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Volumn 141, Issue 1, 2003, Pages 34-42

Pyrodictium cannulae enter the periplasmic space but do not enter the cytoplasm, as revealed by cryo-electron tomography

Author keywords

3D reconstruction; Archaea; Cannulae; Cryo electron tomography; Double tilt; Periplasmic space; Pyrodictium

Indexed keywords

ARCHAEBACTERIUM; ARTICLE; BACTERIAL CELL; CELL STRUCTURE; CRYOELECTRON MICROSCOPY; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; PYRODICTIUM; STRUCTURE ANALYSIS; THREE DIMENSIONAL IMAGING; TOMOGRAPHY;

EID: 0037288048     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1047-8477(02)00581-6     Document Type: Article
Times cited : (82)

References (39)
  • 1
    • 0026467758 scopus 로고
    • Structural features of archaebacterial cell envelopes
    • Baumeister W., Lembcke G. Structural features of archaebacterial cell envelopes. J. Bioenerg. Biomembr. 24:1992;567-575.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 567-575
    • Baumeister, W.1    Lembcke, G.2
  • 2
    • 0034406521 scopus 로고    scopus 로고
    • Macromolecular electron microscopy in the era of structural genomics
    • Baumeister W., Steven A.C. Macromolecular electron microscopy in the era of structural genomics. Trends Biochem. Sci. 25:2000;624-631.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 624-631
    • Baumeister, W.1    Steven, A.C.2
  • 5
    • 0027541315 scopus 로고
    • Toward automatic electron tomography. II. Implementation of autofocus and low-dose procedures
    • Dierksen K., Typke D., Hegerl R., Baumeister W. Toward automatic electron tomography. II. Implementation of autofocus and low-dose procedures. Ultramicroscopy. 49:1993;109-120.
    • (1993) Ultramicroscopy , vol.49 , pp. 109-120
    • Dierksen, K.1    Typke, D.2    Hegerl, R.3    Baumeister, W.4
  • 6
    • 0028953758 scopus 로고
    • Three-dimensional structure of lipid vesicles embedded in vitreous ice and investigated by automated electron tomography
    • Dierksen K., Typke D., Hegerl R., Walz J., Sackmann E., Baumeister W. Three-dimensional structure of lipid vesicles embedded in vitreous ice and investigated by automated electron tomography. Biophys. J. 68:1995;1416-1422.
    • (1995) Biophys. J. , vol.68 , pp. 1416-1422
    • Dierksen, K.1    Typke, D.2    Hegerl, R.3    Walz, J.4    Sackmann, E.5    Baumeister, W.6
  • 7
    • 0032521625 scopus 로고    scopus 로고
    • Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi
    • Dirmeier R., Keller M., Frey G., Huber H., Stetter K.O. Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi. Eur. J. Biochem. 252:1998;486-491.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 486-491
    • Dirmeier, R.1    Keller, M.2    Frey, G.3    Huber, H.4    Stetter, K.O.5
  • 9
    • 0025733570 scopus 로고
    • Three-dimensional reconstruction of the surface protein of Pyrodictium brockii: Comparing two image processing strategies
    • Dürr R., Hegerl R., Volker S., Santorius U., Baumeister W. Three-dimensional reconstruction of the surface protein of Pyrodictium brockii: comparing two image processing strategies. J. Struct. Biol. 106:1991;181-190.
    • (1991) J. Struct. Biol. , vol.106 , pp. 181-190
    • Dürr, R.1    Hegerl, R.2    Volker, S.3    Santorius, U.4    Baumeister, W.5
  • 10
    • 0035057117 scopus 로고    scopus 로고
    • Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters
    • Elferink M.G.L., Albers S.-V., Konings W.N., Driessen A.J.M. Sugar transport in Sulfolobus solfataricus is mediated by two families of binding protein-dependent ABC transporters. Mol. Microbiol. 39:2001;1494-1503.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1494-1503
