyes-Lamothe, R.1    Possoz, C.2    Danilova, O.3    Sherratt, D.J.4
  • 46
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Rizzo, M. A., Springer, G. H., Granada, B., and Piston, D. W. (2004). An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449. doi: 10.1038/nbt945
    • (2004) Nat. Biotechnol , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 47
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp red fluorescent protein
    • Shaner, N. C., Campbell, R. E., Steinbach, P. A., Giepmans, B. N. G., Palmer, A. E., and Tsien, R. Y. (2004). Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22, 1567-1572. doi: 10.1038/nbt1037
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.G.4    Palmer, A.E.5    Tsien, R.Y.6
  • 48
    • 44449109239 scopus 로고    scopus 로고
    • Improving the photostability of bright monomeric orange and red fluorescent proteins
    • Shaner, N. C., Lin, M. Z., Mckeown, M. R., Steinbach, P. A., Hazelwood, K. L., Davidson, M. W., et al. (2008). Improving the photostability of bright monomeric orange and red fluorescent proteins. Nat. Methods 5, 545-551. doi: 10.1038/nmeth.1209
    • (2008) Nat. Methods , vol.5 , pp. 545-551
    • Shaner, N.C.1    Lin, M.Z.2    Mckeown, M.R.3    Steinbach, P.A.4    Hazelwood, K.L.5    Davidson, M.W.6
  • 51
    • 64149089661 scopus 로고    scopus 로고
    • The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD
    • Shen, B., and Lutkenhaus, J. (2009). The conserved C-terminal tail of FtsZ is required for the septal localization and division inhibitory activity of MinC(C)/MinD. Mol. Microbiol. 72, 410-424. doi: 10.1111/j.1365-2958.2009.06651.x
    • (2009) Mol. Microbiol , vol.72 , pp. 410-424
    • Shen, B.1    Lutkenhaus, J.2
  • 52
    • 0036646101 scopus 로고    scopus 로고
    • Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains
    • Shih, Y.-L., Fu, X., King, G. F., Le, T., and Rothfield, L. (2002). Division site placement in E.coli: mutations that prevent formation of the MinE ring lead to loss of the normal midcell arrest of growth of polar MinD membrane domains. EMBO J. 21, 3347-3357. doi: 10.1093/emboj/cdf323
    • (2002) EMBO J , vol.21 , pp. 3347-3357
    • Shih, Y.-L.1    Fu, X.2    King, G.F.3    Le, T.4    Rothfield, L.5
  • 53
    • 27944489446 scopus 로고    scopus 로고
    • The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation
    • Shih, Y.-L., Kawagishi, I., and Rothfield, L. (2005). The MreB and Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation. Mol. Microbiol. 58, 917-928. doi: 10.1111/j.1365-2958.2005.04841.x
    • (2005) Mol. Microbiol , vol.58 , pp. 917-928
    • Shih, Y.-L.1    Kawagishi, I.2    Rothfield, L.3
  • 54
    • 77955608542 scopus 로고    scopus 로고
    • New and old reagents for fluorescent protein tagging of microtubules in fission yeast: experimental and critical evaluation
    • Chap. 9, eds C. Lynne and T. Phong (Waltham, MA: Academic Press)
    • Snaith, H. A., Anders, A., Samejima, I., and Sawin, K. E. (2010). "New and old reagents for fluorescent protein tagging of microtubules in fission yeast: experimental and critical evaluation," in Methods in Cell Biology, Chap. 9, eds C. Lynne and T. Phong (Waltham, MA: Academic Press), 147-172. doi: 10.1016/s0091-679x(10)97009-x
    • (2010) Methods in Cell Biology , pp. 147-172
    • Snaith, H.A.1    Anders, A.2    Samejima, I.3    Sawin, K.E.4
  • 55
    • 0033865904 scopus 로고    scopus 로고
    • Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions
    • Sourjik, V., and Berg, H. C. (2000). Localization of components of the chemotaxis machinery of Escherichia coli using fluorescent protein fusions. Mol. Microbiol. 37, 740-751. doi: 10.1046/j.1365-2958.2000.02044.x
    • (2000) Mol. Microbiol , vol.37 , pp. 740-751
    • Sourjik, V.1    Berg, H.C.2
  • 56
    • 53649100738 scopus 로고    scopus 로고
