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Volumn 62, Issue 2, 2005, Pages 69-83

Three-dimensional reconstruction of axonemal outer dynein arms in situ by electron tomography

Author keywords

Deep etch; Dynein; Electron microscopy; Microtubule based motors; Quick freeze

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 26444460293     PISSN: 08861544     EISSN: None     Source Type: Journal    
DOI: 10.1002/cm.20084     Document Type: Article
Times cited : (38)

References (53)
  • 1
    • 0035341592 scopus 로고    scopus 로고
    • The dynein heavy chain: Structure, mechanics and evolution
    • Asai DJ, Koonce MP. 2001. The dynein heavy chain: structure, mechanics and evolution. Trends Cell Biol 11:196-202.
    • (2001) Trends Cell Biol , vol.11 , pp. 196-202
    • Asai, D.J.1    Koonce, M.P.2
  • 2
    • 0016244574 scopus 로고
    • The spermatozoon of arthropoda XXV. A new model of tail having up to 170 doublets: Monarthropalpus buxi
    • Baccetti B, Dallai R, Giusti F, Bernini F. 1974. The spermatozoon of arthropoda XXV. A new model of tail having up to 170 doublets: Monarthropalpus buxi. Tissue Cell 6:269-278.
    • (1974) Tissue Cell , vol.6 , pp. 269-278
    • Baccetti, B.1    Dallai, R.2    Giusti, F.3    Bernini, F.4
  • 3
    • 14544297527 scopus 로고    scopus 로고
    • From proteomic inventory to architecture
    • Baumeister W. 2005. From proteomic inventory to architecture. FEBS Lett 579:933-937.
    • (2005) FEBS Lett , vol.579 , pp. 933-937
    • Baumeister, W.1
  • 4
    • 0026467758 scopus 로고
    • Structural features of archaebacterial cell envelopes
    • Baumeister W, Lembcke G. 1992. Structural features of archaebacterial cell envelopes. J Bioenerg Biomembr 24:567-575.
    • (1992) J Bioenerg Biomembr , vol.24 , pp. 567-575
    • Baumeister, W.1    Lembcke, G.2
  • 5
    • 0034406521 scopus 로고    scopus 로고
    • Macromolecular electron microscopy in the area of structural genomics
    • Baumeister W, Steven CA. 2000. Macromolecular electron microscopy in the area of structural genomics. Trends Biochem Sci 25:624-631.
    • (2000) Trends Biochem Sci , vol.25 , pp. 624-631
    • Baumeister, W.1    Steven, C.A.2
  • 6
  • 7
    • 0029068861 scopus 로고
    • Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella
    • Burgess SA. 1995. Rigor and relaxed outer dynein arms in replicas of cryofixed motile flagella. J Mol Biol 250:52-63.
    • (1995) J Mol Biol , vol.250 , pp. 52-63
    • Burgess, S.A.1
  • 8
    • 0026071078 scopus 로고
    • Architecture of the outer arm dynein ATPase in an avian sperm flagellum, with further evidence for the B-link
    • Burgess SA, Dover SD, Woolley DM. 1991. Architecture of the outer arm dynein ATPase in an avian sperm flagellum, with further evidence for the B-link. J Cell Sci 98:17-26.
    • (1991) J Cell Sci , vol.98 , pp. 17-26
    • Burgess, S.A.1    Dover, S.D.2    Woolley, D.M.3
  • 11
    • 0002115909 scopus 로고
    • The fidelity of 3D reconstructions from incomplete data and the use of restoration methods
    • Frank J, editor. NY: Plenum
    • Carazo JM. 1992. The fidelity of 3D reconstructions from incomplete data and the use of restoration methods. In: Frank J, editor. Electron Tomography. NY: Plenum, p 117-164.
    • (1992) Electron Tomography , pp. 117-164
    • Carazo, J.M.1
  • 12
    • 84985231785 scopus 로고
    • Information recovery in missing angular cases: An approach by convex projections method in three dimensions
