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Volumn 73, Issue 4, 2009, Pages 534-552

Phylogenetic analysis identifies many uncharacterized actin-like proteins (Alps) in bacteria: Regulated polymerization, dynamic instability and treadmilling in Alp7A

Author keywords

[No Author keywords available]

Indexed keywords

ALP7A PROTEIN; BACTERIAL PROTEIN; HYBRID PROTEIN; UNCLASSIFIED DRUG;

EID: 70350141267     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2009.06771.x     Document Type: Article
Times cited : (103)

References (76)
  • 1
    • 33845772164 scopus 로고    scopus 로고
    • DNA segregation by the bacterial actin AlfA during Bacillus subtilis growth and development
    • DOI 10.1038/sj.emboj.7601443, PII 7601443
    • Becker, E., Herrera, N.C., Gunderson, F.Q., Derman, A.I., Dance, A.L., Sims, J., et al. (2006) DNA segregation by the bacterial actin AIfA during Bacillus subtllis growth and development. EMBO J 25: 5919-5931. (Pubitemid 46001323)
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5919-5931
    • Becker, E.1    Herrera, N.C.2    Gunderson, F.Q.3    Derman, A.I.4    Dance, A.L.5    Sims, J.6    Larsen, R.A.7    Pogliano, J.8
  • 2
    • 0033019429 scopus 로고    scopus 로고
    • New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites
    • Belmont, L.D., Patterson, G.M., and Drubin, D.G. (1999) New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J Cell Sci 112: 1325-1336.
    • (1999) J Cell Sci , vol.112 , pp. 1325-1336
    • Belmont, L.D.1    Patterson, G.M.2    Drubin, D.G.3
  • 3
    • 0033602146 scopus 로고    scopus 로고
    • Self-regulated polymerization of the actin-related protein Arp1
    • Bingham, J.B., and Schroer, T.A. (1999) Self-regulated polymerization of the actin-related protein Arp1. Curr Biol 9: 223-226.
    • (1999) Curr Biol , vol.9 , pp. 223-226
    • Bingham, J.B.1    Schroer, T.A.2
  • 4
    • 0026687729 scopus 로고
    • An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins
    • Bork, P., Sander, C., and Valencia, A. (1992) An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci USA 89: 7290-7294.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7290-7294
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 5
    • 36849033421 scopus 로고    scopus 로고
    • In vivo visualization of type II plasmid segregation: Bacterial actin filaments pushing plasmids
    • Campbell, CS., and Mullins, R.D. (2007) In vivo visualization of type II plasmid segregation: bacterial actin filaments pushing plasmids. J Cell Biol 179: 1059-1066.
    • (2007) J Cell Biol , vol.179 , pp. 1059-1066
    • Campbell, C.S.1    Mullins, R.D.2
  • 7
    • 34250205203 scopus 로고    scopus 로고
    • Nuclear actin and actin-related proteins in chromatin dynamics
    • DOI 10.1016/j.ceb.2007.04.009, PII S0955067407000610, Nucleus and Gene Expression
    • Chen, M., and Shen, X. (2007) Nuclear actin and actinrelated proteins in chromatin dynamics. Curr Opin Cell Biol 19: 326-330. (Pubitemid 46899510)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.3 , pp. 326-330
    • Chen, M.1    Shen, X.2
  • 8
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rodshaped cell
    • Daniel, R.A., and Errington, J. (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rodshaped cell. Cell 113: 767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 9
    • 19344373111 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex: Addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2
    • Dayel, M.J., and Mullins, R.D. (2004) Activation of Arp2/3 complex: addition of the first subunit of the new filament by a WASP protein triggers rapid ATP hydrolysis on Arp2. PLoS Biol 2: 0476-0485.
