메뉴 건너뛰기




Volumn 11, Issue 3-5, 2006, Pages 265-283

The cytoskeleton of spiroplasma: A complex linear motor

Author keywords

Bacterial motility; cryo BM; Cytoskeleton; Linear motor; Mollicutes; Spiroplasma; STEM

Indexed keywords

ACTIN; CYTOSKELETON PROTEIN; ELONGATION FACTOR TU; FTSZ PROTEIN; MREB PROTEIN;

EID: 33748774677     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: 10.1159/000094060     Document Type: Review
Times cited : (21)

References (87)
  • 1
    • 33748770937 scopus 로고    scopus 로고
    • Mycoplasmas: A distinct cytoskeleton for wall-less bacteria
    • Balish MF, Krause DC: Mycoplasmas: a distinct cytoskeleton for wall-less bacteria. J Mol Microbiol Biotechnol 2006;11:244-255.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 244-255
    • Balish, M.F.1    Krause, D.C.2
  • 2
    • 0141564606 scopus 로고    scopus 로고
    • On self-propulsion of micro-machines at low Reynolds number: Purcell's three link swimmer
    • Becker LE, Koehler SA, Stone HA: On self-propulsion of micro-machines at low Reynolds number: Purcell's three link swimmer. J Fluid Mech 2003;490:15-35.
    • (2003) J Fluid Mech , vol.490 , pp. 15-35
    • Becker, L.E.1    Koehler, S.A.2    Stone, H.A.3
  • 3
    • 0036201903 scopus 로고    scopus 로고
    • How Spiroplasma might swim
    • Berg HC: How Spiroplasma might swim. J Bacteriol 2002;184:2063-2064.
    • (2002) J Bacteriol , vol.184 , pp. 2063-2064
    • Berg, H.C.1
  • 4
    • 0031060732 scopus 로고    scopus 로고
    • Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes
    • Bevén L, Wróblewski H: Effect of natural amphipathic peptides on viability, membrane potential, cell shape and motility of mollicutes. Res Microbiol 1997;148:163-175.
    • (1997) Res Microbiol , vol.148 , pp. 163-175
    • Bevén, L.1    Wróblewski, H.2
  • 5
    • 0029859561 scopus 로고    scopus 로고
    • Inhibition of spiralin processing by the lipopeptide antibiotic globomycin
    • Bevén L, Le Henaff M, Fontenelle C, Wróblewski H: Inhibition of spiralin processing by the lipopeptide antibiotic globomycin. Curr Microbiol 1996;33:317-322.
    • (1996) Curr Microbiol , vol.33 , pp. 317-322
    • Bevén, L.1    Le Henaff, M.2    Fontenelle, C.3    Wróblewski, H.4
  • 9
    • 0030748743 scopus 로고    scopus 로고
    • Spiroplasmas: Infectious agents of plants, arthropods and vertebrates
    • Bové JM: Spiroplasmas: infectious agents of plants, arthropods and vertebrates. Wien Klin Wochenschr 1997;109:604-612.
    • (1997) Wien Klin Wochenschr , vol.109 , pp. 604-612
    • Bové, J.M.1
  • 11
    • 0141701190 scopus 로고    scopus 로고
    • Spiroplasma citri, a plant pathogenic molligute: Relationships with its two hosts, the plant and the leafhopper vector
    • Bové JM, Renaudin J, Saillard C, Foissac X, Garnier M: Spiroplasma citri, a plant pathogenic molligute: relationships with its two hosts, the plant and the leafhopper vector. Annu Rev Phytopathol 2003;41:483-500.
    • (2003) Annu Rev Phytopathol , vol.41 , pp. 483-500
    • Bové, J.M.1    Renaudin, J.2    Saillard, C.3    Foissac, X.4    Garnier, M.5
  • 12
    • 0031022569 scopus 로고    scopus 로고
    • The 57-kilodalton phosphoprotein of Spiroplasma melliferum is autophosphorylated
    • Borovsky Z, Aner R, Rottem S: The 57-kilodalton phosphoprotein of Spiroplasma melliferum is autophosphorylated. Curr Microbiol 1997;34:33-37.
