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Volumn 194, Issue 23, 2012, Pages 6369-6371

The price of tags in protein localization studies

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FTSZ PROTEIN; HYBRID PROTEIN; MIN PROTEIN; MREB PROTEIN; PROTEIN TAG; UNCLASSIFIED DRUG; YELLOW FLUORESCENT PROTEIN;

EID: 84871060283     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01640-12     Document Type: Note
Times cited : (52)

References (35)
  • 2
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape
    • 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) E. coli. EMBO J. , vol.28 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    Boer, P.A.D.4
  • 3
    • 84859484529 scopus 로고    scopus 로고
    • Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins
    • Buske PJ, Levin PA. 2012. Extreme C terminus of bacterial cytoskeletal protein FtsZ plays fundamental role in assembly independent of modulatory proteins. J. Biol. Chem. 287:10945-10957.
    • (2012) J. Biol. Chem. , vol.287 , pp. 10945-10957
    • Buske, P.J.1    Levin, P.A.2
  • 4
    • 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
    • Soufo, H.J.D.1    Graumann, P.L.2
  • 5
    • 79960083390 scopus 로고    scopus 로고
    • Processive movement of MreBassociated cell wall biosynthetic complexes in bacteria
    • Dominguez-Escobar J, et al. 2011. Processive movement of MreBassociated cell wall biosynthetic complexes in bacteria. Science 333:225-228.
    • (2011) Science , vol.333 , pp. 225-228
    • Dominguez-escobar, J.1
  • 6
    • 80052009110 scopus 로고    scopus 로고
    • Bacterial cell wall: thinking globally, actin locally
    • Eraso JM, Margolin W. 2011. Bacterial cell wall: thinking globally, actin locally. Curr. Biol. 21:R628-630.
    • (2011) Curr. Biol. , vol.21
    • Eraso, J.M.1    Margolin, W.2
  • 8
    • 79960075043 scopus 로고    scopus 로고
    • Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments
    • Garner EC, et al. 2011. Coupled, circumferential motions of the cell wall synthesis machinery and MreB filaments in B. subtilis. Science 333:222-225.
    • (2011) B. subtilis. Science , vol.333 , pp. 222-225
    • Garner, E.C.1
  • 9
    • 4644282820 scopus 로고    scopus 로고
    • Complex spatial distribution and dynamics of an abundant Escherichia coli outer membrane protein
    • Gibbs KA, et al. 2004. Complex spatial distribution and dynamics of an abundant Escherichia coli outer membrane protein, LamB. Mol. Microbiol. 53:1771-1783.
    • (2004) LamB. Mol. Microbiol. , vol.53 , pp. 1771-1783
    • Gibbs, K.A.1
  • 10
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division
    • Hale CA, de Boer PA. 1997. Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli. Cell 88:175-185.
    • (1997) E. coli. Cell , vol.88 , pp. 175-185
    • Hale, C.A.1    Boer, P.A.D.2
  • 11
    • 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, 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.
    • (1999) Mol. Microbiol. , vol.34 , pp. 82-90
    • Hu, Z.1    Lutkenhaus, J.2
  • 12
    • 79952041482 scopus 로고    scopus 로고
    • Super-resolution imaging of the bacterial cytokinetic protein FtsZ
    • Jennings PC, Cox GC, Monahan LG, Harry EJ. 2011. Super-resolution imaging of the bacterial cytokinetic protein FtsZ. Micron 42:336-341.
    • (2011) Micron , vol.42 , pp. 336-341
    • Jennings, P.C.1    Cox, G.C.2    Monahan, L.G.3    Harry, E.J.4
  • 13
    • 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
  • 14
    • 84860361727 scopus 로고    scopus 로고
    • Segregation of molecules at cell division reveals native protein localization
    • Landgraf D, Okumus B, Chien P, Baker TA, Paulsson J. 2012. Segregation of molecules at cell division reveals native protein localization. Nat. Methods 9:480-482.
    • (2012) Nat. Methods , vol.9 , pp. 480-482
    • Landgraf, D.1    Okumus, B.2    Chien, P.3    Baker, T.A.4    Paulsson, J.5
  • 15
    • 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. Proc. Natl. Acad. Sci. U. S. A. 93:12998-13003.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 12998-13003
    • Ma, X.1    Ehrhardt, D.W.2    Margolin, W.3
  • 16
    • 0032786248 scopus 로고    scopus 로고
    • Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ
    • Ma X, Margolin W. 1999. Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ. J. Bacteriol. 181:7531-7544.
    • (1999) J. Bacteriol. , vol.181 , pp. 7531-7544
    • Ma, X.1    Margolin, W.2
  • 17
    • 84862490620 scopus 로고    scopus 로고
    • Subcellular localization of RNA and proteins in prokaryotes
    • Nevo-Dinur K, Govindarajan S, Amster-Choder O. 2012. Subcellular localization of RNA and proteins in prokaryotes. Trends Genet. 28:314-322.
    • (2012) Trends Genet. , vol.28 , pp. 314-322
    • Nevo-dinur, K.1    Govindarajan, S.2    Amster-choder, O.3
  • 18
    • 34247349124 scopus 로고    scopus 로고
    • A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis
    • Peters PC, Migocki MD, Thoni C, Harry EJ. 2007. A new assembly pathway for the cytokinetic Z ring from a dynamic helical structure in vegetatively growing cells of Bacillus subtilis. Mol. Microbiol. 64:487-499.