    • Conversion of red fluorescent protein into a bright blue probe
    • Subach, O. M., Gundorov, I. S., Yoshimura, M., Subach, F. V., Zhang, J., Grüenwald, D., et al. (2008). Conversion of red fluorescent protein into a bright blue probe. Chem.Bbiol. 15, 1116-1124. doi: 10.1016/j.chembiol.2008.08.006
    • (2008) Chem.Bbiol , vol.15 , pp. 1116-1124
    • Subach, O.M.1    Gundorov, I.S.2    Yoshimura, M.3    Subach, F.V.4    Zhang, J.5    Grüenwald, D.6
  • 57
    • 74049125375 scopus 로고    scopus 로고
    • Characterization of an orange acceptor fluorescent protein for sensitized spectral fluorescence resonance energy transfer microscopy using a white-light laser
    • Sun, Y., Booker, C. F., Kumari, S., Day, R. N., Davidson, M., and Periasamy, A. (2009). Characterization of an orange acceptor fluorescent protein for sensitized spectral fluorescence resonance energy transfer microscopy using a white-light laser. J. Biomed. Opt. 14:054009. doi: 10.1117/1.3227036
    • (2009) J. Biomed. Opt , vol.14
    • Sun, Y.1    Booker, C.F.2    Kumari, S.3    Day, R.N.4    Davidson, M.5    Periasamy, A.6
  • 58
    • 25844456826 scopus 로고    scopus 로고
    • Controlling the shape of filamentous cells of Escherichia coli
    • Takeuchi, S., Diluzio, W. R., Weibel, D. B., and Whitesides, G. M. (2005). Controlling the shape of filamentous cells of Escherichia coli. Nano Lett. 5, 1819-1823. doi: 10.1021/nl0507360
    • (2005) Nano Lett , vol.5 , pp. 1819-1823
    • Takeuchi, S.1    Diluzio, W.R.2    Weibel, D.B.3    Whitesides, G.M.4
  • 59
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi, Y., Choi, P. J., Li, G.-W., Chen, H., Babu, M., Hearn, J., et al. (2010). Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 329, 533-538. doi: 10.1126/science.1188308
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.-W.3    Chen, H.4    Babu, M.5    Hearn, J.6
  • 62
    • 66049157868 scopus 로고    scopus 로고
    • Quantitative genome-scale analysis of protein localization in an asymmetric bacterium
    • Werner, J. N., Chen, E. Y., Guberman, J. M., Zippilli, A. R., Irgon, J. J., and Gitai, Z. (2009). Quantitative genome-scale analysis of protein localization in an asymmetric bacterium. Proc. Natl. Acad. Sci. U.S.A. 106, 7858-7863. doi: 10.1073/pnas.0901781106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 7858-7863
    • Werner, J.N.1    Chen, E.Y.2    Guberman, J.M.3    Zippilli, A.R.4    Irgon, J.J.5    Gitai, Z.6
  • 63
    • 0035077003 scopus 로고    scopus 로고
    • HU-GFP and DAPI co-localize on the Escherichia coli nucleoid
    • Wery, M., Woldringh, C. L., and Rouviere-Yaniv, J. (2001). HU-GFP and DAPI co-localize on the Escherichia coli nucleoid. Biochimie 83, 193-200. doi: 10.1016/S0300-9084(01)01254-8
    • (2001) Biochimie , vol.83 , pp. 193-200
    • Wery, M.1    Woldringh, C.L.2    Rouviere-Yaniv, J.3
  • 64
    • 84964693613 scopus 로고    scopus 로고
    • Symmetry and scale orient Min protein patterns in bacterial shape sculptures
    • Wu, F., Van Schie, B., Keymer, J. E., and Dekker, C. (2015). Symmetry and scale orient Min protein patterns in bacterial shape sculptures. Nat. Nanotechnol. doi: 10.1038/nnano.2015.126
    • (2015) Nat. Nanotechnol
    • Wu, F.1    Van Schie, B.2    Keymer, J.E.3    Dekker, C.4
  • 65
    • 84900840105 scopus 로고    scopus 로고
    • An improved monomeric infrared fluorescent protein for neuronal and tumour brain imaging
    • Yu, D., Gustafson, W. C., Han, C., Lafaye, C., Noirclerc-Savoye, M., Ge, W.-P., et al. (2014). An improved monomeric infrared fluorescent protein for neuronal and tumour brain imaging. Nat. Commun. 5:3626. doi: 10.1038/ncomms4626
    • (2014) Nat. Commun , vol.5 , pp. 3626
    • Yu, D.1    Gustafson, W.C.2    Han, C.3    Lafaye, C.4    Noirclerc-Savoye, M.5    Ge, W.-P.6


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