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Volumn 110, Issue 48, 2013, Pages

Structural and genetic analyses reveal the protein SepF as a new membrane anchor for the Z ring

Author keywords

[No Author keywords available]

Indexed keywords

LIPOSOME; MEMBRANE PROTEIN; SEPF PROTEIN; UNCLASSIFIED DRUG;

EID: 84888379584     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1313978110     Document Type: Article
Times cited : (99)

References (49)
  • 1
    • 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(6): 730-737.
    • (2010) Curr Opin Microbiol , vol.13 , Issue.6 , pp. 730-737
    • De Boer, P.A.1
  • 2
    • 0036791675 scopus 로고    scopus 로고
    • A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ
    • Gueiros-Filho FJ, Losick R (2002) A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev 16(19): 2544-2556.
    • (2002) Genes Dev , vol.16 , Issue.19 , pp. 2544-2556
    • Gueiros-Filho, F.J.1    Losick, R.2
  • 3
    • 34247495145 scopus 로고    scopus 로고
    • FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP
    • Small E, et al. (2007) FtsZ polymer-bundling by the Escherichia coli ZapA orthologue, YgfE, involves a conformational change in bound GTP. J Mol Biol 369(1): 210-221.
    • (2007) J Mol Biol , vol.369 , Issue.1 , pp. 210-221
    • Small, E.1
  • 4
    • 79551614816 scopus 로고    scopus 로고
    • Large ring polymers align FtsZ polymers for normal septum formation
    • Gündögdu ME, et al. (2011) Large ring polymers align FtsZ polymers for normal septum formation. EMBO J 30(3): 617-626.
    • (2011) EMBO J , vol.30 , Issue.3 , pp. 617-626
    • Gündögdu, M.E.1
  • 5
    • 69949125297 scopus 로고    scopus 로고
    • Characterization of the FtsZ-interacting septal proteins SepF and Ftn6 in the spherical-celled cyanobacterium Synechocystis strain PCC 6803
    • Marbouty M, Saguez C, Cassier-Chauvat C, Chauvat F (2009) Characterization of the FtsZ-interacting septal proteins SepF and Ftn6 in the spherical-celled cyanobacterium Synechocystis strain PCC 6803. J Bacteriol 191(19): 6178-6185.
    • (2009) J Bacteriol , vol.191 , Issue.19 , pp. 6178-6185
    • Marbouty, M.1    Saguez, C.2    Cassier-Chauvat, C.3    Chauvat, F.4
  • 6
    • 57649165574 scopus 로고    scopus 로고
    • SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length
    • Singh JK, Makde RD, Kumar V, Panda D (2008) SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length. J Biol Chem 283(45): 31116-31124.
    • (2008) J Biol Chem , vol.283 , Issue.45 , pp. 31116-31124
    • Singh, J.K.1    Makde, R.D.2    Kumar, V.3    Panda, D.4
  • 7
    • 0141994961 scopus 로고    scopus 로고
    • Characterization of divIVA and other genes located in the chromosomal region downstream of the dcw cluster in Streptococcus pneumoniae
    • Fadda D, et al. (2003) Characterization of divIVA and other genes located in the chromosomal region downstream of the dcw cluster in Streptococcus pneumoniae. J Bacteriol 185(20): 6209-6214.
    • (2003) J Bacteriol , vol.185 , Issue.20 , pp. 6209-6214
    • Fadda, D.1
  • 8
    • 33645055098 scopus 로고    scopus 로고
    • SepF, a novel FtsZ-interacting protein required for a late step in cell division
    • Hamoen LW, Meile JC, de Jong W, Noirot P, Errington J (2006) SepF, a novel FtsZ-interacting protein required for a late step in cell division. Mol Microbiol 59(3): 989-999.
    • (2006) Mol Microbiol , vol.59 , Issue.3 , pp. 989-999
    • Hamoen, L.W.1    Meile, J.C.2    De Jong, W.3    Noirot, P.4    Errington, J.5
  • 9
    • 16244387910 scopus 로고    scopus 로고
    • Identification of cyanobacterial cell division genes by comparative and mutational analyses
    • Miyagishima SY, Wolk CP, Osteryoung KW (2005) Identification of cyanobacterial cell division genes by comparative and mutational analyses. Mol Microbiol 56(1): 126-143.
    • (2005) Mol Microbiol , vol.56 , Issue.1 , pp. 126-143
    • Miyagishima, S.Y.1    Wolk, C.P.2    Osteryoung, K.W.3
  • 10
    • 24944469539 scopus 로고    scopus 로고
    • Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-ring assembly
    • Jensen SO, Thompson LS, Harry EJ (2005) Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-ring assembly. J Bacteriol 187(18): 6536-6544.
