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Volumn 6, Issue 9, 2010, Pages

The metabolic enzyme mana reveals a link between cell wall integrity and chromosome morphology

Author keywords

[No Author keywords available]

Indexed keywords

MANNOSE PHOSPHATE ISOMERASE;

EID: 78049425656     PISSN: 15537390     EISSN: 15537404     Source Type: Journal    
DOI: 10.1371/journal.pgen.1001119     Document Type: Article
Times cited : (27)

References (70)
  • 2
    • 37349041697 scopus 로고    scopus 로고
    • Lipid intermediates in the biosynthesis of bacterial peptidoglycan
    • van Heijenoort J (2007) Lipid intermediates in the biosynthesis of bacterial peptidoglycan. Microbiol Mol Biol Rev 71: 620-635.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 620-635
    • van Heijenoort, J.1
  • 4
    • 65549153535 scopus 로고    scopus 로고
    • Specific labeling of peptidoglycan precursors as a tool for bacterial cell wall studies
    • van Dam V, Olrichs N, Breukink E (2009) Specific labeling of peptidoglycan precursors as a tool for bacterial cell wall studies. Chembiochem 10: 617-624.
    • (2009) Chembiochem , vol.10 , pp. 617-624
    • van Dam, V.1    Olrichs, N.2    Breukink, E.3
  • 5
    • 0037494988 scopus 로고    scopus 로고
    • Control of cell morphogenesis in bacteria: Two distinct ways to make a rod-shaped cell
    • Daniel RA, Errington J (2003) Control of cell morphogenesis in bacteria: two distinct ways to make a rod-shaped cell. Cell 113: 767-776.
    • (2003) Cell , vol.113 , pp. 767-776
    • Daniel, R.A.1    Errington, J.2
  • 6
    • 15944399775 scopus 로고    scopus 로고
    • A magnesium-dependent mreB null mutant: Implications for the role of mreB in Bacillus subtilis
    • Formstone A, Errington J (2005) A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol Microbiol 55: 1646-1657.
    • (2005) Mol Microbiol , vol.55 , pp. 1646-1657
    • Formstone, A.1    Errington, J.2
  • 7
    • 33746639594 scopus 로고    scopus 로고
    • Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics
    • Tiyanont K, Doan T, Lazarus MB, Fang X, Rudner DZ, et al. (2006) Imaging peptidoglycan biosynthesis in Bacillus subtilis with fluorescent antibiotics. Proc Natl Acad Sci U S A 103: 11033-11038.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11033-11038
    • Tiyanont, K.1    Doan, T.2    Lazarus, M.B.3    Fang, X.4    Rudner, D.Z.5
  • 8
    • 34547618469 scopus 로고    scopus 로고
    • FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli
    • Varma A, de Pedro MA, Young KD (2007) FtsZ directs a second mode of peptidoglycan synthesis in Escherichia coli. J Bacteriol 189: 5692-5704.
    • (2007) J Bacteriol , vol.189 , pp. 5692-5704
    • Varma, A.1    de Pedro, M.A.2    Young, K.D.3
  • 10
    • 35948967558 scopus 로고    scopus 로고
    • Skin and bones: The bacterial cytoskeleton, cell wall, and cell morphogenesis
    • Cabeen MT, Jacobs-Wagner C (2007) Skin and bones: the bacterial cytoskeleton, cell wall, and cell morphogenesis. J Cell Biol 179: 381-387.
    • (2007) J Cell Biol , vol.179 , pp. 381-387
    • Cabeen, M.T.1    Jacobs-Wagner, C.2
  • 11
    • 0037237123 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: In vivo dynamics of the actin-like protein Mbl of Bacillus subtilis
    • Carballido-Lopez R, Errington J (2003) The bacterial cytoskeleton: in vivo dynamics of the actin-like protein Mbl of Bacillus subtilis. Dev Cell 4: 19-28.
    • (2003) Dev Cell , vol.4 , pp. 19-28
    • Carballido-Lopez, R.1    Errington, J.2
  • 12
    • 33750713640 scopus 로고    scopus 로고
    • Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB
    • Defeu Soufo HJ, Graumann PL (2006) Dynamic localization and interaction with other Bacillus subtilis actin-like proteins are important for the function of MreB. Mol Microbiol 62: 1340-1356.
