메뉴 건너뛰기




Volumn 110, Issue 26, 2013, Pages 10586-10591

Erratum: SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid (Proceedings of the National Academy of Sciences of the United States of America (2013) 110, 26, (10586-10591) DOI: 10.1073/pnas.1221036110);SlmA forms a higher-order structure on DNA that inhibits cytokinetic Z-ring formation over the nucleoid

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DIMER; DNA; FTSZ PROTEIN; NUCLEIC ACID; PROTEIN; SLMA PROTEIN; UNCLASSIFIED DRUG;

EID: 84879531614     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1314545110     Document Type: Erratum
Times cited : (78)

References (34)
  • 1
    • 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(6349):161-164.
    • (1991) Nature , vol.354 , Issue.6349 , pp. 161-164
    • Bi, E.F.1    Lutkenhaus, J.2
  • 2
    • 69249126551 scopus 로고    scopus 로고
    • Bacterial cell division: Assembly, maintenance and disassembly of the Z ring
    • Adams DW, Errington J (2009) Bacterial cell division: Assembly, maintenance and disassembly of the Z ring. Nat Rev Microbiol 7(9):642-653.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.9 , pp. 642-653
    • Adams, D.W.1    Errington, J.2
  • 3
    • 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(4):504-528.
    • (2010) Microbiol Mol Biol Rev , vol.74 , Issue.4 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 4
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin W (2005) FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 6(11):862-871.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.11 , pp. 862-871
    • Margolin, W.1
  • 5
    • 44049091371 scopus 로고    scopus 로고
    • Reconstitution of contractile FtsZ rings in liposomes
    • Osawa M, Anderson DE, Erickson HP (2008) Reconstitution of contractile FtsZ rings in liposomes. Science 320(5877):792-794.
    • (2008) Science , vol.320 , Issue.5877 , pp. 792-794
    • Osawa, M.1    Anderson, D.E.2    Erickson, H.P.3
  • 6
    • 84859055009 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism
    • Biteen JS, Goley ED, Shapiro L, Moerner WE (2012) Three-dimensional super-resolution imaging of the midplane protein FtsZ in live Caulobacter crescentus cells using astigmatism. ChemPhysChem 13(4):1007-1012.
    • (2012) ChemPhysChem , vol.13 , Issue.4 , pp. 1007-1012
    • Biteen, J.S.1    Goley, E.D.2    Shapiro, L.3    Moerner, W.E.4
  • 7
    • 36248938686 scopus 로고    scopus 로고
    • The structure of FtsZ filaments in vivo suggests a force-generating role in cell division
    • Li Z, Trimble MJ, Brun YV, Jensen GJ (2007) The structure of FtsZ filaments in vivo suggests a force-generating role in cell division. EMBO J 26(22):4694-4708.
    • (2007) EMBO J , vol.26 , Issue.22 , pp. 4694-4708
    • Li, Z.1    Trimble, M.J.2    Brun, Y.V.3    Jensen, G.J.4
  • 8
    • 77958525927 scopus 로고    scopus 로고
    • In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM)
    • Fu G, et al. (2010) In vivo structure of the E. coli FtsZ-ring revealed by photoactivated localization microscopy (PALM). PLoS ONE 5(9):e12682.
    • (2010) PLoS ONE , vol.5 , Issue.9
    • Fu, G.1
  • 9
    • 79952041482 scopus 로고    scopus 로고
    • Super-resolution imaging of the bacterial cytokinetic protein FtsZ
    • Jennings PC, Cox GC, Monahan LG, Harry EJ (2010) Super-resolution imaging of the bacterial cytokinetic protein FtsZ. Micron 42:336-341.
    • (2010) Micron , vol.42 , pp. 336-341
    • Jennings, P.C.1    Cox, G.C.2    Monahan, L.G.3    Harry, E.J.4
  • 10
    • 0242693139 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial cell division protein FTSZ: Poised at the edge of stability
    • Romberg L, Levin PA (2003) Assembly dynamics of the bacterial cell division protein FTSZ: Poised at the edge of stability. Annu Rev Microbiol 57:125-154.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 125-154