    • (1997) Curr Microbiol , vol.34 , pp. 33-37
    • Borovsky, Z.1    Aner, R.2    Rottem, S.3
  • 14
    • 0029017836 scopus 로고
    • Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic α-helix
    • Brenner C, Duclohier H, Krchnak V, Wróblewski H: Conformation, pore-forming activity, and antigenicity of synthetic peptide analogues of a spiralin putative amphipathic α-helix. Biochim Biophys Acta 1995;1235:161-168.
    • (1995) Biochim Biophys Acta , vol.1235 , pp. 161-168
    • Brenner, C.1    Duclohier, H.2    Krchnak, V.3    Wróblewski, H.4
  • 16
    • 45849155789 scopus 로고    scopus 로고
    • Periodic chirality transformations propagating on bacterial flagella
    • Coombs D, Huber G, Kessler J, Goldstein R: Periodic chirality transformations propagating on bacterial flagella. Phys Rev Lett 2002;89:118101-118104.
    • (2002) Phys Rev Lett , vol.89 , pp. 118101-118104
    • Coombs, D.1    Huber, G.2    Kessler, J.3    Goldstein, R.4
  • 17
    • 0021244468 scopus 로고
    • Chemotactic behavior of Spiroplasma
    • Daniels MJ, Longland JM: Chemotactic behavior of Spiroplasma. Curr Biol 1984;10:191-194.
    • (1984) Curr Biol , vol.10 , pp. 191-194
    • Daniels, M.J.1    Longland, J.M.2
  • 18
  • 19
    • 0001728310 scopus 로고
    • Spiroplasma: Motile, helical microorganisms associated with corn stunt disease
    • Davis RE, Worley JF: Spiroplasma: motile, helical microorganisms associated with corn stunt disease. Phytopatholgy 1973;63:403-408.
    • (1973) Phytopatholgy , vol.63 , pp. 403-408
    • Davis, R.E.1    Worley, J.F.2
  • 20
    • 0000957468 scopus 로고
    • Helical filaments produced by a mycoplasma-like organism associated with corn stunt disease
    • Davis RE, Worley JF, Whitcomb RF, Ishijima T, Steere RL: Helical filaments produced by a mycoplasma-like organism associated with corn stunt disease. Science 1972;176:521-523.
    • (1972) Science , vol.176 , pp. 521-523
    • Davis, R.E.1    Worley, J.F.2    Whitcomb, R.F.3    Ishijima, T.4    Steere, R.L.5
  • 21
    • 0028109456 scopus 로고
    • Phosphorylation of cytadherence-accessory proteins in Mycoplasma pneumoniae
    • Dirksen LB, Krebes KA, Krause DC: Phosphorylation of cytadherence- accessory proteins in Mycoplasma pneumoniae. J Bacteriol 1994;176:7499-7505.
    • (1994) J Bacteriol , vol.176 , pp. 7499-7505
    • Dirksen, L.B.1    Krebes, K.A.2    Krause, D.C.3
  • 22
    • 0142104346 scopus 로고    scopus 로고
    • Spiralin is not essential for helicity, motility, or pathogenicity but is required for efficient transmission of Spiroplasma citri by its leafhopper vector Circulifer haematoceps
    • Duret S, Berho N, Danet JL, Garnier M, Renaudin J: Spiralin is not essential for helicity, motility, or pathogenicity but is required for efficient transmission of Spiroplasma citri by its leafhopper vector Circulifer haematoceps. Appl Environ Microbiol 2003;69:6225-6234.
    • (2003) Appl Environ Microbiol , vol.69 , pp. 6225-6234
    • Duret, S.1    Berho, N.2    Danet, J.L.3    Garnier, M.4    Renaudin, J.5
  • 23
    • 0035817902 scopus 로고    scopus 로고
    • Cytoskeleton. Evolution in bacteria
    • Erickson HP: Cytoskeleton. Evolution in bacteria. Nature 2001;413:30.
    • (2001) Nature , vol.413 , pp. 30
    • Erickson, H.P.1
  • 24
    • 0030006192 scopus 로고    scopus 로고
    • Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation
    • Foissac X, Saillard C, Gandar J, Zreik L, Bové JM: Spiralin polymorphism in strains of Spiroplasma citri is not due to differences in posttranslational palmitoylation. J Bacteriol 1996;178:2934-2940.