    • (2004) PLoS Biol , vol.2 , pp. 476-485
    • Dayel, M.J.1    Mullins, R.D.2
  • 10
    • 0035910044 scopus 로고    scopus 로고
    • Arp2/3 complex requires hydrolysable ATP for nucleation of new actin filaments
    • Dayel, M.J., Holleran, E.A., and Mullins, R.D. (2001) Arp2/3 complex requires hydrolysable ATP for nucleation of new actin filaments. Proc Natl Acad Sci USA 98:14871-14876.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14871-14876
    • Dayel, M.J.1    Holleran, E.A.2    Mullins, R.D.3
  • 11
    • 0027457077 scopus 로고
    • A signal sequence is not required for protein export in prlA mutants of Escherichia coli
    • Derman, A.I., Puziss, J.W., Bassford, P.J., Jr, and Beckwith, J. (1993) A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J 12: 879-888. (Pubitemid 23095836)
    • (1993) EMBO Journal , vol.12 , Issue.3 , pp. 879-888
    • Derman, A.I.1    Puziss, J.W.2    Bassford Jr., P.J.3    Beckwith, J.4
  • 12
    • 0036010591 scopus 로고    scopus 로고
    • Bacterial actins? An evolutionary perspective
    • Doolittle, R.F., and York, A.L. (2002) Bacterial actins? An evolutionary perspective. Bioessays 24: 293-296.
    • (2002) Bioessays , vol.24 , pp. 293-296
    • Doolittle, R.F.1    York, A.L.2
  • 14
    • 0015222721 scopus 로고
    • Fate of transforming DNA after uptake competent Bacillus subtilis
    • Dubnau, D., and Davidoff-Abelson, R. (1971) Fate of transforming DNA after uptake competent Bacillus subtilis. J Mol Biol 56: 209-221.
    • (1971) J Mol Biol , vol.56 , pp. 209-221
    • Dubnau, D.1    Davidoff-Abelson, R.2
  • 15
    • 0035846596 scopus 로고    scopus 로고
    • Molecular evolution: Actin's long lost relative found
    • Egelman, E.H. (2001) Molecular evolution: actin's long lost relative found. Curr Biol 11: R1022-R1024.
    • (2001) Curr Biol , vol.11
    • Egelman, E.H.1
  • 16
    • 0034675921 scopus 로고    scopus 로고
    • Crystal structure of the cell division protein FtsA from Thermotoga maritima
    • van den Ent, F., and Löwe, 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    Löwe, J.2
  • 17
    • 0035817819 scopus 로고    scopus 로고
    • Prokaryotic origin of the actin cytoskeleton
    • van den Ent, F., Amos, L., and Löwe, J. (2001) Prokaryotic origin of the actin cytoskeleton. Nature 413: 39-44.
    • (2001) Nature , vol.413 , pp. 39-44
    • Van Den Ent, F.1    Amos, L.2    Löwe, J.3
  • 18
    • 12244298896 scopus 로고    scopus 로고
    • F-actin-like filaments formed by plasmid segregation protein ParM
    • DOI 10.1093/emboj/cdf672
    • van den Ent, F., Mailer-Jensen, J., Amos, L.A., Gerdes, K., and Löwe, J. (2002) F-actin-like filaments formed by plasmid segregation protein ParM. EMBO J 21: 6935-6943. (Pubitemid 36014565)
    • (2002) EMBO Journal , vol.21 , Issue.24 , pp. 6935-6943
    • Van Den Ent, F.1    Moller-Jensen, J.2    Amos, L.A.3    Gerdes, K.4    Lowe, J.5
  • 19
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge, R.M., Divakaruni, A.V., and Gober, J.W. (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
  • 21
    • 0037006805 scopus 로고    scopus 로고
    • A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure
    • DOI 10.1016/S0960-9822(02)00742-X, PII S096098220200742X
    • Galkin, V.E., VanLoock, M.S., Orlova, A., and Egelman, E.H. (2002) A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin's sequence and structure. Curr Biol 12: 570-575. (Pubitemid 34271371)
    • (2002) Current Biology , vol.12 , Issue.7 , pp. 570-575
    • Galkin, V.E.1    Vanloock, M.S.2    Orlova, A.3    Egelman, E.H.4
  • 22
    • 8344247018 scopus 로고    scopus 로고
    • Dynamic instability in a DNA-segregating prokaryotic actin homologue
    • Garner, E.C, Campbell, CS., and Mullins, R.D. (2004) Dynamic instability in a DNA-segregating prokaryotic actin homologue. Science 306: 1021-1025.