    • Carazo JM, Carrascosa JL. 1987. Information recovery in missing angular cases: an approach by convex projections method in three dimensions. J Microsc 145:23-43.
    • (1987) J Microsc , vol.145 , pp. 23-43
    • Carazo, J.M.1    Carrascosa, J.L.2
  • 14
    • 0000305995 scopus 로고
    • Alignment by cross-correlation
    • Frank J, editor. NY: Plenum
    • Frank J, McEwen BF. 1992. Alignment by cross-correlation. In: Frank J, editor. Electron Tomography. NY: Plenum, p 205-213.
    • (1992) Electron Tomography , pp. 205-213
    • Frank, J.1    McEwen, B.F.2
  • 15
    • 0001797994 scopus 로고
    • Three-dimensional reconstruction of nonperiodic macromolecular assemblies from electron micrographs
    • Koehler J, editor. Berlin: Springer-Verlag
    • Frank J, Radermacher M. 1986. Three-dimensional reconstruction of nonperiodic macromolecular assemblies from electron micrographs. In: Koehler J, editor. Advanced Techniques in Biological Electron Microscopy. Berlin: Springer-Verlag, p 1-72.
    • (1986) Advanced Techniques in Biological Electron Microscopy , pp. 1-72
    • Frank, J.1    Radermacher, M.2
  • 16
    • 0031444202 scopus 로고    scopus 로고
    • An extended microtubule-binding structure within the dynein motor domain
    • Gee MA, Heuser JE, Vallee RB. 1997. An extended microtubule-binding structure within the dynein motor domain. Nature 390:636-639.
    • (1997) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 17
    • 0020410980 scopus 로고
    • Structure of the outer dynein arm
    • Goodenough UW, Heuser JE. 1982. Structure of the outer dynein arm. J Cell Biol 95:798-815.
    • (1982) J Cell Biol , vol.95 , pp. 798-815
    • Goodenough, U.W.1    Heuser, J.E.2
  • 18
    • 0021630304 scopus 로고
    • Structural comparison of purified dynein proteins with in situ dynein arms
    • Goodenough UW, Heuser JE. 1984. Structural comparison of purified dynein proteins with in situ dynein arms. J Mol Biol 180:1083-1118.
    • (1984) J Mol Biol , vol.180 , pp. 1083-1118
    • Goodenough, U.W.1    Heuser, J.E.2
  • 19
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson PI, Roth R, Morisaki H, Jahn R, Heuser JE. 1997. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90:523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 20
    • 0141865704 scopus 로고    scopus 로고
    • Untangling desmosomal knots with electron tomography
    • He W, Cowin P, Stokes D. 2003. Untangling desmosomal knots with electron tomography. Science 302:109-113.
    • (2003) Science , vol.302 , pp. 109-113
    • He, W.1    Cowin, P.2    Stokes, D.3
  • 21
    • 0019343461 scopus 로고
    • Preparing biological samples for stereomicroscopy by the quick-freeze, deep-etch, rotary-replication technique
    • Heuser J. 1981. Preparing biological samples for stereomicroscopy by the quick-freeze, deep-etch, rotary-replication technique. Meth Cell Biol 22:97-122.
    • (1981) Meth Cell Biol , vol.22 , pp. 97-122
    • Heuser, J.1
  • 22
    • 0026078742 scopus 로고
    • Alignment of tomographic projections using an incomplete set of fiducial markers
    • Jing ZQ, Sachs F. 1991. Alignment of tomographic projections using an incomplete set of fiducial markers. Ultramicroscopy 35:37-43.
    • (1991) Ultramicroscopy , vol.35 , pp. 37-43
    • Jing, Z.Q.1    Sachs, F.2
  • 23
    • 0020730789 scopus 로고
    • Structure and molecular weight of the dynein ATPase
    • Johnson KA, Wall JS. 1983. Structure and molecular weight of the dynein ATPase. J Cell Biol 96:669-678.