    • (1996) J Bacteriol , vol.178 , pp. 2934-2940
    • Foissac, X.1    Saillard, C.2    Gandar, J.3    Zreik, L.4    Bové, J.M.5
  • 25
    • 0036511630 scopus 로고    scopus 로고
    • Spiroplasmas: Evolution, adaptation and diversity
    • Gasparich GE: Spiroplasmas: evolution, adaptation and diversity. Front Biosci 2002;7:d619-d640.
    • (2002) Front Biosci , vol.7
    • Gasparich, G.E.1
  • 26
    • 2942630791 scopus 로고    scopus 로고
    • The genus Spiroplasma and its non-helical descendants: Phylogenetic classification, correlation with phenotype and roots of the Mycoplasma mycoides clade
    • Gasparich GE, Whitcomb RF, Dodge D, French FE, Glass J, Williamson DL: The genus Spiroplasma and its non-helical descendants: phylogenetic classification, correlation with phenotype and roots of the Mycoplasma mycoides clade. Int J Syst Evol Microbiol 2004;54:893-918.
    • (2004) Int J Syst Evol Microbiol , vol.54 , pp. 893-918
    • Gasparich, G.E.1    Whitcomb, R.F.2    Dodge, D.3    French, F.E.4    Glass, J.5    Williamson, D.L.6
  • 27
    • 0017838727 scopus 로고
    • Inhibition of mycoplasma cell division by cytochalasin B
    • Ghosh A, Maniloff J, Gerling DA: Inhibition of mycoplasma cell division by cytochalasin B. Cell 1978;13:57-64.
    • (1978) Cell , vol.13 , pp. 57-64
    • Ghosh, A.1    Maniloff, J.2    Gerling, D.A.3
  • 28
    • 0037240714 scopus 로고    scopus 로고
    • Motility modes of Spiroplasma melliferum BC3: A helical, wall-less bacterium driven by a linear motor
    • Gilad R, Porat A, Trachtenberg S: Motility modes of Spiroplasma melliferum BC3: a helical, wall-less bacterium driven by a linear motor. Mol Microbiol 2003;47:657-669.
    • (2003) Mol Microbiol , vol.47 , pp. 657-669
    • Gilad, R.1    Porat, A.2    Trachtenberg, S.3
  • 30
    • 14844304655 scopus 로고    scopus 로고
    • The new bacterial cell biology: Moving parts and subcellular architecture
    • Gitai Z: The new bacterial cell biology: moving parts and subcellular architecture. Cell 2005;120:577-586.
    • (2005) Cell , vol.120 , pp. 577-586
    • Gitai, Z.1
  • 31
    • 0020953929 scopus 로고
    • Supramolecular structures in mycoplasmas
    • Göbel U: Supramolecular structures in mycoplasmas. Yale J Biol Med 1983;56:695-700.
    • (1983) Yale J Biol Med , vol.56 , pp. 695-700
    • Göbel, U.1
  • 32
    • 0019816823 scopus 로고
    • Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents
    • Göbel U, Speth V, Bredt W: Filamentous structures in adherent Mycoplasma pneumoniae cells treated with nonionic detergents. J Cell Biol 1981;91:537-543.
    • (1981) J Cell Biol , vol.91 , pp. 537-543
    • Göbel, U.1    Speth, V.2    Bredt, W.3
  • 34
    • 0036809920 scopus 로고    scopus 로고
    • Cytoskeletal elements in the bacterium Mycoplasma pneumoniae
    • Hegermann J, Herrmann R, Mayer F: Cytoskeletal elements in the bacterium Mycoplasma pneumoniae. Naturwissenschaften 2002;89:453-458.
    • (2002) Naturwissenschaften , vol.89 , pp. 453-458
    • Hegermann, J.1    Herrmann, R.2    Mayer, F.3
  • 35
    • 3042515670 scopus 로고    scopus 로고
    • Energetics of gliding motility in Mycoplasma mobile
    • Jaffe JD, Miyata M, Berg HC: Energetics of gliding motility in Mycoplasma mobile. J Bacteriol 2004;186:4254-4261.
    • (2004) J Bacteriol , vol.186 , pp. 4254-4261
    • Jaffe, J.D.1    Miyata, M.2    Berg, H.C.3
  • 36
    • 1842301665 scopus 로고    scopus 로고
    • Isolation, characterization, and complementation of a motility mutant of Spiroplasma citri
    • Jacob C, Nouzieres F, Duret S, Bové JM, Renaudin J: Isolation, characterization, and complementation of a motility mutant of Spiroplasma citri. J Bacteriol 1997;179:4802-4810.