    • (2006) Mol Microbiol , vol.62 , pp. 1340-1356
    • Defeu Soufo, H.J.1    Graumann, P.L.2
  • 13
    • 1542616355 scopus 로고    scopus 로고
    • MreB, the cell shape-determining bacterial actin homologue, co-ordinates cell wall morphogenesis in Caulobacter crescentus
    • Figge RM, Divakaruni AV, Gober JW (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
  • 14
    • 2942588534 scopus 로고    scopus 로고
    • An actin-like gene can determine cell polarity in bacteria
    • Gitai Z, Dye N, Shapiro L (2004) An actin-like gene can determine cell polarity in bacteria. Proc Natl Acad Sci U S A 101: 8643-8648.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8643-8648
    • Gitai, Z.1    Dye, N.2    Shapiro, L.3
  • 15
    • 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
  • 16
    • 33645999343 scopus 로고    scopus 로고
    • Structures of Staphylococcus aureus cell-wall complexes with vancomycin, eremomycin, and chloroeremomycin derivatives by 13C{19F} and 15N{19F} rotational-echo double resonance
    • Kim SJ, Cegelski L, Preobrazhenskaya M, Schaefer J (2006) Structures of Staphylococcus aureus cell-wall complexes with vancomycin, eremomycin, and chloroeremomycin derivatives by 13C{19F} and 15N{19F} rotational-echo double resonance. Biochemistry 45: 5235-5250.
    • (2006) Biochemistry , vol.45 , pp. 5235-5250
    • Kim, S.J.1    Cegelski, L.2    Preobrazhenskaya, M.3    Schaefer, J.4
  • 17
    • 33747837700 scopus 로고    scopus 로고
    • Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE
    • Carballido-Lopez R, Formstone A, Li Y, Ehrlich SD, Noirot P, et al. (2006) Actin homolog MreBH governs cell morphogenesis by localization of the cell wall hydrolase LytE. Dev Cell 11: 399-409.
    • (2006) Dev Cell , vol.11 , pp. 399-409
    • Carballido-Lopez, R.1    Formstone, A.2    Li, Y.3    Ehrlich, S.D.4    Noirot, P.5
  • 18
    • 39749142159 scopus 로고    scopus 로고
    • Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli
    • Bendezu FO, de Boer PA (2008) Conditional lethality, division defects, membrane involution, and endocytosis in mre and mrd shape mutants of Escherichia coli. J Bacteriol 190: 1792-1811.
    • (2008) J Bacteriol , vol.190 , pp. 1792-1811
    • Bendezu, F.O.1    de Boer, P.A.2
  • 19
    • 0031944802 scopus 로고    scopus 로고
    • Control of cell shape and elongation by the rodA gene in Bacillus subtilis
    • Henriques AO, Glaser P, Piggot PJ, Moran CP, Jr. (1998) Control of cell shape and elongation by the rodA gene in Bacillus subtilis. Mol Microbiol 28: 235-247.
    • (1998) Mol Microbiol , vol.28 , pp. 235-247
    • Henriques, A.O.1    Glaser, P.2    Piggot, P.J.3    Moran Jr., C.P.4
  • 20
    • 12344306119 scopus 로고    scopus 로고
    • The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex
    • Kruse T, Bork-Jensen J, Gerdes K (2005) The morphogenetic MreBCD proteins of Escherichia coli form an essential membrane-bound complex. Mol Microbiol 55: 78-89.
    • (2005) Mol Microbiol , vol.55 , pp. 78-89
    • Kruse, T.1    Bork-Jensen, J.2    Gerdes, K.3
  • 21
    • 0141864658 scopus 로고    scopus 로고
    • Dysfunctional MreB inhibits chromosome segregation in Escherichia coli
    • Kruse T, Moller-Jensen J, Lobner-Olesen A, Gerdes K (2003) Dysfunctional MreB inhibits chromosome segregation in Escherichia coli. EMBO J 22: 5283-5292.