    • Elferink, M.G.L.1    Albers, S.-V.2    Konings, W.N.3    Driessen, A.J.M.4
  • 12
    • 0030199056 scopus 로고    scopus 로고
    • Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging
    • Grimm R., Typke D., Bärmann M., Baumeister W. Determination of the inelastic mean free path in ice by examination of tilted vesicles and automated most probable loss imaging. Ultramicroscopy. 63:1996;169-179.
    • (1996) Ultramicroscopy , vol.63 , pp. 169-179
    • Grimm, R.1    Typke, D.2    Bärmann, M.3    Baumeister, W.4
  • 15
    • 0000333548 scopus 로고
    • Uridine and dolichol diphosphate activated oligosaccharides are intermediates in the biosynthesis of the S-layer glycoprotein of Methanothermus fervidus
    • Hartmann E., König H. Uridine and dolichol diphosphate activated oligosaccharides are intermediates in the biosynthesis of the S-layer glycoprotein of Methanothermus fervidus. Arch. Microbiol. 151:1989;274-281.
    • (1989) Arch. Microbiol. , vol.151 , pp. 274-281
    • Hartmann, E.1    König, H.2
  • 16
    • 0029879294 scopus 로고    scopus 로고
    • The EM program package: A platform for image processing in biological electron microscopy
    • Hegerl R. The EM program package: A platform for image processing in biological electron microscopy. J. Struct. Biol. 116:1996;30-34.
    • (1996) J. Struct. Biol. , vol.116 , pp. 30-34
    • Hegerl, R.1
  • 17
    • 0032816834 scopus 로고    scopus 로고
    • In vivo observation of cell division of anaerobic hyperthermophiles by using a high-intensity dark-field microscope
    • Horn C., Paulmann B., Kerlen G., Junker N., Huber H. In vivo observation of cell division of anaerobic hyperthermophiles by using a high-intensity dark-field microscope. J. Bacteriol. 181:1999;5114-5118.
    • (1999) J. Bacteriol. , vol.181 , pp. 5114-5118
    • Horn, C.1    Paulmann, B.2    Kerlen, G.3    Junker, N.4    Huber, H.5
  • 18
    • 0034889137 scopus 로고    scopus 로고
    • The tripartite ATP-dependent periplasmic (TRAP) transporters of bacteria and archaea
    • Kelly D.J., Thomas G.H. The tripartite ATP-dependent periplasmic (TRAP) transporters of bacteria and archaea. FEMS Microbiol. Rev. 25:2001;405-424.
    • (2001) FEMS Microbiol. Rev. , vol.25 , pp. 405-424
    • Kelly, D.J.1    Thomas, G.H.2
  • 19
    • 38249032458 scopus 로고
    • The fine structure of the fibres of Pyrodictium occultum
    • König H., Messner P., Stetter K.O. The fine structure of the fibres of Pyrodictium occultum. FEMS Microbiol. Lett. 49:1988;207-212.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 207-212
    • König, H.1    Messner, P.2    Stetter, K.O.3
  • 24
    • 0031422417 scopus 로고    scopus 로고
    • Dual-axis tomography: An approach with alignment methods that preserve resolution
    • Mastronarde D.N. Dual-axis tomography: an approach with alignment methods that preserve resolution. J. Struct. Biol. 120:1997;343-352.
    • (1997) J. Struct. Biol. , vol.120 , pp. 343-352
    • Mastronarde, D.N.1
  • 25
    • 0030156252 scopus 로고    scopus 로고
    • A hyperthermostable protease of the subtilisin family bound to the surface layer of the archaeon Staphylothermus marinus
    • Mayr J., Lupas A., Kellermann J., Eckerskorn C., Baumeister W., Peters J. A hyperthermostable protease of the subtilisin family bound to the surface layer of the archaeon Staphylothermus marinus. Curr. Biol. 6:1996;739-749.
    • (1996) Curr. Biol. , vol.6 , pp. 739-749
    • Mayr, J.1    Lupas, A.2    Kellermann, J.3    Eckerskorn, C.4    Baumeister, W.5    Peters, J.6
  • 26
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakis D., Raina S. Protein folding in the bacterial periplasm. J. Bacteriol. 179:1997;2465-2471.