    • (2007) Mol. Microbiol. , vol.64 , pp. 487-499
    • Peters, P.C.1    Migocki, M.D.2    Thoni, C.3    Harry, E.J.4
  • 19
    • 0033609139 scopus 로고    scopus 로고
    • Rapid pole-to-pole oscillation of a protein required for directing division to the middle of Escherichia coli.
    • Raskin DM, de Boer PA. 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.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 4971-4976
    • Raskin, D.M.1    Boer, P.A.D.2
  • 20
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje J, van den Ent F, de Boer P, Löwe J. 2012. Direct membrane binding by bacterial actin MreB. Mol. Cell 43:478-487.
    • (2012) Mol. Cell , vol.43 , pp. 478-487
    • Salje, J.1    Ent, F.V.D.2    Boer, P.D.3    Löwe, J.4
  • 21
    • 27944489446 scopus 로고    scopus 로고
    • The MreB and Min cytoskeletallike systems play independent roles in prokaryotic polar differentiation
    • Shih YL, Kawagishi I, Rothfield L. 2005. The MreB and Min cytoskeletallike systems play independent roles in prokaryotic polar differentiation. Mol. Microbiol. 58:917-928.
    • (2005) Mol. Microbiol. , vol.58 , pp. 917-928
    • Shih, Y.L.1    Kawagishi, I.2    Rothfield, L.3
  • 22
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih YL, Le T, Rothfield L. 2003. Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc. Natl. Acad. Sci. U. S. A. 100:7865-7870.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7865-7870
    • Shih, Y.L.1    Le, T.2    Rothfield, L.3
  • 23
    • 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
  • 24
    • 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
  • 25
    • 79955040193 scopus 로고    scopus 로고
    • Long helical filaments are not seen encircling cells in electron cryotomograms of rod-shaped bacteria
    • Swulius MT, et al. 2011. Long helical filaments are not seen encircling cells in electron cryotomograms of rod-shaped bacteria. Biochem. Biophys. Res. Commun. 407:650-655.
    • (2011) Biochem. Biophys. Res. Commun. , vol.407 , pp. 650-655
    • Swulius, M.T.1
  • 26
    • 84871055385 scopus 로고    scopus 로고
    • The helical MreB cytoskeleton in Escherichia coli MC1000/pLE7 is an artifact of the N-terminal yellow fluorescent protein tag
    • Swulius MT, Jensen GJ. 2012. The helical MreB cytoskeleton in Escherichia coli MC1000/pLE7 is an artifact of the N-terminal yellow fluorescent protein tag. J. Bacteriol. 194:6382-6386.
    • (2012) J. Bacteriol. , vol.194 , pp. 6382-6386
    • Swulius, M.T.1    Jensen, G.J.2
  • 28
    • 33846818898 scopus 로고    scopus 로고
    • RNaseE and the other constituents of theRNAdegradosome are components of the bacterial cytoskeleton
    • Taghbalout A, Rothfield L. 2007. RNaseE and the other constituents of theRNAdegradosome are components of the bacterial cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 104:1667-1672.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 1667-1672
    • Taghbalout, A.1    Rothfield, L.2
  • 29
    • 77953985369 scopus 로고    scopus 로고
    • Self-assembly of the bacterial cytoskeletonassociated RNA helicase B protein into polymeric filamentous structures
    • Taghbalout A, Yang Q. 2010. Self-assembly of the bacterial cytoskeletonassociated RNA helicase B protein into polymeric filamentous structures. J. Bacteriol. 192:3222-3226.
    • (2010) J. Bacteriol. , vol.192 , pp. 3222-3226
    • Taghbalout, A.1    Yang, Q.2
  • 30
    • 3142602980 scopus 로고    scopus 로고
    • FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli
    • Thanedar S, Margolin W. 2004. FtsZ exhibits rapid movement and oscillation waves in helix-like patterns in Escherichia coli. Curr. Biol. 14:1167-1173.
    • (2004) Curr. Biol. , vol.14 , pp. 1167-1173
    • Thanedar, S.1    Margolin, W.2
  • 31
    • 84859852186 scopus 로고    scopus 로고
    • Image analysis in fluorescence microscopy: bacterial dynamics as a case study
    • van Teeffelen S, Shaevitz JW, Gitai Z. 2012. Image analysis in fluorescence microscopy: bacterial dynamics as a case study. Bioessays 34:427-436.
    • (2012) Bioessays , vol.34 , pp. 427-436
    • Teeffelen, S.V.1    Shaevitz, J.W.2    Gitai, Z.3
  • 32
    • 80052431295 scopus 로고    scopus 로고
    • The bacterial actin MreB rotates, and rotation depends on cell-wall assembly
    • van Teeffelen S, et al. 2011. The bacterial actin MreB rotates, and rotation depends on cell-wall assembly. Proc. Natl. Acad. Sci. U. S. A. 108:15822-15827.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 15822-15827
    • Teeffelen, S.V.1
  • 33
    • 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. Proc. Natl. Acad. Sci. U. S. A. 104:17795-17800.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 17795-17800
    • Vats, P.1    Rothfield, L.2
  • 34
    • 62949149564 scopus 로고    scopus 로고
    • Assembly of the MreB-associated cytoskeletal ring of Escherichia coli
    • Vats P, Shih YL, Rothfield L. 2009. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.