    • (2003) EMBO J , vol.22 , pp. 5283-5292
    • Kruse, T.1    Moller-Jensen, J.2    Lobner-Olesen, A.3    Gerdes, K.4
  • 22
    • 33745278528 scopus 로고    scopus 로고
    • Cell wall assembly in Bacillus subtilis: How spirals and spaces challenge paradigms
    • Bhavsar AP, Brown ED (2006) Cell wall assembly in Bacillus subtilis: how spirals and spaces challenge paradigms. Mol Microbiol 60: 1077-1090.
    • (2006) Mol Microbiol , vol.60 , pp. 1077-1090
    • Bhavsar, A.P.1    Brown, E.D.2
  • 23
    • 0038063761 scopus 로고
    • The synthesis of teichoic acids. I. polyglycerophosphate
    • Burger MM, Glaser L (1964) The Synthesis of Teichoic Acids. I. Polyglycerophosphate. J Biol Chem 239: 3168-3177.
    • (1964) J Biol Chem , vol.239 , pp. 3168-3177
    • Burger, M.M.1    Glaser, L.2
  • 24
    • 0347917654 scopus 로고
    • The Synthesis of Teichoic Acids. 3. Glucosylation of Polyglycerophosphate
    • Glaser L, Burger MM (1964) The Synthesis of Teichoic Acids. 3. Glucosylation of Polyglycerophosphate. J Biol Chem 239: 3187-3191.
    • (1964) J Biol Chem , vol.239 , pp. 3187-3191
    • Glaser, L.1    Burger, M.M.2
  • 25
    • 0015459457 scopus 로고
    • The location of Nacetylgalactosamine in the walls of Bacillus subtilis 168
    • Duckworth M, Archibald AR, Baddiley J (1972) The location of Nacetylgalactosamine in the walls of Bacillus subtilis 168. Biochem J 130: 691-696.
    • (1972) Biochem J , vol.130 , pp. 691-696
    • Duckworth, M.1    Archibald, A.R.2    Baddiley, J.3
  • 26
    • 0015845933 scopus 로고
    • The structure of a polymer containing galactosamine from walls of Bacillus subtilis 168
    • Shibaev VN, Duckworth M, Archibald AR, Baddiley J (1973) The structure of a polymer containing galactosamine from walls of Bacillus subtilis 168. Biochem J 135: 383-384.
    • (1973) Biochem J , vol.135 , pp. 383-384
    • Shibaev, V.N.1    Duckworth, M.2    Archibald, A.R.3    Baddiley, J.4
  • 27
  • 28
    • 0034749923 scopus 로고    scopus 로고
    • Precise deletion of tagD and controlled depletion of its product, glycerol 3-phosphate cytidylyltransferase, leads to irregular morphology and lysis of Bacillus subtilis grown at physiological temperature
    • Bhavsar AP, Beveridge TJ, Brown ED (2001) Precise deletion of tagD and controlled depletion of its product, glycerol 3-phosphate cytidylyltransferase, leads to irregular morphology and lysis of Bacillus subtilis grown at physiological temperature. J Bacteriol 183: 6688-6693.
    • (2001) J Bacteriol , vol.183 , pp. 6688-6693
    • Bhavsar, A.P.1    Beveridge, T.J.2    Brown, E.D.3
  • 29
    • 33751585943 scopus 로고    scopus 로고
    • Wall teichoic acid polymers are dispensable for cell viability in Bacillus subtilis
    • D'Elia MA, Millar KE, Beveridge TJ, Brown ED (2006) Wall teichoic acid polymers are dispensable for cell viability in Bacillus subtilis. J Bacteriol 188: 8313-8316.
    • (2006) J Bacteriol , vol.188 , pp. 8313-8316
    • D'Elia, M.A.1    Millar, K.E.2    Beveridge, T.J.3    Brown, E.D.4
  • 30
    • 65449173646 scopus 로고    scopus 로고
    • Distinct and essential morphogenic functions for wall- and lipo-teichoic acids in Bacillus subtilis
    • Schirner K, Marles-Wright J, Lewis RJ, Errington J (2009) Distinct and essential morphogenic functions for wall- and lipo-teichoic acids in Bacillus subtilis. EMBO J 28: 830-842.