    • (2004) Science , vol.306 , pp. 1021-1025
    • Garner, E.C.1    Campbell, C.S.2    Mullins, R.D.3
  • 23
    • 33847675333 scopus 로고    scopus 로고
    • Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homologue
    • Garner, E.C, Campbell, CS., Weibel, D.B., and Mullins, R.D. (2007) Reconstitution of DNA segregation driven by assembly of a prokaryotic actin homologue. Science 315: 1270-1274.
    • (2007) Science , vol.315 , pp. 1270-1274
    • Garner, E.C.1    Campbell, C.S.2    Weibel, D.B.3    Mullins, R.D.4
  • 25
    • 44449133509 scopus 로고    scopus 로고
    • Actin in the endocytic pathway: From yeast to mammals
    • Girao, H., Geli, M.I., and Idrissi, F.Z. (2008) Actin in the endocytic pathway: from yeast to mammals. FEBS Lett 582: 2112-2119.
    • (2008) FEBS Lett , vol.582 , pp. 2112-2119
    • Girao, H.1    Geli, M.I.2    Idrissi, F.Z.3
  • 27
    • 35848966372 scopus 로고    scopus 로고
    • Cytoskeletal elements in bacteria
    • Graumann, P.L. (2007) Cytoskeletal elements in bacteria. Annu Rev Microbiol 61: 589-618.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 589-618
    • Graumann, P.L.1
  • 28
    • 0030597337 scopus 로고    scopus 로고
    • Plasmids for ectopic integration in Bacillus subtllis
    • Guérout-Fleury, A.-M., Frandsen, N., and Stragier, P. (1996) Plasmids for ectopic integration in Bacillus subtllis. Gene 180:57-61.
    • (1996) Gene , vol.180 , pp. 57-61
    • Guérout-Fleury, A.-M.1    Frandsen, N.2    Stragier, P.3
  • 29
    • 0000075317 scopus 로고
    • Techniques for transformation of E. coll
    • Glover, D.M. (ed.). Oxford: IRL Press
    • Hanahan, D. (1985) Techniques for transformation of E. coll. In DNA Cloning: A Practical Approach. Glover, D.M. (ed.). Oxford: IRL Press, pp. 109-135.
    • (1985) DNA Cloning: A Practical Approach , pp. 109-135
    • Hanahan, D.1
  • 30
    • 0029948487 scopus 로고    scopus 로고
    • The sugar kinase/heat shock protein 70/actin superfamily: Implications of conserved structure for mechanism
    • Hurley, J.H. (1996) The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism. Annu Rev Biophys Blomol Struct 25:137-162.
    • (1996) Annu Rev Biophys Blomol Struct , vol.25 , pp. 137-162
    • Hurley, J.H.1
  • 31
    • 33645223518 scopus 로고    scopus 로고
    • Conjugational transfer kinetics of pLS20 between Bacillus subtilis in liquid medium
    • Itaya, M., Sakaya, N., Matsunaga, S., Fujita, K., and Kaneko, S. (2006) Conjugational transfer kinetics of pLS20 between Bacillus subtilis in liquid medium. Biosci Biotechnol Biochem 70: 740-742.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 740-742
    • Itaya, M.1    Sakaya, N.2    Matsunaga, S.3    Fujita, K.4    Kaneko, S.5
  • 33
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • Jones, L., Carballido-López, R., and 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.1    Carballido-López, R.2    Errington, J.3
  • 34
    • 50349083508 scopus 로고    scopus 로고
    • The actinome of Dictyostelium discoideum in comparison to actins and actin-related proteins from other organisms
    • Joseph, J.M., Fey, P., Ramalingam, N., Liu, X.I., Rohlfs, M., Noegel, A.A., et al. (2008) The actinome of Dictyostelium discoideum in comparison to actins and actin-related proteins from other organisms. PLoS ONE 3: e2654.