    • (1997) J Bacteriol , vol.179 , pp. 4802-4810
    • Jacob, C.1    Nouzieres, F.2    Duret, S.3    Bové, J.M.4    Renaudin, J.5
  • 37
    • 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: Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 2001;104:913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.1    Carballido-Lopez, R.2    Errington, J.3
  • 38
    • 0029937832 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae cytadherence: Unravelling the tie that binds
    • Krause DC: Mycoplasma pneumoniae cytadherence: unravelling the tie that binds. Mol Microbiol 1996;20:247-253.
    • (1996) Mol Microbiol , vol.20 , pp. 247-253
    • Krause, D.C.1
  • 39
    • 0031914772 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae cytadherence: Organization and assembly of the attachment organelle
    • Krause DC: Mycoplasma pneumoniae cytadherence: organization and assembly of the attachment organelle. Trends Microbiol 1998;6:15-18.
    • (1998) Trends Microbiol , vol.6 , pp. 15-18
    • Krause, D.C.1
  • 40
    • 0029127556 scopus 로고
    • Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extracts
    • Krebes KA, Dirksen LB, Krause DC: Phosphorylation of Mycoplasma pneumoniae cytadherence-accessory proteins in cell extracts. J Bacteriol 1995;177:4571-4574.
    • (1995) J Bacteriol , vol.177 , pp. 4571-4574
    • Krebes, K.A.1    Dirksen, L.B.2    Krause, D.C.3
  • 41
    • 12344274281 scopus 로고    scopus 로고
    • Cryoelectron tomography reveals the cytoskeletal structure of Spiroplasma melliferum
    • Kurner J, Frangakis AS, Baumeister W: Cryoelectron tomography reveals the cytoskeletal structure of Spiroplasma melliferum. Science 2005;307:436-438.
    • (2005) Science , vol.307 , pp. 436-438
    • Kurner, J.1    Frangakis, A.S.2    Baumeister, W.3
  • 44
    • 12744271503 scopus 로고    scopus 로고
    • Cortactin phosphorylation as a switch for actin cytoskeletal network and cell dynamics control
    • Lua BL, Low BC: Cortactin phosphorylation as a switch for actin cytoskeletal network and cell dynamics control. FEBS Lett 2005;579:577-585.
    • (2005) FEBS Lett , vol.579 , pp. 577-585
    • Lua, B.L.1    Low, B.C.2
  • 45
    • 0018253480 scopus 로고
    • Heavy meromyosin decoration of filaments from Escherichia coli
    • Mallot DW, McCurdy HD: Heavy meromyosin decoration of filaments from Escherichia coli. Curr Microbiol 1978;1:201-202.
    • (1978) Curr Microbiol , vol.1 , pp. 201-202
    • Mallot, D.W.1    McCurdy, H.D.2
  • 46
    • 0018561187 scopus 로고
    • Gliding mycoplasmas are inhibited by cytochalasin B and contain a polymerizable protein fraction
    • Maniloff J, Chaudhuri U: Gliding mycoplasmas are inhibited by cytochalasin B and contain a polymerizable protein fraction. J Supramol Struct 1979;12:299-304.
    • (1979) J Supramol Struct , vol.12 , pp. 299-304
    • Maniloff, J.1    Chaudhuri, U.2
  • 47
    • 0003845479 scopus 로고
    • Maniloff J, McElhaney RN, Finch LR, Baseman JB (eds): Washington, American Society for Microbiology
    • Maniloff J, McElhaney RN, Finch LR, Baseman JB (eds): Mycoplasmas: Molecular Biology and Pathogeneis. Washington, American Society for Microbiology, 1992.
    • (1992) Mycoplasmas: Molecular Biology and Pathogeneis
  • 48
    • 27644540151 scopus 로고    scopus 로고
    • FtsZ and the division of prokaryotic cells and organelles
    • Margolin W: FtsZ and the division of prokaryotic cells and organelles. Nat Rev Mol Cell Biol 2005;6:862-871.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 862-871
    • Margolin, W.1
  • 49
    • 0037551711 scopus 로고    scopus 로고
    • Cytoskeletons in prokaryotes
    • Mayer F: Cytoskeletons in prokaryotes. Cell Biol Int 2003;27:429-438.