    • (2009) EMBO J , vol.28 , pp. 830-842
    • Schirner, K.1    Marles-Wright, J.2    Lewis, R.J.3    Errington, J.4
  • 31
    • 0036063920 scopus 로고    scopus 로고
    • Characterization of a Bacillus subtilis thermosensitive teichoic acid-deficient mutant: Gene mnaA (yvyH) encodes the UDP-N-acetylglucosamine 2-epimerase
    • Soldo B, Lazarevic V, Pooley HM, Karamata D (2002) Characterization of a Bacillus subtilis thermosensitive teichoic acid-deficient mutant: gene mnaA (yvyH) encodes the UDP-N-acetylglucosamine 2-epimerase. J Bacteriol 184: 4316-4320.
    • (2002) J Bacteriol , vol.184 , pp. 4316-4320
    • Soldo, B.1    Lazarevic, V.2    Pooley, H.M.3    Karamata, D.4
  • 32
    • 0029988489 scopus 로고    scopus 로고
    • The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution
    • Cleasby A, Wonacott A, Skarzynski T, Hubbard RE, Davies GJ, et al. (1996) The x-ray crystal structure of phosphomannose isomerase from Candida albicans at 1.7 angstrom resolution. Nat Struct Biol 3: 470-479.
    • (1996) Nat Struct Biol , vol.3 , pp. 470-479
    • Cleasby, A.1    Wonacott, A.2    Skarzynski, T.3    Hubbard, R.E.4    Davies, G.J.5
  • 33
    • 0030910954 scopus 로고    scopus 로고
    • Dynamic, mitotic-like behavior of a bacterial protein required for accurate chromosome partitioning
    • Glaser P, Sharpe ME, Raether B, Perego M, Ohlsen K, et al. (1997) Dynamic, mitotic-like behavior of a bacterial protein required for accurate chromosome partitioning. Genes Dev 11: 1160-1168.
    • (1997) Genes Dev , vol.11 , pp. 1160-1168
    • Glaser, P.1    Sharpe, M.E.2    Raether, B.3    Perego, M.4    Ohlsen, K.5
  • 34
    • 0032489548 scopus 로고    scopus 로고
    • Identification and characterization of a bacterial chromosome partitioning site
    • Lin DC, Grossman AD (1998) Identification and characterization of a bacterial chromosome partitioning site. Cell 92: 675-685.
    • (1998) Cell , vol.92 , pp. 675-685
    • Lin, D.C.1    Grossman, A.D.2
  • 35
    • 0031001565 scopus 로고    scopus 로고
    • Bipolar localization of a chromosome partition protein in Bacillus subtilis
    • Lin DC, Levin PA, Grossman AD (1997) Bipolar localization of a chromosome partition protein in Bacillus subtilis. Proc Natl Acad Sci U S A 94: 4721-4726.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4721-4726
    • Lin, D.C.1    Levin, P.A.2    Grossman, A.D.3
  • 36
    • 65549149524 scopus 로고    scopus 로고
    • Recruitment of SMC by ParBparS organizes the origin region and promotes efficient chromosome segregation
    • Sullivan NL, Marquis KA, Rudner DZ (2009) Recruitment of SMC by ParBparS organizes the origin region and promotes efficient chromosome segregation. Cell 137: 697-707.
    • (2009) Cell , vol.137 , pp. 697-707
    • Sullivan, N.L.1    Marquis, K.A.2    Rudner, D.Z.3
  • 37
    • 33847383586 scopus 로고    scopus 로고
    • Nutritional control of elongation of DNA replication by (p)ppGpp
    • Wang JD, Sanders GM, Grossman AD (2007) Nutritional control of elongation of DNA replication by (p)ppGpp. Cell 128: 865-875.
    • (2007) Cell , vol.128 , pp. 865-875
    • Wang, J.D.1    Sanders, G.M.2    Grossman, A.D.3
  • 38
    • 0014413357 scopus 로고
    • Chromosome replication and the division cycle of Escherichia coli B/r
    • Cooper S, Helmstetter CE (1968) Chromosome replication and the division cycle of Escherichia coli B/r. J Mol Biol 31: 519-540.