    • (2008) PLoS ONE , vol.3
    • Joseph, J.M.1    Fey, P.2    Ramalingam, N.3    Liu, X.I.4    Rohlfs, M.5    Noegel, A.A.6
  • 35
    • 0028944687 scopus 로고
    • The actin fold
    • Kabsch, W., and Holmes, K.C. (1995) The actin fold. FASEB J 9: 167-174.
    • (1995) FASEB J , vol.9 , pp. 167-174
    • Kabsch, W.1    Holmes, K.C.2
  • 36
    • 0024988340 scopus 로고
    • Atomic structure of the actin:DNase i complex
    • DOI 10.1038/347037a0
    • Kabsch, W., Mannherz, H.G., Suck, D., Pai, E.F., and Holmes, K.C. (1990) Atomic structure of the actin: DNase I complex. Nature 347: 37-44. (Pubitemid 20280179)
    • (1990) Nature , vol.347 , Issue.6288 , pp. 37-44
    • Kabsch, W.1    Mannherz, H.G.2    Suck, D.3    Pai, E.F.4    Holmes, K.C.5
  • 37
    • 0036250284 scopus 로고    scopus 로고
    • Construction and application of epitope- And green fluorescent protein-tagging integration vectors for Bacillus subtilis
    • DOI 10.1128/AEM.68.5.2624-2628.2002
    • Kaltwasser, M., Wiegert, T., and Schumann, W. (2002) Construction and application of epitope- and green fluorscent protein-tagging integration vectors for Bacillus subtilis. Appl Environ Microbiol 68: 2624-2628. (Pubitemid 34477871)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.5 , pp. 2624-2628
    • Kaltwasser, M.1    Wiegert, T.2    Schumann, W.3
  • 38
    • 33746655349 scopus 로고    scopus 로고
    • Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus
    • Kim, S.Y., Gitai, Z., Kinkhabwala, A., Shapiro, L., and Moerner, W.E. (2006) Single molecules of the bacterial actin MreB undergo directed treadmilling motion in Caulobacter crescentus. Proc Natl Acad USA 103: 10929-10934.
    • (2006) Proc Natl Acad USA , vol.103 , pp. 10929-10934
    • Kim, S.Y.1    Gitai, Z.2    Kinkhabwala, A.3    Shapiro, L.4    Moerner, W.E.5
  • 39
    • 30844471175 scopus 로고    scopus 로고
    • Magnetosomes are cell membrane imaginations organized by the actin-like protein MamK
    • DOI 10.1126/science.1123231
    • Komeili, A., Li, Z., Newman, D.K., and Jensen, G.J. (2006) Magnetosomes are cell membrane invaginations organized by the actin-like protein MamK. Science 311: 242-245. (Pubitemid 43108192)
    • (2006) Science , vol.311 , Issue.5758 , pp. 242-245
    • Komeili, A.1    Li, Z.2    Newman, D.K.3    Jensen, G.J.4
  • 40
    • 33744779420 scopus 로고    scopus 로고
    • Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Förster radius
    • Kremers, G.J., Goedhard, J., van Munster, E.B., and Gadella, T.W., Jr (2006) Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Förster radius. Biochemistry 45: 6570-6580.
    • (2006) Biochemistry , vol.45 , pp. 6570-6580
    • Kremers, G.J.1    Goedhard, J.2    Van Munster, E.B.3    Gadella Jr., T.W.4
  • 42
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • Le Clainche, C., and Carlier, M.-F. (2008) Regulation of actin assembly associated with protrusion and adhesion in cell migration. Physiol Rev 88: 489-513.