    • (2003) Cell Biol Int , vol.27 , pp. 429-438
    • Mayer, F.1
  • 50
    • 33748804180 scopus 로고    scopus 로고
    • Cytoskeletal elements in bacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli as revealed by electron microscopy
    • Mayer F: Cytoskeletal elements in bacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli as revealed by electron microscopy. J Mol Microbiol Biotechnol 2006;11:228-243.
    • (2006) J Mol Microbiol Biotechnol , vol.11 , pp. 228-243
    • Mayer, F.1
  • 51
    • 2642539035 scopus 로고    scopus 로고
    • The bacterial cytoskeleton and its putative role in membrane vesicle formation observed in a Gram-positive bacterium producing starch-degrading enzymes
    • Mayer F, Gottschalk G: The bacterial cytoskeleton and its putative role in membrane vesicle formation observed in a Gram-positive bacterium producing starch-degrading enzymes. J Mol Microbiol Biotechnol 2003;6:127-132.
    • (2003) J Mol Microbiol Biotechnol , vol.6 , pp. 127-132
    • Mayer, F.1    Gottschalk, G.2
  • 52
    • 0019205331 scopus 로고
    • Intracellular structures of Mycoplasma pneumoniae revealed after membrane removal
    • Meng KE, Pfister RM: Intracellular structures of Mycoplasma pneumoniae revealed after membrane removal. J Bacteriol 1980;144:390-399.
    • (1980) J Bacteriol , vol.144 , pp. 390-399
    • Meng, K.E.1    Pfister, R.M.2
  • 54
  • 55
    • 0017759026 scopus 로고
    • Extraction of an actin-like protein from the prokaryote Mycoplasma pneumoniae
    • Neimark HC: Extraction of an actin-like protein from the prokaryote Mycoplasma pneumoniae. Proc Natl Acad Sci USA 1977;74:4041-4045.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 4041-4045
    • Neimark, H.C.1
  • 56
    • 0020930960 scopus 로고
    • Mycoplasma and bacterial proteins resembling contractile proteins: A review
    • Neimark H: Mycoplasma and bacterial proteins resembling contractile proteins: a review. Yale J Biol Med 1983;56:419-423.
    • (1983) Yale J Biol Med , vol.56 , pp. 419-423
    • Neimark, H.1
  • 57
    • 0024268970 scopus 로고
    • Phosvitin kinase activity in Acholeplasma axanthum
    • Platt MW, Rottem S: Phosvitin kinase activity in Acholeplasma axanthum. FEBS Lett 1988;242:97-100.
    • (1988) FEBS Lett , vol.242 , pp. 97-100
    • Platt, M.W.1    Rottem, S.2
  • 59
    • 0025332517 scopus 로고
    • A 57-kilodalton protein associated with Spiroplasma melliferum fibrils undergoes reversible phosphorylation
    • Platt MW, Reizer J, Rottem S: A 57-kilodalton protein associated with Spiroplasma melliferum fibrils undergoes reversible phosphorylation. J Bacteriol 1990;172:2808-2811.
    • (1990) J Bacteriol , vol.172 , pp. 2808-2811
    • Platt, M.W.1    Reizer, J.2    Rottem, S.3
  • 60
    • 84890506631 scopus 로고
    • Life at low Reynolds number
    • Purcell EM: Life at low Reynolds number. Am J Phys 1977;45:3-11.
    • (1977) Am J Phys , vol.45 , pp. 3-11
    • Purcell, E.M.1
  • 61
    • 0030881690 scopus 로고    scopus 로고
    • The efficiency of propulsion by a rotating flagellum
    • Purcell EM: The efficiency of propulsion by a rotating flagellum. Proc Natl Acad Sci USA 1997;94:11307-11311.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11307-11311
    • Purcell, E.M.1
  • 63
    • 0035050279 scopus 로고    scopus 로고
    • Defining the mycoplasma 'cytoskeleton': The protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry
    • Regula JT, Boguth G, Gorg A, Hegermann J, Mayer F, Frank R, Herrmann R: Defining the mycoplasma 'cytoskeleton': the protein composition of the Triton X-100 insoluble fraction of the bacterium Mycoplasma pneumoniae determined by 2-D gel electrophoresis and mass spectrometry. Microbiology 2001;147:1045-1057.