    • (1968) J Mol Biol , vol.31 , pp. 519-540
    • Cooper, S.1    Helmstetter, C.E.2
  • 39
    • 0029003406 scopus 로고
    • Primosome assembly site in Bacillus subtilis
    • Bruand C, Ehrlich SD, Janniere L (1995) Primosome assembly site in Bacillus subtilis. EMBO J 14: 2642-2650.
    • (1995) EMBO J , vol.14 , pp. 2642-2650
    • Bruand, C.1    Ehrlich, S.D.2    Janniere, L.3
  • 40
    • 85047698887 scopus 로고
    • Nucleotide sequence and organization of dnaB gene and neighbouring genes on the Bacillus subtilis chromosome
    • Ogasawara N, Moriya S, Mazza PG, Yoshikawa H (1986) Nucleotide sequence and organization of dnaB gene and neighbouring genes on the Bacillus subtilis chromosome. Nucleic Acids Res 14: 9989-9999.
    • (1986) Nucleic Acids Res , vol.14 , pp. 9989-9999
    • Ogasawara, N.1    Moriya, S.2    Mazza, P.G.3    Yoshikawa, H.4
  • 41
    • 0037407703 scopus 로고    scopus 로고
    • Growth rate-dependent regulation of medial FtsZ ring formation
    • Weart RB, Levin PA (2003) Growth rate-dependent regulation of medial FtsZ ring formation. J Bacteriol 185: 2826-2834.
    • (2003) J Bacteriol , vol.185 , pp. 2826-2834
    • Weart, R.B.1    Levin, P.A.2
  • 42
    • 0029902635 scopus 로고    scopus 로고
    • Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: Inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli
    • Brandish PE, Kimura KI, Inukai M, Southgate R, Lonsdale JT, et al. (1996) Modes of action of tunicamycin, liposidomycin B, and mureidomycin A: inhibition of phospho-N-acetylmuramyl-pentapeptide translocase from Escherichia coli. Antimicrob Agents Chemother 40: 1640-1644.
    • (1996) Antimicrob Agents Chemother , vol.40 , pp. 1640-1644
    • Brandish, P.E.1    Kimura, K.I.2    Inukai, M.3    Southgate, R.4    Lonsdale, J.T.5
  • 43
    • 0034077595 scopus 로고    scopus 로고
    • Incorporation of [2-3H] glycerol into cell surface components of Bacillus subtilis 168 and thermosensitive mutants affected in wall teichoic acid synthesis: Effect of tunicamycin
    • Pooley HM, Karamata D (2000) Incorporation of [2-3H] glycerol into cell surface components of Bacillus subtilis 168 and thermosensitive mutants affected in wall teichoic acid synthesis: effect of tunicamycin. Microbiology 146 (Pt 4): 797-805.
    • (2000) Microbiology , vol.146 , Issue.PART 4 , pp. 797-805
    • Pooley, H.M.1    Karamata, D.2
  • 44
    • 37549030896 scopus 로고    scopus 로고
    • Cell wall carbohydrate compositions of strains from the Bacillus cereus group of species correlate with phylogenetic relatedness
    • Leoff C, Saile E, Sue D, Wilkins P, Quinn CP, et al. (2008) Cell wall carbohydrate compositions of strains from the Bacillus cereus group of species correlate with phylogenetic relatedness. J Bacteriol 190: 112-121.
    • (2008) J Bacteriol , vol.190 , pp. 112-121
    • Leoff, C.1    Saile, E.2    Sue, D.3    Wilkins, P.4    Quinn, C.P.5
  • 47
    • 0028091843 scopus 로고
    • An investigation of enumeration and DNA partitioning in Bacillus subtilis L-form bacteria
    • Waterhouse RN, Allan EJ, Amijee F, Undrill VJ, Glover LA (1994) An investigation of enumeration and DNA partitioning in Bacillus subtilis L-form bacteria. J Appl Bacteriol 77: 497-503.
    • (1994) J Appl Bacteriol , vol.77 , pp. 497-503
    • Waterhouse, R.N.1    Allan, E.J.2    Amijee, F.3    Undrill, V.J.4    Glover, L.A.5
  • 48
    • 0037157178 scopus 로고    scopus 로고
    • Bifunctional phosphomannose isomerase/GDP-D-mannose pyrophosphorylase is the point of control for GDP-D-mannose biosynthesis in Helicobacter pylori
    • Wu B, Zhang Y, Zheng R, Guo C, Wang PG (2002) Bifunctional phosphomannose isomerase/GDP-D-mannose pyrophosphorylase is the point of control for GDP-D-mannose biosynthesis in Helicobacter pylori. FEBS Lett 519: 87-92.