    • (2008) Physiol Rev , vol.88 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.-F.2
  • 44
    • 0030008710 scopus 로고    scopus 로고
    • P1 plasmid partition: A mutational analysis of ParB
    • DOI 10.1006/jmbi.1996.0326
    • Lobocka, M., and Yarmolinsky, M. (1996) P1 plasmid partition: a mutational analysis of ParB. J Mol Biol 259: 366-382. (Pubitemid 26179644)
    • (1996) Journal of Molecular Biology , vol.259 , Issue.3 , pp. 366-382
    • Lobocka, M.1    Yarmolinsky, M.2
  • 45
    • 0029162683 scopus 로고
    • Characterization of the replication region of the Bacillus subtilis plasmid pLS20: A novel type of replicon
    • Meijer, W.J., de Boer, A.J., van Tongeren, S., Venema, G., and Bron, S. (1995) Characterization of the replication region of the Bacillus subtilis plasmid pLS20: a novel type of replicon. Nucleic Acids Res 23: 3214-3223.
    • (1995) Nucleic Acids Res , vol.23 , pp. 3214-3223
    • Meijer, W.J.1    De Boer, A.J.2    Van Tongeren, S.3    Venema, G.4    Bron, S.5
  • 46
    • 0346980557 scopus 로고    scopus 로고
    • Bacterial Mitosis: ParM of Plasmid R1 Moves Plasmid DNA by an Actin-like Insertional Polymerization Mechanism
    • DOI 10.1016/S1097-2765(03)00451-9
    • Mailer-Jensen, J., Borch, J., Dam, M., Jensen, R.B., Roepstorff, P., and Gerdes, K. (2003) Bacterial mitosis: ParM of plasmid R1 moves plasmid DNA by an actin-like insertional polymerization mechanism. Mol Cell 12: 1477-1487. (Pubitemid 38037016)
    • (2003) Molecular Cell , vol.12 , Issue.6 , pp. 1477-1487
    • Moller-Jensen, J.1    Borch, J.2    Dam, M.3    Jensen, R.B.4    Roepstorff, P.5    Gerdes, K.6
  • 47
    • 0037124325 scopus 로고    scopus 로고
    • Prokaryotic DNA segregation by an actin-like filament
    • DOI 10.1093/emboj/cdf320
    • Mailer-Jensen, J., Jensen, R., Lowe, J., and Gerdes, K. (2002) Prokaryotic DNA segregation by an actin-like filament. EMBO J 21: 3119-3127. (Pubitemid 34670395)
    • (2002) EMBO Journal , vol.21 , Issue.12 , pp. 3119-3127
    • Moller-Jensen, J.1    Jensen, R.B.2    Lowe, J.3    Gerdes, K.4
  • 48
    • 28644433381 scopus 로고    scopus 로고
    • Sequence and comparative genomic analysis of actin-related proteins
    • DOI 10.1091/mbc.E05-06-0508
    • Muller, J., Oma, Y., Vallar, L., Friederich, E., Poch, O., and Winsor, B. (2005) Sequence and comparative genomic analysis of actin-related proteins. Mol Biol Cell 16: 5736-5748. (Pubitemid 41752222)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.12 , pp. 5736-5748
    • Muller, J.1    Oma, Y.2    Vallar, L.3    Friederich, E.4    Poch, O.5    Winsor, B.6
  • 50
    • 0026805942 scopus 로고
    • Rapid isolation of genomic DNA from Gram-negative bacteria
    • Neumann, B., Pospiech, A., and Schairer, H.U. (1992) Rapid isolation of genomic DNA from Gram-negative bacteria. Trends Genet 8: 332-333.