    • (2001) Microbiology , vol.147 , pp. 1045-1057
    • Regula, J.T.1    Boguth, G.2    Gorg, A.3    Hegermann, J.4    Mayer, F.5    Frank, R.6    Herrmann, R.7
  • 65
    • 0017056554 scopus 로고
    • Does a bacterial elongation factor share a common evolutionary ancestor with actin
    • Rosenbusch JP, Jacobson GR, Jaton JC: Does a bacterial elongation factor share a common evolutionary ancestor with actin. J Supramol Struct 1976;5:391-396.
    • (1976) J Supramol Struct , vol.5 , pp. 391-396
    • Rosenbusch, J.P.1    Jacobson, G.R.2    Jaton, J.C.3
  • 66
    • 25144479327 scopus 로고    scopus 로고
    • Spiroplasma swim by a processive change in body helicity
    • Shaevitz JW, Lee JY, Fletcher DA: Spiroplasma swim by a processive change in body helicity. Cell 2005;122:941-945.
    • (2005) Cell , vol.122 , pp. 941-945
    • Shaevitz, J.W.1    Lee, J.Y.2    Fletcher, D.A.3
  • 67
    • 0242504515 scopus 로고
    • Immunochemical identification of actin-like protein from Spiroplasma citri
    • Simoneau P, Labarère J: Immunochemical identification of actin-like protein from Spiroplasma citri. Zentralbl Bakteriol 1990;20(suppl):927-931.
    • (1990) Zentralbl Bakteriol , vol.20 , Issue.SUPPL. , pp. 927-931
    • Simoneau, P.1    Labarère, J.2
  • 68
    • 0017379983 scopus 로고
    • Isolation and characterization of a nonhelical strain of Spiroplasma citri
    • Townsend R, Markham PG, Plaskitt KA, Daniels MJ: Isolation and characterization of a nonhelical strain of Spiroplasma citri. J Gen Microbiol 1977;100:15-21.
    • (1977) J Gen Microbiol , vol.100 , pp. 15-21
    • Townsend, R.1    Markham, P.G.2    Plaskitt, K.A.3    Daniels, M.J.4
  • 69
    • 0018934235 scopus 로고
    • Purification and preliminary characterization of Spiroplasma fibrils
    • Townsend R, Archer DB, Plaskitt KA: Purification and preliminary characterization of Spiroplasma fibrils. J Bacteriol 1980a;142:694-700.
    • (1980) J Bacteriol , vol.142 , pp. 694-700
    • Townsend, R.1    Archer, D.B.2    Plaskitt, K.A.3
  • 70
    • 0019205167 scopus 로고
    • Morphology and ultrastructure of helical and nonhelical strains of Spiroplasma citri
    • Townsend R, Burgess J, Plaskitt KA: Morphology and ultrastructure of helical and nonhelical strains of Spiroplasma citri. J Bacteriol 1980b;142:973-981.
    • (1980) J Bacteriol , vol.142 , pp. 973-981
    • Townsend, R.1    Burgess, J.2    Plaskitt, K.A.3
  • 71
    • 0032455875 scopus 로고    scopus 로고
    • Mollicutes-wall-less bacteria with internal cytoskeletons
    • Trachtenberg S: Mollicutes-wall-less bacteria with internal cytoskeletons. J Struct Biol 1998;124:244-256.
    • (1998) J Struct Biol , vol.124 , pp. 244-256
    • Trachtenberg, S.1
  • 74
    • 33748786732 scopus 로고    scopus 로고
    • Spiroplasma motility and chemotaxis: Molecular aspects of cell behaviour
    • Blanchard A, Browning G (eds): Norfolk, Horizon Bioscience
    • Trachtenberg S: Spiroplasma motility and chemotaxis: molecular aspects of cell behaviour; in Blanchard A, Browning G (eds): Mycoplasmas: Pathogenesis, Molecular Biology, and Emerging Strategies for Control. Norfolk, Horizon Bioscience, 2005b, pp 165-188.
    • (2005) Mycoplasmas: Pathogenesis, Molecular Biology, and Emerging Strategies for Control , pp. 165-188
    • Trachtenberg, S.1
  • 75
    • 0035724921 scopus 로고    scopus 로고
    • A bacterial linear motor: Cellular and molecular organization of the contractile cytoskeleton of the helical bacterium Spiroplasma melliferum BC3
    • Trachtenberg S, Gilad R: A bacterial linear motor: cellular and molecular organization of the contractile cytoskeleton of the helical bacterium Spiroplasma melliferum BC3. Mol Microbiol 2001;41:827-848.