    • Romberg, L.1    Levin, P.A.2
  • 11
    • 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 USA 96(9): 4971-4976.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.9 , pp. 4971-4976
    • Raskin, D.M.1    De Boer, P.A.2
  • 12
    • 34548630230 scopus 로고    scopus 로고
    • Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring
    • Lutkenhaus J (2007) Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring. Annu Rev Biochem 76:539-562.
    • (2007) Annu Rev Biochem , vol.76 , pp. 539-562
    • Lutkenhaus, J.1
  • 13
    • 19444386428 scopus 로고    scopus 로고
    • SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli
    • Bernhardt TG, de Boer PAJ (2005) SlmA, a nucleoid-associated, FtsZ binding protein required for blocking septal ring assembly over chromosomes in E. coli. Mol Cell 18(5): 555-564.
    • (2005) Mol Cell , vol.18 , Issue.5 , pp. 555-564
    • Bernhardt, T.G.1    De Boer Paj2
  • 14
    • 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 Y-L, 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 USA 100(13):7865-7870.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.13 , pp. 7865-7870
    • Shih, Y.-L.1    Le Rothfield T, L.2
  • 15
    • 0024720146 scopus 로고
    • Actively replicating nucleoids influence positioning of division sites in Escherichia coli filaments forming cells lacking DNA
    • Mulder E, Woldringh CL (1989) Actively replicating nucleoids influence positioning of division sites in Escherichia coli filaments forming cells lacking DNA. J Bacteriol 171(8): 4303-4314.
    • (1989) J Bacteriol , vol.171 , Issue.8 , pp. 4303-4314
    • Mulder, E.1    Woldringh, C.L.2
  • 16
    • 78650910561 scopus 로고    scopus 로고
    • Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check
    • Tonthat NK, et al. (2011) Molecular mechanism by which the nucleoid occlusion factor, SlmA, keeps cytokinesis in check. EMBO J 30(1):154-164.
    • (2011) EMBO J , vol.30 , Issue.1 , pp. 154-164
    • Tonthat, N.K.1
  • 17
    • 79952741894 scopus 로고    scopus 로고
    • Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist
    • Cho H, McManus HR, Dove SL, Bernhardt TG (2011) Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist. Proc Natl Acad Sci USA 108(9):3773-3778.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.9 , pp. 3773-3778
    • Cho, H.1    McManus, H.R.2    Dove, S.L.3    Bernhardt, T.G.4
  • 18
    • 2942752105 scopus 로고    scopus 로고
    • Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis
    • Wu LJ, Errington J (2004) Coordination of cell division and chromosome segregation by a nucleoid occlusion protein in Bacillus subtilis. Cell 117(7):915-925.
    • (2004) Cell , vol.117 , Issue.7 , pp. 915-925
    • Wu, L.J.1    Errington, J.2
  • 19
    • 67650435786 scopus 로고    scopus 로고
    • Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation
    • Wu LJ, et al. (2009) Noc protein binds to specific DNA sequences to coordinate cell division with chromosome segregation. EMBO J 28(13):1940-1952.
    • (2009) EMBO J , vol.28 , Issue.13 , pp. 1940-1952
    • Wu, L.J.1
  • 20
    • 79958167357 scopus 로고    scopus 로고
    • Conformational changes of FtsZ reported by tryptophan mutants
    • Chen Y, Erickson HP (2011) Conformational changes of FtsZ reported by tryptophan mutants. Biochemistry 50(21):4675-4684.
    • (2011) Biochemistry , vol.50 , Issue.21 , pp. 4675-4684
    • Chen, Y.1    Erickson, H.P.2
  • 21
    • 84859619053 scopus 로고    scopus 로고
    • SulA inhibits assembly of FtsZ by a simple sequestration mechanism
    • Chen Y, Milam SL, Erickson HP (2012) SulA inhibits assembly of FtsZ by a simple sequestration mechanism. Biochemistry 51(14):3100-3109.
    • (2012) Biochemistry , vol.51 , Issue.14 , pp. 3100-3109
    • Chen, Y.1    Milam, S.L.2    Erickson, H.P.3