    • (2002) FEBS Lett , vol.519 , pp. 87-92
    • Wu, B.1    Zhang, Y.2    Zheng, R.3    Guo, C.4    Wang, P.G.5
  • 50
    • 71049157096 scopus 로고    scopus 로고
    • Characterization of the Aspergillus fumigatus phosphomannose isomerase Pmi1 and its impact on cell wall synthesis and morphogenesis
    • Fang W, Yu X, Wang B, Zhou H, Ouyang H, et al. (2009) Characterization of the Aspergillus fumigatus phosphomannose isomerase Pmi1 and its impact on cell wall synthesis and morphogenesis. Microbiology 155: 3281-3293.
    • (2009) Microbiology , vol.155 , pp. 3281-3293
    • Fang, W.1    Yu, X.2    Wang, B.3    Zhou, H.4    Ouyang, H.5
  • 51
    • 67649394401 scopus 로고    scopus 로고
    • Active transcription of rRNA operons condenses the nucleoid in Escherichia coli: Examining the effect of transcription on nucleoid structure in the absence of transertion
    • Cabrera JE, Cagliero C, Quan S, Squires CL, Jin DJ (2009) Active transcription of rRNA operons condenses the nucleoid in Escherichia coli: examining the effect of transcription on nucleoid structure in the absence of transertion. J Bacteriol 191: 4180-4185.
    • (2009) J Bacteriol , vol.191 , pp. 4180-4185
    • Cabrera, J.E.1    Cagliero, C.2    Quan, S.3    Squires, C.L.4    Jin, D.J.5
  • 52
    • 0036050398 scopus 로고    scopus 로고
    • The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation
    • Woldringh CL (2002) The role of co-transcriptional translation and protein translocation (transertion) in bacterial chromosome segregation. Mol Microbiol 45: 17-29.
    • (2002) Mol Microbiol , vol.45 , pp. 17-29
    • Woldringh, C.L.1
  • 53
    • 59649121975 scopus 로고    scopus 로고
    • RodZ, a new player in bacterial cell morphogenesis
    • Gerdes K (2009) RodZ, a new player in bacterial cell morphogenesis. EMBO J 28: 171-172.
    • (2009) EMBO J , vol.28 , pp. 171-172
    • Gerdes, K.1
  • 54
    • 59649113418 scopus 로고    scopus 로고
    • RodZ (YfgA) is required for proper assembly of the MreB actin cytoskeleton and cell shape in E. coli
    • 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) EMBO J , vol.28 , pp. 193-204
    • Bendezu, F.O.1    Hale, C.A.2    Bernhardt, T.G.3    de Boer, P.A.4
  • 55
    • 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
  • 57
    • 0142093602 scopus 로고    scopus 로고
    • SetB: An integral membrane protein that affects chromosome segregation in Escherichia coli
    • Espeli O, Nurse P, Levine C, Lee C, Marians KJ (2003) SetB: an integral membrane protein that affects chromosome segregation in Escherichia coli. Mol Microbiol 50: 495-509.
    • (2003) Mol Microbiol , vol.50 , pp. 495-509
    • Espeli, O.1    Nurse, P.2    Levine, C.3    Lee, C.4    Marians, K.J.5
  • 58
    • 0040436094 scopus 로고    scopus 로고
    • Functional and biochemical characterization of Escherichia coli sugar efflux transporters
    • Liu JY, Miller PF, Willard J, Olson ER (1999) Functional and biochemical characterization of Escherichia coli sugar efflux transporters. J Biol Chem 274: 22977-22984.
    • (1999) J Biol Chem , vol.274 , pp. 22977-22984
    • Liu, J.Y.1    Miller, P.F.2    Willard, J.3    Olson, E.R.4
  • 60
    • 0028365984 scopus 로고
    • From peptidoglycan to glycoproteins: Common features of lipid-linked oligosaccharide biosynthesis
    • Bugg TD, Brandish PE (1994) From peptidoglycan to glycoproteins: common features of lipid-linked oligosaccharide biosynthesis. FEMS Microbiol Lett 119: 255-262.
