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Volumn 178, Issue 2, 1996, Pages 332-339

Primary structure of cyanelle peptidoglycan of Cyanophora paradoxa: A prokaryotic cell wall as part of an organelle envelope

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDOGLYCAN;

EID: 0030048929     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.2.332-339.1996     Document Type: Article
Times cited : (68)

References (45)
  • 1
    • 0018391966 scopus 로고
    • Characterization of peptidoglycan from cyanelles of Cyanophora paradoxa
    • Aitken, A., and R. Y. Stanier. 1979. Characterization of peptidoglycan from cyanelles of Cyanophora paradoxa J Gen. Microbiol. 112:219-223.
    • (1979) J Gen. Microbiol. , vol.112 , pp. 219-223
    • Aitken, A.1    Stanier, R.Y.2
  • 2
    • 84990662760 scopus 로고
    • Optimization of sample deposition for plasma desorption mass spectrometry of peptidoglycan monomers
    • Allmaier, G., M. Caparros, and E. Pittenauer. 1992 Optimization of sample deposition for plasma desorption mass spectrometry of peptidoglycan monomers. Rapid Commun. Mass Spectrom. 6:284-288.
    • (1992) Rapid Commun. Mass Spectrom. , vol.6 , pp. 284-288
    • Allmaier, G.1    Caparros, M.2    Pittenauer, E.3
  • 4
    • 0023491106 scopus 로고
    • Penicillin-binding proteins in the cyanelles of Cyanophora paradoxa, a eukaryotic photoautotroph sensitive to β-lactam antibiotics
    • Berenguer, J., F. Rojo, M. A. de Pedro, B. Pfanzagl, and W. Löffelhardt. 1987. Penicillin-binding proteins in the cyanelles of Cyanophora paradoxa, a eukaryotic photoautotroph sensitive to β-lactam antibiotics. FEBS Lett. 224: 401-405.
    • (1987) FEBS Lett. , vol.224 , pp. 401-405
    • Berenguer, J.1    Rojo, F.2    De Pedro, M.A.3    Pfanzagl, B.4    Löffelhardt, W.5
  • 5
    • 0028922903 scopus 로고
    • Comparisons of nuclear-encoded small subunit ribosomal RNAs reveal the evolutionary position of the Glaucocystophyta
    • Bhattacharya, D., T. Helmchen, C. Bibeau, and M. Melkonian. 1995. Comparisons of nuclear-encoded small subunit ribosomal RNAs reveal the evolutionary position of the Glaucocystophyta. Mol. Biol. Evol. 12:415-420.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 415-420
    • Bhattacharya, D.1    Helmchen, T.2    Bibeau, C.3    Melkonian, M.4
  • 6
    • 0020174586 scopus 로고
    • The subcellular location of DNA components from Cyanophora paradoxa, a flagellate containing endosymbiotic cyanelles
    • Bohnert, H. J., E. J. Crouse, J. Pouyet, H. Mueke, and W. Löffelhardt. 1982. The subcellular location of DNA components from Cyanophora paradoxa, a flagellate containing endosymbiotic cyanelles Eur. J. Biochem. 126:381-388
    • (1982) Eur. J. Biochem. , vol.126 , pp. 381-388
    • Bohnert, H.J.1    Crouse, E.J.2    Pouyet, J.3    Mueke, H.4    Löffelhardt, W.5
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0023973882 scopus 로고
    • Physical map and protein gene map of cyanelle DNA from the second known isolate of Cyanophora paradoxa (Kies-strain)
    • Breiteneder, H., C. Seiser, W. Löffelhardt, C. Michalowski, and H. J. Bohnert. 1988. Physical map and protein gene map of cyanelle DNA from the second known isolate of Cyanophora paradoxa (Kies-strain). Curr. Genet 13:199-206
    • (1988) Curr. Genet , vol.13 , pp. 199-206
    • Breiteneder, H.1    Seiser, C.2    Löffelhardt, W.3    Michalowski, C.4    Bohnert, H.J.5
  • 9
    • 0026795665 scopus 로고
    • Effect of D-amino acids on structure and synthesis ot peptidoglycan in Escherichia coli
    • Caparrós, M., A. G. Pisabarro, and M. A. de Pedro. 1992 Effect of D-amino acids on structure and synthesis ot peptidoglycan in Escherichia coli. J. Bacteriol 174:5549-5559.