    • (2005) J Bacteriol , vol.187 , Issue.18 , pp. 6536-6544
    • Jensen, S.O.1    Thompson, L.S.2    Harry, E.J.3
  • 11
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • Pichoff S, Lutkenhaus J (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 55(6): 1722-1734.
    • (2005) Mol Microbiol , vol.55 , Issue.6 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 12
    • 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. Proc Natl Acad Sci USA 107(27): 12281-12286.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.27 , pp. 12281-12286
    • Strahl, H.1    Hamoen, L.W.2
  • 13
    • 0031444158 scopus 로고    scopus 로고
    • Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E coli
    • 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(2): 175-185.
    • (1997) Cell , vol.88 , Issue.2 , pp. 175-185
    • Hale, C.A.1    De Boer, P.A.2
  • 14
    • 0037386678 scopus 로고    scopus 로고
    • A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli
    • Geissler B, Elraheb D, MargolinW(2003) A gain-of-function mutation in ftsA bypasses the requirement for the essential cell division gene zipA in Escherichia coli. Proc Natl Acad Sci USA 100(7): 4197-4202.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.7 , pp. 4197-4202
    • Geissler, B.1    Margolinw, E.D.2
  • 15
    • 34648819672 scopus 로고    scopus 로고
    • A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ
    • Singh JK, Makde RD, Kumar V, Panda D (2007) A membrane protein, EzrA, regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ. Biochemistry 46(38): 11013-11022.
    • (2007) Biochemistry , vol.46 , Issue.38 , pp. 11013-11022
    • Singh, J.K.1    Makde, R.D.2    Kumar, V.3    Panda, D.4
  • 16
    • 84865058426 scopus 로고    scopus 로고
    • Bacillus subtilis SepF binds to the C-terminus of FtsZ
    • Król E, et al. (2012) Bacillus subtilis SepF binds to the C-terminus of FtsZ. PLoS ONE 7(8):e43293.
    • (2012) PLoS ONE , vol.7 , Issue.8
    • Król, E.1
  • 17
    • 33744479995 scopus 로고    scopus 로고
    • A new FtsZinteracting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis
    • Ishikawa S, Kawai Y, Hiramatsu K, Kuwano M, Ogasawara N (2006) A new FtsZinteracting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis. Mol Microbiol 60(6): 1364-1380.
    • (2006) Mol Microbiol , vol.60 , Issue.6 , pp. 1364-1380
    • Ishikawa, S.1    Kawai, Y.2    Hiramatsu, K.3    Kuwano, M.4    Ogasawara, N.5
  • 18
    • 0034600952 scopus 로고    scopus 로고
    • The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography
    • Mosyak L, et al. (2000) The bacterial cell-division protein ZipA and its interaction with an FtsZ fragment revealed by X-ray crystallography. EMBO J 19(13): 3179-3191.
    • (2000) EMBO J , vol.19 , Issue.13 , pp. 3179-3191
    • Mosyak, L.1
  • 19
    • 84861151969 scopus 로고    scopus 로고
    • FtsA forms actin-like protofilaments
    • Szwedziak P, Wang Q, Freund SM, Löwe J (2012) FtsA forms actin-like protofilaments. EMBO J 31(10): 2249-2260.
    • (2012) EMBO J , vol.31 , Issue.10 , pp. 2249-2260
    • Szwedziak, P.1    Wang, Q.2    Freund, S.M.3    Löwe, J.4
  • 20
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenstrom P (2010) Dali server: Conservation mapping in 3D. Nucleic Acids Res 38(Web Server issue):W545-W549.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Holm, L.1    Rosenstrom, P.2
  • 21
    • 0034711380 scopus 로고    scopus 로고
    • High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division
    • Katoh E, et al. (2000) High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division. J Mol Biol 304(2): 219-229.
    • (2000) J Mol Biol , vol.304 , Issue.2 , pp. 219-229
    • Katoh, E.1
  • 22
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Ikeuchi Y, Shigi N, Kato J, Nishimura A, Suzuki T (2006) Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol Cell 21(1): 97-108.
    • (2006) Mol Cell , vol.21 , Issue.1 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.3    Nishimura, A.4    Suzuki, T.5
  • 23
    • 0033578438 scopus 로고    scopus 로고
    • Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis
    • Levin PA, Kurtser IG, Grossman AD (1999) Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis. Proc Natl Acad Sci USA 96(17): 9642-9647.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.17 , pp. 9642-9647
    • Levin, P.A.1    Kurtser, I.G.2    Grossman, A.D.3
  • 24
    • 0026544880 scopus 로고
    • Impaired cell division and sporulation of a Bacillus subtilis strain with the ftsA gene deleted
    • Beall B, Lutkenhaus J (1992) Impaired cell division and sporulation of a Bacillus subtilis strain with the ftsA gene deleted. J Bacteriol 174(7): 2398-2403.
    • (1992) J Bacteriol , vol.174 , Issue.7 , pp. 2398-2403
    • Beall, B.1    Lutkenhaus, J.2
  • 25
    • 33644846421 scopus 로고    scopus 로고
    • How proteins produce cellular membrane curvature
    • Zimmerberg J, Kozlov MM (2006) How proteins produce cellular membrane curvature. Nat Rev Mol Cell Biol 7(1): 9-19.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.1 , pp. 9-19
    • Zimmerberg, J.1    Kozlov, M.M.2
  • 26
    • 33748881180 scopus 로고    scopus 로고
    • Prediction of amphipathic in-plane membrane anchors in monotopic proteins using a SVM classifier
    • Sapay N, Guermeur Y, Deléage G (2006) Prediction of amphipathic in-plane membrane anchors in monotopic proteins using a SVM classifier. BMC Bioinformatics 7:255.
    • (2006) BMC Bioinformatics , vol.7 , pp. 255
    • Sapay, N.1    Guermeur, Y.2    Deléage, G.3
  • 27
    • 0037180562 scopus 로고    scopus 로고
    • Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts
    • Szeto TH, Rowland SL, Rothfield LI, King GF (2002) Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts. Proc Natl Acad Sci USA 99(24): 15693-15698.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.24 , pp. 15693-15698
    • Szeto, T.H.1    Rowland, S.L.2    Rothfield, L.I.3    King, G.F.4
  • 28
    • 0037241005 scopus 로고    scopus 로고
    • A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum
    • Hu Z, Lutkenhaus J (2003) A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum. Mol Microbiol 47(2): 345-355.
    • (2003) Mol Microbiol , vol.47 , Issue.2 , pp. 345-355
    • Hu, Z.1    Lutkenhaus, J.2
  • 29
    • 79960913936 scopus 로고    scopus 로고
    • Direct membrane binding by bacterial actin MreB
    • Salje J, van den Ent F, de Boer P, Löwe J (2011) Direct membrane binding by bacterial actin MreB. Mol Cell 43(3): 478-487.
    • (2011) Mol Cell , vol.43 , Issue.3 , pp. 478-487
    • Salje, J.1    Van Den Ent, F.2    De Boer, P.3    Löwe, J.4
  • 30
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly SM, Jess TJ, Price NC (2005) How to study proteins by circular dichroism. Biochim Biophys Acta 1751(2): 119-139.
    • (2005) Biochim Biophys Acta , vol.1751 , Issue.2 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 31
    • 77951896130 scopus 로고    scopus 로고
    • Amphipathic helices and membrane curvature
    • Drin G, Antonny B (2010) Amphipathic helices and membrane curvature. FEBS Lett 584(9): 1840-1847.
    • (2010) FEBS Lett , vol.584 , Issue.9 , pp. 1840-1847
    • Drin, G.1    Antonny, B.2
  • 32
    • 0141925615 scopus 로고    scopus 로고
    • The MinD membrane targeting sequence is a transplantable lipid-binding helix
    • Szeto TH, Rowland SL, Habrukowich CL, King GF (2003) The MinD membrane targeting sequence is a transplantable lipid-binding helix. J Biol Chem 278(41): 40050-40056.
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 40050-40056
    • Szeto, T.H.1    Rowland, S.L.2    Habrukowich, C.L.3    King, G.F.4
  • 33
    • 80052280843 scopus 로고    scopus 로고
    • Cationic lipid enhances assembly of bacterial cell division protein FtsZ: A possible role of bacterial membrane in FtsZ assembly dynamics
    • Kuchibhatla A, Bellare J, Panda D (2011) Cationic lipid enhances assembly of bacterial cell division protein FtsZ: A possible role of bacterial membrane in FtsZ assembly dynamics. Int J Biol Macromol 49(4): 737-741.
    • (2011) Int J Biol Macromol , vol.49 , Issue.4 , pp. 737-741
    • Kuchibhatla, A.1    Bellare, J.2    Panda, D.3
  • 34
    • 0030068218 scopus 로고    scopus 로고
    • Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers
    • Erickson HP, Taylor DW, Taylor KA, Bramhill D (1996) Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc Natl Acad Sci USA 93(1): 519-523.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.1 , pp. 519-523