    • (1994) FEMS Microbiol Lett , vol.119 , pp. 255-262
    • Bugg, T.D.1    Brandish, P.E.2
  • 61
    • 24044494631 scopus 로고    scopus 로고
    • Modeling bacterial UDP-HexNAc: Polyprenol-P HexNAc-1-P transferases
    • Price NP, Momany FA (2005) Modeling bacterial UDP-HexNAc: polyprenol-P HexNAc-1-P transferases. Glycobiology 15: 29R-42R.
    • (2005) Glycobiology , vol.15
    • Price, N.P.1    Momany, F.A.2
  • 62
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A, Aebi M (2001) Intracellular functions of N-linked glycans. Science 291: 2364-2369.
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 63
    • 0018803824 scopus 로고
    • Mechanism of action of tunicamycin on the UDP-GlcNAc: Dolichyl-phosphate Glc-NAc-1-phosphate transferase
    • Heifetz A, Keenan RW, Elbein AD (1979) Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase. Biochemistry 18: 2186-2192.
    • (1979) Biochemistry , vol.18 , pp. 2186-2192
    • Heifetz, A.1    Keenan, R.W.2    Elbein, A.D.3
  • 64
    • 0035937852 scopus 로고    scopus 로고
    • Oligosaccharide-based information in endoplasmic reticulum quality control and other biological systems
    • Lehrman MA (2001) Oligosaccharide-based information in endoplasmic reticulum quality control and other biological systems. J Biol Chem 276: 8623-8626.
    • (2001) J Biol Chem , vol.276 , pp. 8623-8626
    • Lehrman, M.A.1
  • 65
    • 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 JB, Losick R (1984) 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. Plasmid 12: 1-9.
    • (1984) Plasmid , vol.12 , pp. 1-9
    • Youngman, P.1    Perkins, J.B.2    Losick, R.3
  • 67
    • 0019168132 scopus 로고
    • Enzyme changes during Bacillus subtilis sporulation caused by deprivation of guanine nucleotides
    • Vasantha N, Freese E (1980) Enzyme changes during Bacillus subtilis sporulation caused by deprivation of guanine nucleotides. J Bacteriol 144: 1119-1125.
    • (1980) J Bacteriol , vol.144 , pp. 1119-1125
    • Vasantha, N.1    Freese, E.2
  • 68
    • 1942468855 scopus 로고    scopus 로고
    • Genes governing swarming in Bacillus subtilis and evidence for a phase variation mechanism controlling surface motility
    • Kearns DB, Chu F, Rudner R, Losick R (2004) Genes governing swarming in Bacillus subtilis and evidence for a phase variation mechanism controlling surface motility. Mol Microbiol 52: 357-369.
    • (2004) Mol Microbiol , vol.52 , pp. 357-369
    • Kearns, D.B.1    Chu, F.2    Rudner, R.3    Losick, R.4
  • 69
    • 0028345372 scopus 로고
    • Easy cloning of mini-Tn10 insertions from the Bacillus subtilis chromosome
    • Steinmetz M, Richter R (1994) Easy cloning of mini-Tn10 insertions from the Bacillus subtilis chromosome. J Bacteriol 176: 1761-1763.
    • (1994) J Bacteriol , vol.176 , pp. 1761-1763
    • Steinmetz, M.1    Richter, R.2
  • 70
    • 33646501915 scopus 로고    scopus 로고
    • A checkpoint protein that scans the chromosome for damage at the start of sporulation in Bacillus subtilis
    • Bejerano-Sagie M, Oppenheimer-Shaanan Y, Berlatzky I, Rouvinski A, Meyerovich M, et al. (2006) A checkpoint protein that scans the chromosome for damage at the start of sporulation in Bacillus subtilis. Cell 125: 679-690.
    • (2006) Cell , vol.125 , pp. 679-690
    • Bejerano-Sagie, M.1    Oppenheimer-Shaanan, Y.2    Berlatzky, I.3    Rouvinski, A.4    Meyerovich, M.5


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