    • (1997) J. Bacteriol. , vol.179 , pp. 2465-2471
    • Missiakis, D.1    Raina, S.2
  • 30
    • 0028842805 scopus 로고
    • Ultrastructure of the hyperthermophilic archaeon Pyrodictium abyssi
    • Rieger G., Rachel R., Hermann R., Stetter K.O. Ultrastructure of the hyperthermophilic archaeon Pyrodictium abyssi. J. Struct. Biol. 115:1995;78-87.
    • (1995) J. Struct. Biol. , vol.115 , pp. 78-87
    • Rieger, G.1    Rachel, R.2    Hermann, R.3    Stetter, K.O.4
  • 31
    • 0030714623 scopus 로고    scopus 로고
    • Cultivation of hyperthermophilic archaea in capillary tubes resulting in improved preservation of fine structure
    • Rieger G., Müller K., Hermann R., Stetter K.O., Rachel R. Cultivation of hyperthermophilic archaea in capillary tubes resulting in improved preservation of fine structure. Arch. Microbiol. 168:1997;373-379.
    • (1997) Arch. Microbiol. , vol.168 , pp. 373-379
    • Rieger, G.1    Müller, K.2    Hermann, R.3    Stetter, K.O.4    Rachel, R.5
  • 33
    • 0035854480 scopus 로고    scopus 로고
    • Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf Kinase Inhibitor Protein
    • Serre L., Pereira de Jesus K., Zelwer C., Bureaud N., Schoentgen F., Bénédetti H. Crystal structures of YBHB and YBCL from Escherichia coli, two bacterial homologues to a Raf Kinase Inhibitor Protein. J. Mol. Biol. 310:2001;617-634.
    • (2001) J. Mol. Biol. , vol.310 , pp. 617-634
    • Serre, L.1    Pereira de Jesus, K.2    Zelwer, C.3    Bureaud, N.4    Schoentgen, F.5    Bénédetti, H.6
  • 34
    • 0031920998 scopus 로고    scopus 로고
    • Microbial magnesium transport: Unusual transporters searching for identity
    • Smith R.L., Maguire M.E. Microbial magnesium transport: unusual transporters searching for identity. Mol. Microbiol. 28:1998;217-226.
    • (1998) Mol. Microbiol. , vol.28 , pp. 217-226
    • Smith, R.L.1    Maguire, M.E.2
  • 35
    • 0001371296 scopus 로고
    • Ultrathin mycelia-forming organisms from submarine volcanic areas having an optimum growth temperature of 105 °C
    • Stetter K.O. Ultrathin mycelia-forming organisms from submarine volcanic areas having an optimum growth temperature of 105°C Nature. 300:1982;258-260.
    • (1982) Nature , vol.300 , pp. 258-260
    • Stetter, K.O.1
  • 36
    • 85025384988 scopus 로고
    • Pyrodictium gen. nov., a new genus of submarine disc-shaped sulfur reducing archaebacteria growing optimally at 105°C
    • Stetter K.O., König H., Stackebrandt E. Pyrodictium gen. nov., a new genus of submarine disc-shaped sulfur reducing archaebacteria growing optimally at 105°C Syst. Appl. Microbiol. 4:1983;535-551.
    • (1983) Syst. Appl. Microbiol. , vol.4 , pp. 535-551
    • Stetter, K.O.1    König, H.2    Stackebrandt, E.3
  • 37
    • 0029991767 scopus 로고    scopus 로고
    • Hyperthermophilic procaryotes
    • Stetter K.O. Hyperthermophilic procaryotes. FEMS Microbiol. Rev. 18:1996;149-158.
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 149-158
    • Stetter, K.O.1
  • 38
    • 0023235232 scopus 로고
    • Halobacterial glycoprotein biosynthesis
    • Sumper M. Halobacterial glycoprotein biosynthesis. Biochim. Biophys. Acta. 906:1987;69-79.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 69-79
    • Sumper, M.1
  • 39
    • 0025605636 scopus 로고
    • Primary structure and glycosylation of the S-layer protein of Haloferax volcanii
    • Sumper M., Berg E., Mengele R., Strobel I. Primary structure and glycosylation of the S-layer protein of Haloferax volcanii. J. Bacteriol. 172:1990;7111-7118.
    • (1990) J. Bacteriol. , vol.172 , pp. 7111-7118
    • Sumper, M.1    Berg, E.2    Mengele, R.3    Strobel, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.