    • (1992) J. Bacteriol , vol.174 , pp. 5549-5559
    • Caparrós, M.1    Pisabarro, A.G.2    De Pedro, M.A.3
  • 10
    • 0027498126 scopus 로고
    • Molecular weight-determination of biosynthetically modified monomeric and oligomeric muropeptides from Escherichia coli by plasma desorption-mass spectrometry
    • Caparrós, M., E. Pittenauer, E. R. Schmid, M. A. de Pedro, and G. Allmaier. 1993. Molecular weight-determination of biosynthetically modified monomeric and oligomeric muropeptides from Escherichia coli by plasma desorption-mass spectrometry. FEBS Lett. 316:181-185.
    • (1993) FEBS Lett. , vol.316 , pp. 181-185
    • Caparrós, M.1    Pittenauer, E.2    Schmid, E.R.3    De Pedro, M.A.4    Allmaier, G.5
  • 11
    • 0020650682 scopus 로고
    • Amino acid analysis in the picomole range by precolumn derivatization and high-performance liquid chromatography
    • Chang, J.-Y., R. Knecht, and D. G. Braun. 1983. Amino acid analysis in the picomole range by precolumn derivatization and high-performance liquid chromatography. Methods Enzymol. 91:41-48.
    • (1983) Methods Enzymol. , vol.91 , pp. 41-48
    • Chang, J.-Y.1    Knecht, R.2    Braun, D.G.3
  • 13
    • 0001667795 scopus 로고
    • Structure of the thylakoids and envelope membranes of the cyanelles of Cyanophora paradoxa
    • Giddings, T. H., Jr., C. Wasmann, and L. A. Staehelin. 1983. Structure of the thylakoids and envelope membranes of the cyanelles of Cyanophora paradoxa. Plant Physiol. 71:409-419
    • (1983) Plant Physiol. , vol.71 , pp. 409-419
    • Giddings Jr., T.H.1    Wasmann, C.2    Staehelin, L.A.3
  • 14
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with HPLC
    • Glauner, B. 1988 Separation and quantification of muropeptides with HPLC. Anal. Biochem. 172:451-464.
    • (1988) Anal. Biochem. , vol.172 , pp. 451-464
    • Glauner, B.1
  • 15
    • 0023677844 scopus 로고
    • The composition of murein of Escherichia coli
    • Glauner, B., J.-V. Höltje, and U. Schwarz. 1988. The composition of murein of Escherichia coli. J. Biol. Chem. 263:10088-10095.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.-V.2    Schwarz, U.3
  • 16
    • 0025012287 scopus 로고
    • Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography
    • Harz, H., K. Burgdorf, and J.-V. Höltje. 1990. Isolation and separation of the glycan strands from murein of Escherichia coli by reversed-phase high-performance liquid chromatography. Anal. Biochem. 190:120-128.
    • (1990) Anal. Biochem. , vol.190 , pp. 120-128
    • Harz, H.1    Burgdorf, K.2    Höltje, J.-V.3
  • 17
    • 0014199545 scopus 로고
    • The N,O-diacetyl-muramidase of Chalaropsis species; purification and crystallization
    • Hash, J. H., and M. V. Rothlauf. 1967. The N,O-diacetyl-muramidase of Chalaropsis species; purification and crystallization. J. Biol. Chem. 242:5586-5590.
    • (1967) J. Biol. Chem. , vol.242 , pp. 5586-5590
    • Hash, J.H.1    Rothlauf, M.V.2
  • 18
    • 0017389014 scopus 로고
    • The cyanelle: Chloroplast or endosymbiotic procaryote
    • Herdman, M., and R. Y. Stanier. 1977. The cyanelle: chloroplast or endosymbiotic procaryote. FEMS Microbiol. Lett. 1:7-12.