    • (1992) Trends Genet , vol.8 , pp. 332-333
    • Neumann, B.1    Pospiech, A.2    Schairer, H.U.3
  • 51
    • 8144229871 scopus 로고    scopus 로고
    • Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP
    • Nolen, B.J., Littlefield, R.S., and Pollard, T.D. (2004) Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proc Natl Acad Sci USA 101: 15627-15632.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15627-15632
    • Nolen, B.J.1    Littlefield, R.S.2    Pollard, T.D.3
  • 53
    • 36549033450 scopus 로고    scopus 로고
    • Cell shape determination in Escherichia coli
    • Osborn, M.J., and Rothfield, L. (2007) Cell shape determination in Escherichia coli. Curr Opin Microbiol 10: 606-610.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 606-610
    • Osborn, M.J.1    Rothfield, L.2
  • 54
    • 0002014756 scopus 로고    scopus 로고
    • Site-directed mutagenesis in one day with >80% efficiency
    • Papworth, C., Bauer, J. C., Braman, J., and Wright, D.A. (1996) Site-directed mutagenesis in one day with >80% efficiency. Strategies 8: 3-4.
    • (1996) Strategies , vol.8 , pp. 3-4
    • Papworth, C.1    Bauer, J.C.2    Braman, J.3    Wright, D.A.4
  • 55
    • 15744385269 scopus 로고    scopus 로고
    • Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA
    • DOI 10.1111/j.1365-2958.2005.04522.x
    • Pichoff, S., and Lutkenhaus, J. (2005) Tethering the Z ring to the membrane through a conserved membrane targeting sequence in FtsA. Mol Microbiol 55: 1722-1734. (Pubitemid 40445209)
    • (2005) Molecular Microbiology , vol.55 , Issue.6 , pp. 1722-1734
    • Pichoff, S.1    Lutkenhaus, J.2
  • 56
    • 39149141843 scopus 로고    scopus 로고
    • The bacterial cytoskeleton
    • Pogliano, J. (2008) The bacterial cytoskeleton. Curr Opin Cell Biol 20: 19-27.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 19-27
    • Pogliano, J.1
  • 57
    • 0033000497 scopus 로고    scopus 로고
    • A vital stain for studying membrane dynamics in bacteria: A novel mechanism controlling septation during Bacillus subtilis sporulation
    • DOI 10.1046/j.1365-2958.1999.01255.x
    • Pogliano, J., Osborne, N., Sharp, M.D., Abanes-DeMello, A., Perez, A., Sun, Y.-L., and Pogliano, K. (1999) A vital stain for studying membrane dynamics in bacteria: a novel mechanism controlling septation during Bacillus subtilis sporulation. Mol Microbiol 31: 1149-1159. (Pubitemid 29082244)
    • (1999) Molecular Microbiology , vol.31 , Issue.4 , pp. 1149-1159
    • Pogliano, J.1    Osborne, N.2    Sharp, M.D.3    Mello, A.A.-D.4    Perez, A.5    Sun, Y.-L.6    Pogliano, K.7
  • 58
    • 45249117275 scopus 로고    scopus 로고
    • Progress towards understanding the mechanism of cytokinesis in fission yeast
    • Pollard, T.D. (2008) Progress towards understanding the mechanism of cytokinesis in fission yeast. Biochem Soc Trans 36: 425-430.