    • (2001) Mol Microbiol , vol.41 , pp. 827-848
    • Trachtenberg, S.1    Gilad, R.2
  • 76
    • 0037334898 scopus 로고    scopus 로고
    • Mass distribution and spatial organization of the linear bacterial motor of Spiroplasma citri R8A2
    • Trachtenberg S, Andrews SB, Leapman RD: Mass distribution and spatial organization of the linear bacterial motor of Spiroplasma citri R8A2. J Bacteriol 2003a;185:1987-1994.
    • (2003) J Bacteriol , vol.185 , pp. 1987-1994
    • Trachtenberg, S.1    Andrews, S.B.2    Leapman, R.D.3
  • 77
    • 0037241863 scopus 로고    scopus 로고
    • The bacterial linear motor of Spiroplasma melliferum BC3: From single molecules to swimming cells
    • Trachtenberg S, Gilad R, Geffen N: The bacterial linear motor of Spiroplasma melliferum BC3: from single molecules to swimming cells. Mol Microbiol 2003b;47:671-697.
    • (2003) Mol Microbiol , vol.47 , pp. 671-697
    • Trachtenberg, S.1    Gilad, R.2    Geffen, N.3
  • 78
    • 24644452446 scopus 로고    scopus 로고
    • Gliding ghosts of Mycoplasma mobile
    • Uenoyama A, Miyata M: Gliding ghosts of Mycoplasma mobile. Proc Natl Acad Sci USA 2005;102:12754-12758.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12754-12758
    • Uenoyama, A.1    Miyata, M.2
  • 80
    • 0029919949 scopus 로고    scopus 로고
    • Characterization of the ftsZ gene from Mycoplasma pulmonis, an organism lacking a cell wall
    • Wang X, Lutkenhaus J: Characterization of the ftsZ gene from Mycoplasma pulmonis, an organism lacking a cell wall. J Bacteriol 1996;178:2314-2319.
    • (1996) J Bacteriol , vol.178 , pp. 2314-2319
    • Wang, X.1    Lutkenhaus, J.2
  • 82
    • 0018610766 scopus 로고
    • Antiactin peroxidase staining of the helical wall-free prokaryote Spiroplasma citri
    • Williamson DL, Blanstein DI, Levine RJC, Elfvin MJ: Antiactin peroxidase staining of the helical wall-free prokaryote Spiroplasma citri. Curr Biol 1979;2:143-145.
    • (1979) Curr Biol , vol.2 , pp. 143-145
    • Williamson, D.L.1    Blanstein, D.I.2    Levine, R.J.C.3    Elfvin, M.J.4
  • 83
    • 0025733735 scopus 로고
    • Nucleotide sequence of the Spiroplasma citri fibril protein gene
    • Williamson DL, Renaudin J, Bové JM: Nucleotide sequence of the Spiroplasma citri fibril protein gene. J Bacteriol 1991;173:4353-4362.
    • (1991) J Bacteriol , vol.173 , pp. 4353-4362
    • Williamson, D.L.1    Renaudin, J.2    Bové, J.M.3
  • 84
    • 0017287807 scopus 로고
    • Ultrastructural study of Mycoplasma pneumoniae in organ culture
    • Wilson MH, Collier AM: Ultrastructural study of Mycoplasma pneumoniae in organ culture. J Bacteriol 1976;125:332-339.
    • (1976) J Bacteriol , vol.125 , pp. 332-339
    • Wilson, M.H.1    Collier, A.M.2
  • 87
    • 1242292243 scopus 로고    scopus 로고
    • Cell division gene cluster in Spiroplasma kunkelii: Functional characterization of ftsZ and the first report of ftsA in mollicutes
    • Zhao Y, Hammond RW, Lee IM, Roe BA, Lin S, Davis RE: Cell division gene cluster in Spiroplasma kunkelii: functional characterization of ftsZ and the first report of ftsA in mollicutes. DNA Cell Biol 2004;23:127-134.
    • (2004) DNA Cell Biol , vol.23 , pp. 127-134
    • Zhao, Y.1    Hammond, R.W.2    Lee, I.M.3    Roe, B.A.4    Lin, S.5    Davis, R.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.