    • (1977) FEMS Microbiol. Lett. , vol.1 , pp. 7-12
    • Herdman, M.1    Stanier, R.Y.2
  • 19
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • Höltje, J. V., D. Mirelman, N. Sharon, and U. Schwarz. 1975. Novel type of murein transglycosylase in Escherichia coli. J. Bacteriol. 124:1067-1076.
    • (1975) J. Bacteriol. , vol.124 , pp. 1067-1076
    • Höltje, J.V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 20
    • 85035158384 scopus 로고    scopus 로고
    • Personal communication
    • Jürgens, U. J. Personal communication.
    • Jürgens, U.J.1
  • 21
    • 0020600413 scopus 로고
    • Primary structure of the peptidoglycan from the unicellular cyanobacterium Synechocystis sp strain PCC 6714
    • Jürgens, U. J., G. Drews, and J. Weckesser. 1983. Primary structure of the peptidoglycan from the unicellular cyanobacterium Synechocystis sp strain PCC 6714. J. Bacteriol. 154:471-478.
    • (1983) J. Bacteriol. , vol.154 , pp. 471-478
    • Jürgens, U.J.1    Drews, G.2    Weckesser, J.3
  • 22
    • 0022996657 scopus 로고
    • Polysaccharide covalently linked to the peptidoglycan of the cyanobacterium Synechocystis sp. strain PCC6714
    • Jurgens, U. J., and J. Weckesser. 1986 Polysaccharide covalently linked to the peptidoglycan of the cyanobacterium Synechocystis sp. strain PCC6714. J. Bacteriol. 168:568-572.
    • (1986) J. Bacteriol. , vol.168 , pp. 568-572
    • Jurgens, U.J.1    Weckesser, J.2
  • 23
    • 0023424893 scopus 로고
    • Structural specificity of diamines covalently linked to peptidoglycan for cell growth of Veillonella alcalescens and Selenomonas ruminantium
    • Kamio, Y. 1987. Structural specificity of diamines covalently linked to peptidoglycan for cell growth of Veillonella alcalescens and Selenomonas ruminantium. J. Bacteriol. 169:4837-4840.
    • (1987) J. Bacteriol. , vol.169 , pp. 4837-4840
    • Kamio, Y.1
  • 24
    • 0019514944 scopus 로고
    • Chemical structure of peptidoglycan in Selenomonas ruminantium. cadaverine links covalently to the D-glutamic acid residue of peptidoglycan
    • Kamio, Y., Y. Itoh, and Y. Terawaki. 1981. Chemical structure of peptidoglycan in Selenomonas ruminantium. cadaverine links covalently to the D-glutamic acid residue of peptidoglycan J. Bacteriol. 146:49-53.
    • (1981) J. Bacteriol. , vol.146 , pp. 49-53
    • Kamio, Y.1    Itoh, Y.2    Terawaki, Y.3
  • 25
    • 0019464726 scopus 로고
    • Cadaverine is covalently linked to peptidoglycan in Selenomonas ruminantium
    • Kamio, Y., Y. Itoh, Y. Terawaki, and T. Kusano. 1981. Cadaverine is covalently linked to peptidoglycan in Selenomonas ruminantium. J. Bacteriol. 145:122-128.
    • (1981) J. Bacteriol. , vol.145 , pp. 122-128
    • Kamio, Y.1    Itoh, Y.2    Terawaki, Y.3    Kusano, T.4
  • 26
    • 0023219970 scopus 로고
    • Putrescine and cadaverine are constituents of peptidoglycan in Veillonella alcalescens and Veillonella parvula
    • Kamio, Y., and K. Nakamura. 1987. Putrescine and cadaverine are constituents of peptidoglycan in Veillonella alcalescens and Veillonella parvula. J. Bacteriol. 169:2881-2884.