    • (2008) Biochem Soc Trans , vol.36 , pp. 425-430
    • Pollard, T.D.1
  • 59
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D., and Borisy, G.G. (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112: 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 60
    • 38949129203 scopus 로고    scopus 로고
    • Molecular structure of the ParM polymer and the mechanism leading to its nucleotide-driven dynamic instability
    • DOI 10.1038/sj.emboj.7601978, PII 7601978
    • Popp, D., Narita, A., Odo, T., Fujisawa, T., Matsuo, H., Nitanai, Y., et al. (2008) Molecular structure of the ParM polymer and the mechanism leading to its nucleotidedriven dynamic instability. EMBO J 27: 570-579. (Pubitemid 351225678)
    • (2008) EMBO Journal , vol.27 , Issue.3 , pp. 570-579
    • Popp, D.1    Narita, A.2    Oda, T.3    Fujisawa, T.4    Matsuo, H.5    Nitanai, Y.6    Iwasa, M.7    Maeda, K.8    Onishi, H.9    Maeda, Y.10
  • 61
    • 0033231557 scopus 로고    scopus 로고
    • Control of development by altered localization of a transcription factor in B. subtilis
    • Quisel, J.D., Lin. D.C-H., and Grossman, A.D. (1999) Control of development by altered localization of a transcription factor in B. subtilis. Mol Cell 4: 665-672.
    • (1999) Mol Cell , vol.4 , pp. 665-672
    • Quisel, J.D.1    Lin, D.C.-H.2    Grossman, A.D.3
  • 63
    • 0025892985 scopus 로고
    • Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon
    • Rygus, T., and Hillen, W. (1991) Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon. Appl Microbiol Biotechnol 35: 594-599.
    • (1991) Appl Microbiol Biotechnol , vol.35 , pp. 594-599
    • Rygus, T.1    Hillen, W.2
  • 64
    • 58849121358 scopus 로고    scopus 로고
    • Electron cryomicroscopy of E. coli reveals filament bundles involved in plasmid DNA segregation
    • Salje, J., Zuber, B., and Löwe, J. (2009) Electron cryomicroscopy of E. coli reveals filament bundles involved in plasmid DNA segregation. Science 323: 509-512.
    • (2009) Science , vol.323 , pp. 509-512
    • Salje, J.1    Zuber, B.2    Löwe, J.3
  • 65
    • 44849083494 scopus 로고    scopus 로고
    • Genetics and cell biology of magnetosome formation in magnetotactic bacteria
    • Schüler, D. (2008) Genetics and cell biology of magnetosome formation in magnetotactic bacteria. FEMS Microbiol Rev 32: 654-672.
    • (2008) FEMS Microbiol Rev , vol.32 , pp. 654-672
    • Schüler, D.1
  • 66
    • 0037016404 scopus 로고    scopus 로고
    • Role of cell-specific SpoIIIE assembly in polarity of DNA transfer
    • DOI 10.1126/science.1066274
    • Sharp. M.D., and Pogliano, K. (2002) Role of cell-specific SpolllE assembly in polarity of DNA transfer. Science 295: 137-139. (Pubitemid 34052364)
    • (2002) Science , vol.295 , Issue.5552 , pp. 137-139
    • Sharp, M.D.1    Pogliano, K.2
  • 67
    • 0037699937 scopus 로고    scopus 로고
    • Division site selection in Escherichia coll involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
    • Shih, Y.-L, Le, T., and Rothfield, L. (2003) Division site selection in Escherichia coll involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles. Proc Natl Acad Sci USA 100:7865-7870.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7865-7870
    • Shih, Y.-L.1    Le, T.2    Rothfield, L.3
  • 68
    • 36549087126 scopus 로고    scopus 로고
    • Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring
    • DOI 10.1111/j.1365-2958.2007.05998.x
    • Shiomi, D., and Margolin, W. (2007) Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring. Mol Microbiol 66: 1396-1415. (Pubitemid 350179675)
    • (2007) Molecular Microbiology , vol.66 , Issue.6 , pp. 1396-1415
    • Shiomi, D.1    Margolin, W.2
  • 69
    • 4444285310 scopus 로고    scopus 로고
    • Dynamic movement of actin-like proteins within bacterial cells
    • Soufo, H.J.D., and Graumann, P.L. (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
  • 70
    • 0017521147 scopus 로고
    • Isolation and characterization of four types of plasmids from Bacillus subtilis (natto)
    • Tanaka, T., and Koshikawa, T. (1977) Isolation and characterization of four types of plasmids from Bacillus subtilis (natto). J Bacteriol 131: 699-701.