    • Erickson, H.P.1    Taylor, D.W.2    Taylor, K.A.3    Bramhill, D.4
  • 35
    • 0012580170 scopus 로고
    • Fate of transforming deoxyribonucleic acid in Bacillus Subtilis
    • Venema G, Pritchard RH, Venema-Schroeder T (1965) Fate of transforming deoxyribonucleic acid in Bacillus Subtilis. J Bacteriol 89: 1250-1255.
    • (1965) J Bacteriol , vol.89 , pp. 1250-1255
    • Venema, G.1    Pritchard, R.H.2    Venema-Schroeder, T.3
  • 36
    • 0001134202 scopus 로고
    • Requirements for transformation in Bacillus subtilis
    • Anagnostopoulos C, Spizizen J (1961) Requirements for transformation in Bacillus subtilis. J Bacteriol 81(5): 741-746.
    • (1961) J Bacteriol , vol.81 , Issue.5 , pp. 741-746
    • Anagnostopoulos, C.1    Spizizen, J.2
  • 37
    • 0037115816 scopus 로고    scopus 로고
    • Improving the predictive value of the competence transcription factor (ComK) binding site in Bacillus subtilis using a genomic approach
    • Hamoen LW, Smits WK, de Jong A, Holsappel S, Kuipers OP (2002) Improving the predictive value of the competence transcription factor (ComK) binding site in Bacillus subtilis using a genomic approach. Nucleic Acids Res 30(24): 5517-5528.
    • (2002) Nucleic Acids Res , vol.30 , Issue.24 , pp. 5517-5528
    • Hamoen, L.W.1    Smits, W.K.2    De Jong, A.3    Holsappel, S.4    Kuipers, O.P.5
  • 38
    • 0036855348 scopus 로고    scopus 로고
    • Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis
    • Morimoto T, et al. (2002) Six GTP-binding proteins of the Era/Obg family are essential for cell growth in Bacillus subtilis. Microbiology 148(Pt 11): 3539-3552.
    • (2002) Microbiology , vol.148 , Issue.PART 11 , pp. 3539-3552
    • Morimoto, T.1
  • 39
    • 45749100545 scopus 로고    scopus 로고
    • The functional analysis of YabA, which interacts with DnaA and regulates initiation of chromosome replication in Bacillus subtilis
    • Cho E, Ogasawara N, Ishikawa S (2008) The functional analysis of YabA, which interacts with DnaA and regulates initiation of chromosome replication in Bacillus subtilis. Genes Genet Syst 83(2): 111-125.
    • (2008) Genes Genet Syst , vol.83 , Issue.2 , pp. 111-125
    • Cho, E.1    Ogasawara, N.2    Ishikawa, S.3
  • 41
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Cryst 40(Pt 4): 658-674.
    • (2007) J Appl Cryst , vol.40 , Issue.PART 4 , pp. 658-674
    • McCoy, A.J.1
  • 43
    • 79953763877 scopus 로고    scopus 로고
    • REFMAC5 for the refinement of macromolecular crystal structures
    • Murshudov GN, et al. (2011) REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67(Pt 4): 355-367.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , Issue.PART 4 , pp. 355-367
    • Murshudov, G.N.1
  • 44
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2): 213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 46
    • 46749098901 scopus 로고    scopus 로고
    • The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA
    • Scheffers DJ (2008) The effect of MinC on FtsZ polymerization is pH dependent and can be counteracted by ZapA. FEBS Lett 582(17): 2601-2608.
    • (2008) FEBS Lett , vol.582 , Issue.17 , pp. 2601-2608
    • Scheffers, D.J.1
  • 47
    • 0027257145 scopus 로고
    • The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration
    • Wang X, Lutkenhaus J (1993) The FtsZ protein of Bacillus subtilis is localized at the division site and has GTPase activity that is dependent upon FtsZ concentration. Mol Microbiol 9(3): 435-442.
    • (1993) Mol Microbiol , vol.9 , Issue.3 , pp. 435-442
    • Wang, X.1    Lutkenhaus, J.2
  • 48
    • 40849083594 scopus 로고    scopus 로고
    • K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer
    • Heitkamp T, et al. (2008) K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer. Biochemistry 47(11): 3564-3575.
    • (2008) Biochemistry , vol.47 , Issue.11 , pp. 3564-3575
    • Heitkamp, T.1
  • 49
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ (1959) A rapid method of total lipid extraction and purification. Can J Biochem Physiol 37(8): 911-917.
    • (1959) Can J Biochem Physiol , vol.37 , Issue.8 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.