    • (1987) J. Bacteriol. , vol.169 , pp. 2881-2884
    • Kamio, Y.1    Nakamura, K.2
  • 27
    • 0023035411 scopus 로고
    • Cadaverine covalently linked to a peptidoglycan is an essential constituent of the peptidoglycan necessary for the normal growth in Selenomonas ruminantium
    • Kamio, Y., H. Pösö, Y. Terawaki, and L. Paulin. 1986 Cadaverine covalently linked to a peptidoglycan is an essential constituent of the peptidoglycan necessary for the normal growth in Selenomonas ruminantium. J. Biol. Chem. 261:6585-6589.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6585-6589
    • Kamio, Y.1    Pösö, H.2    Terawaki, Y.3    Paulin, L.4
  • 28
    • 0020490457 scopus 로고
    • Biosynthesis of cadaverine-containing peptidoglycan in Selenomonas ruminantium
    • Kamio, Y., Y. Terawaki, and K. Izaki. 1982. Biosynthesis of cadaverine-containing peptidoglycan in Selenomonas ruminantium. J. Biol. Chem. 257: 3326-3333.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3326-3333
    • Kamio, Y.1    Terawaki, Y.2    Izaki, K.3
  • 29
    • 0000652750 scopus 로고
    • The effect of penicillin on the morphology and ultrastructure of Cyanophora, Gloeachaete and Glaucocystis (Glaucocystophyceae) and their cyanelles
    • Kies, L. 1988. The effect of penicillin on the morphology and ultrastructure of Cyanophora, Gloeachaete and Glaucocystis (Glaucocystophyceae) and their cyanelles Endocytobiosis Cell Res. 5:361-372
    • (1988) Endocytobiosis Cell Res. , vol.5 , pp. 361-372
    • Kies, L.1
  • 30
    • 0002338681 scopus 로고
    • Molecular biology of cyanelles
    • D. A Bryant (ed.). Kluwer, Dordrecht, The Netherlands
    • Löffelhardt, W., and H. J. Bohnert. 1994. Molecular biology of cyanelles, p. 65-89. In D. A Bryant (ed.), The molecular biology of cyanobacteria. Kluwer, Dordrecht, The Netherlands.
    • (1994) The Molecular Biology of Cyanobacteria , pp. 65-89
    • Löffelhardt, W.1    Bohnert, H.J.2
  • 31
    • 0003064893 scopus 로고
    • Immunocytochemical localization of ribulose-1,5-bisphosphate carboxylase/oxygenase in the cyanelles of Cyanophora paradoxa and Glaucocystis nostochinearum
    • Mangeney, E., and S. P. Gibbs. 1987. Immunocytochemical localization of ribulose-1,5-bisphosphate carboxylase/oxygenase in the cyanelles of Cyanophora paradoxa and Glaucocystis nostochinearum. Eur. J. Cell Biol. 43:65-70.
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 65-70
    • Mangeney, E.1    Gibbs, S.P.2
  • 32
    • 0018868002 scopus 로고
    • Partial characterization of the genome of the "endosymbiotic" cyanelles from Cyanophora paradoxa
    • Mucke, H., W. Löffelhardt, and H. J. Bohnert. 1980 Partial characterization of the genome of the "endosymbiotic" cyanelles from Cyanophora paradoxa. FEBS Lett. 111:347-352.
    • (1980) FEBS Lett. , vol.111 , pp. 347-352
    • Mucke, H.1    Löffelhardt, W.2    Bohnert, H.J.3
  • 36
    • 0025907090 scopus 로고
    • Subcellular distribution of enzymes involved in the biosynthesis of cyanelle murein in the protist Cyanophora paradoxa
    • Plaimauer, B., B. Pfanzagl, J. Berenguer, M. A. de Pedro, and W. Löffelhardt. 1991 Subcellular distribution of enzymes involved in the biosynthesis of cyanelle murein in the protist Cyanophora paradoxa FEBS Lett. 284:169-172
    • (1991) FEBS Lett. , vol.284 , pp. 169-172
    • Plaimauer, B.1    Pfanzagl, B.2    Berenguer, J.3    De Pedro, M.A.4    Löffelhardt, W.5
  • 37
    • 84942558823 scopus 로고
    • Nachweis einer lysozymempfindlichen Stützmembran der Endocyanellen von Cyanophora paradoxa (Korschikoff)
    • Schenk, H. E. A. 1970. Nachweis einer lysozymempfindlichen Stützmembran der Endocyanellen von Cyanophora paradoxa (Korschikoff). Z. Naturforsch Sect. B 25:656.