    • (1977) J Bacteriol , vol.131 , pp. 699-701
    • Tanaka, T.1    Koshikawa, T.2
  • 71
    • 35548995474 scopus 로고    scopus 로고
    • Complete genomic sequence and mass spectrometric analysis of highly diverse, atypical Bacillus thuringiensis phage 0305φ{symbol}8-36
    • DOI 10.1016/j.virol.2007.06.043, PII S0042682207004643
    • Thomas, J.A., Hardies, S.C., Rolando, M., Hayes, S. J., Lieman, K., Carroll, C.A., et al. (2007) Complete genomic sequence and mass spectrometric analysis of highly diverse, atypical Bacillus thuringiensis phage 0305Φ8-36. Virology 368: 405-421. (Pubitemid 350017836)
    • (2007) Virology , vol.368 , Issue.2 , pp. 405-421
    • Thomas, J.A.1    Hardies, S.C.2    Rolando, M.3    Hayes, S.J.4    Lieman, K.5    Carroll, C.A.6    Weintraub, S.T.7    Serwer, P.8
  • 72
    • 0021099326 scopus 로고
    • The kinetics of actin nucleation and polymerization
    • Tobacman, L.S., and Korn, E.D. (1983) The kinetics of actin nucleation and polymerization. J Biol Chem 258: 3207-3214.
    • (1983) J Biol Chem , vol.258 , pp. 3207-3214
    • Tobacman, L.S.1    Korn, E.D.2
  • 73
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange™ site-directed mutagenesis
    • Wang, W., and Malcolm, B.A. (1999) Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuikChange™ site-directed mutagenesis. Biotechniques 26: 680-682. (Pubitemid 129526133)
    • (1999) BioTechniques , vol.26 , Issue.4 , pp. 680-682
    • Wang, W.1    Malcolm, B.A.2
  • 74
    • 34548279011 scopus 로고    scopus 로고
    • Regulation of otic vesicle and hair cell stereocilia morphogenesis by Ena/ VASP-like (EvI) in Xenopus
    • Wanner, SJ., and Miller, J.R. (2007) Regulation of otic vesicle and hair cell stereocilia morphogenesis by Ena/ VASP-like (EvI) in Xenopus. J Cell Sci 120: 2641-2651.
    • (2007) J Cell Sci , vol.120 , pp. 2641-2651
    • Wanner, S.J.1    Miller, J.R.2
  • 75
    • 0032932435 scopus 로고    scopus 로고
    • Localization of FtsI (PBP3) to the septal ring requires its membrane anchor, the Z ring, FtsA, FtsQ, and FtsL
    • Weiss, D.S., Chen, J.C., Ghigo, J.-M., Boyd, D., and Beckwith, J. (1999) Localization of Ftsl (PBP3) to the septal ring requires its membrane anchor, the Z Ring, FtsA, FtsQ, and FtsL. J Bacteriol 181: 508-520. (Pubitemid 29045142)
    • (1999) Journal of Bacteriology , vol.181 , Issue.2 , pp. 508-520
    • Weiss, D.S.1    Chen, J.C.2    Ghigo, J.-M.3    Boyd, D.4    Beckwith, J.5
  • 76
    • 0021204113 scopus 로고
    • Construction of a cloning site near one end of Tn917 into which foreign DNA may be inserted without affecting transposition in Bacillus subtilis or expression of the transposon-borne erm gene
    • Youngman, P., Perkins, J.B., and Losick, R. (1984) Construction of a cloning site near one end of Tn917 into which foreign DNA may be inserted without affecting transposition in Baciillus subtilis or expression of the transposonborne erm gene. Plasmid M: 1-9. (Pubitemid 14046086)
    • (1984) Plasmid , vol.12 , Issue.1 , pp. 1-9
    • Youngman, P.1    Perkins, J.B.2    Losick, R.3


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