  • 22
    • 67249144043 scopus 로고    scopus 로고
    • FtsZ condensates: An in vitro electron microscopy study
    • Popp D, Iwasa M, Narita A, Erickson HP, Maéda Y (2009) FtsZ condensates: An in vitro electron microscopy study. Biopolymers 91(5):340-350.
    • (2009) Biopolymers , vol.91 , Issue.5 , pp. 340-350
    • Popp, D.1    Iwasa, M.2    Narita, A.3    Erickson, H.P.4    Maéda, Y.5
  • 23
    • 4344620779 scopus 로고    scopus 로고
    • Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules
    • Burgess SA, Walker ML, Thirumurugan K, Trinick J, Knight PJ (2004) Use of negative stain and single-particle image processing to explore dynamic properties of flexible macromolecules. J Struct Biol 147(3):247-258.
    • (2004) J Struct Biol , vol.147 , Issue.3 , pp. 247-258
    • Burgess, S.A.1    Walker, M.L.2    Thirumurugan, K.3    Trinick, J.4    Knight, P.J.5
  • 24
    • 20544432535 scopus 로고    scopus 로고
    • The TetR family of transcriptional repressors
    • Ramos JL, et al. (2005) The TetR family of transcriptional repressors. Microbiol Mol Biol Rev 69(2):326-356.
    • (2005) Microbiol Mol Biol Rev , vol.69 , Issue.2 , pp. 326-356
    • Ramos, J.L.1
  • 25
    • 0035824388 scopus 로고    scopus 로고
    • Structural mechanisms of QacR induction and multidrug recognition
    • Schumacher MA, et al. (2001) Structural mechanisms of QacR induction and multidrug recognition. Science 294(5549):2158-2163.
    • (2001) Science , vol.294 , Issue.5549 , pp. 2158-2163
    • Schumacher, M.A.1
  • 26
    • 72449161765 scopus 로고    scopus 로고
    • Structural plasticity and distinct drug-binding modes of LfrR, a mycobacterial efflux pump regulator
    • Bellinzoni M, et al. (2009) Structural plasticity and distinct drug-binding modes of LfrR, a mycobacterial efflux pump regulator. J Bacteriol 191(24):7531-7537.
    • (2009) J Bacteriol , vol.191 , Issue.24 , pp. 7531-7537
    • Bellinzoni, M.1
  • 27
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89(2):1237-1250.
    • (2005) Biophys J , vol.89 , Issue.2 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 28
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76(6):2879-2886.
    • (1999) Biophys J , vol.76 , Issue.6 , pp. 2879-2886
    • Svergun, D.I.1
  • 29
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80(6):2946-2953.
    • (2001) Biophys J , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 30
    • 84874784097 scopus 로고    scopus 로고
    • Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome
    • Cho H, Bernhardt TG (2013) Identification of the SlmA active site responsible for blocking bacterial cytokinetic ring assembly over the chromosome. PLOS Genet 9(2):e1003304.
    • (2013) PLOS Genet , vol.9 , Issue.2
    • Cho, H.1    Bernhardt, T.G.2
  • 31
    • 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(13):1167-1173.
    • (2004) Curr Biol , vol.14 , Issue.13 , pp. 1167-1173
    • Thanedar, S.1    Margolin, W.2
  • 32
    • 84860828333 scopus 로고    scopus 로고
    • Membrane protein expression triggers chromosomal locus repositioning in bacteria
    • Libby EA, Roggiani M, Goulian M (2012) Membrane protein expression triggers chromosomal locus repositioning in bacteria. Proc Natl Acad Sci USA 109(19):7445-7450.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.19 , pp. 7445-7450
    • Libby, E.A.1    Roggiani, M.2    Goulian, M.3
  • 33
    • 84860822838 scopus 로고    scopus 로고
    • Robustness and accuracy of cell division in Escherichia coli in diverse cell shapes
    • Männik J, et al. (2012) Robustness and accuracy of cell division in Escherichia coli in diverse cell shapes. Proc Natl Acad Sci USA 109(18):6957-6962.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.18 , pp. 6957-6962
    • Männik, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.