    • (1970) Z. Naturforsch Sect. B , vol.25 , pp. 656
    • Schenk, H.E.A.1
  • 39
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H., and O. Kandler. 1972. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36:407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 40
    • 0025169931 scopus 로고
    • Taxonomic study of anaerobic, gram-negative, rod-shaped bacteria from breweries: Emended description of Pectinatus cerevisiiphilus and description of Pectinatus frisingensis sp. nov., Selenomonas lacticifex sp. nov., Zymophilus raffinosivorans gen. nov., sp nov., and Zymophilus paucivorans sp. nov.
    • Schleifer, K. H., M. Leuteritz, N. Weiss, W. Ludwig, G. Kirchhof, and H. Seidel-Rüfer. 1990. Taxonomic study of anaerobic, gram-negative, rod-shaped bacteria from breweries: emended description of Pectinatus cerevisiiphilus and description of Pectinatus frisingensis sp. nov., Selenomonas lacticifex sp. nov., Zymophilus raffinosivorans gen. nov., sp nov., and Zymophilus paucivorans sp. nov. Int. J. Syst. Bacteriol. 40:19-27.
    • (1990) Int. J. Syst. Bacteriol. , vol.40 , pp. 19-27
    • Schleifer, K.H.1    Leuteritz, M.2    Weiss, N.3    Ludwig, W.4    Kirchhof, G.5    Seidel-Rüfer, H.6
  • 41
    • 44949273956 scopus 로고
    • 2,5-Dihydroxybenzoic acid: A new matrix for laser desorption ionization mass spectrometry
    • Strupat, K., M. Karas, and F. Hillenkamp 1991. 2,5-Dihydroxybenzoic acid: a new matrix for laser desorption ionization mass spectrometry. Int. J. Mass Spectrom. Ion Processes 111:89-102
    • (1991) Int. J. Mass Spectrom. Ion Processes , vol.111 , pp. 89-102
    • Strupat, K.1    Karas, M.2    Hillenkamp, F.3
  • 42
    • 0000090170 scopus 로고
    • Alkali-catalyzed elimination of D-lactic acid from muramic acid and its derivatives and the determination of muramic acid
    • Tipper, D. J. 1968. Alkali-catalyzed elimination of D-lactic acid from muramic acid and its derivatives and the determination of muramic acid. Biochemistry 7:1441-1449
    • (1968) Biochemistry , vol.7 , pp. 1441-1449
    • Tipper, D.J.1
  • 43
    • 0023853225 scopus 로고
    • Autolysis-resistant peptidoglycan of anomalous composition in amino-acid-starved Escherichia coli
    • Tuomanen, E., Z. Markiewicz, and A. Tomasz. 1988. Autolysis-resistant peptidoglycan of anomalous composition in amino-acid-starved Escherichia coli. J. Bacteriol 170:1373-1376.
    • (1988) J. Bacteriol , vol.170 , pp. 1373-1376
    • Tuomanen, E.1    Markiewicz, Z.2    Tomasz, A.3
  • 44
    • 0026623124 scopus 로고
    • Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: Possible roles of PBP 1b and PBP 3
    • van Heijenoort, Y., M. Gómez, M. Derrien, J. Ayala, and J. van Heijenoort. 1992. Membrane intermediates in the peptidoglycan metabolism of Escherichia coli: possible roles of PBP 1b and PBP 3. J. Bacteriol. 174:3549-3557
    • (1992) J. Bacteriol. , vol.174 , pp. 3549-3557
    • Van Heijenoort, Y.1    Gómez, M.2    Derrien, M.3    Ayala, J.4    Van Heijenoort, J.5
  • 45
    • 70449195156 scopus 로고
    • Reaction of ninhydrin in acid solution with straight chain amino acids containing two amino groups and its application to the estimation of αε-diaminopimelic acid
    • Work, E. 1957 Reaction of ninhydrin in acid solution with straight chain amino acids containing two amino groups and its application to the estimation of αε-diaminopimelic acid. Biochem. J. 67:416-423.
    • (1957) Biochem. J. , vol.67 , pp. 416-423
    • Work, E.1


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