    • (1983) J Cell Biol , vol.96 , pp. 669-678
    • Johnson, K.A.1    Wall, J.S.2
  • 24
    • 0027097082 scopus 로고
    • Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein
    • Kagami O, Kamiya R. 1992. Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein. J Cell Sci 103:653-664.
    • (1992) J Cell Sci , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 25
    • 0033895197 scopus 로고    scopus 로고
    • AAA domains and organization of the dynein motor unit
    • King SM. 2000. AAA domains and organization of the dynein motor unit. J Cell Sci 113:2521-2526.
    • (2000) J Cell Sci , vol.113 , pp. 2521-2526
    • King, S.M.1
  • 26
  • 27
    • 11144223254 scopus 로고    scopus 로고
    • Conical tomography of freeze-fracture replicas: A method for the study of integral membrane proteins inserted in phospholipid bilayers
    • Lanzavecchia S, Cantele F, Bellon PL, Zampighi L, Kreman M, Wright E, Zampighi GA. 2005. Conical tomography of freeze-fracture replicas: a method for the study of integral membrane proteins inserted in phospholipid bilayers. J Struct Biol 149:87-98.
    • (2005) J Struct Biol , vol.149 , pp. 87-98
    • Lanzavecchia, S.1    Cantele, F.2    Bellon, P.L.3    Zampighi, L.4    Kreman, M.5    Wright, E.6    Zampighi, G.A.7
  • 28
    • 0002439918 scopus 로고
    • Least-squares methods of alignment using markers
    • Frank J, editor. NY: Plenum
    • Lawrence MC. 1992. Least-squares methods of alignment using markers. In: Frank J, editor. Electron Tomography. NY: Plenum, p 197-204.
    • (1992) Electron Tomography , pp. 197-204
    • Lawrence, M.C.1
  • 29
    • 0024757533 scopus 로고
    • The application of the maximum entropy method to electron microscopic tomography
    • Lawrence MC, Jaffer MA, Sewell BT. 1989. The application of the maximum entropy method to electron microscopic tomography. Ultramicroscopy 31:285-302.
    • (1989) Ultramicroscopy , vol.31 , pp. 285-302
    • Lawrence, M.C.1    Jaffer, M.A.2    Sewell, B.T.3
  • 30
    • 0345714919 scopus 로고    scopus 로고
    • Does axonemal dynein push, pull, or oscillate?
    • Lindemann CB, Hunt AJ. 2003. Does axonemal dynein push, pull, or oscillate? Cell Motil Cytoskeleton 56:237-244.
    • (2003) Cell Motil Cytoskeleton , vol.56 , pp. 237-244
    • Lindemann, C.B.1    Hunt, A.J.2
  • 31
    • 0031955547 scopus 로고    scopus 로고
    • Structural and molecular characterization of dynein in a gall-midge insect having motile sperm with only the outer arm
    • Lupetti P, Mencarelli C, Rosetto M, Heuser JE, Dallai R. 1998. Structural and molecular characterization of dynein in a gall-midge insect having motile sperm with only the outer arm. Cell Motil Cytoskeleton 39:303-317.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 303-317
    • Lupetti, P.1    Mencarelli, C.2    Rosetto, M.3    Heuser, J.E.4    Dallai, R.5
  • 32
    • 0036414847 scopus 로고    scopus 로고
    • Use of frozen-hydrated axonemes to assess imaging parameters and resolution limits in cryoelectron tomography
    • McEwen BF, Marko M, Hsieh CE, Mannella C. 2002. Use of frozen-hydrated axonemes to assess imaging parameters and resolution limits in cryoelectron tomography. J Struct Biol 138:47-57.
    • (2002) J Struct Biol , vol.138 , pp. 47-57
    • McEwen, B.F.1    Marko, M.2    Hsieh, C.E.3    Mannella, C.4
  • 33
    • 0037044862 scopus 로고    scopus 로고
    • Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography
    • Medalia O, Weber I, Frangakis AS, Nicastro D, Gerish G, Baumeister W. 2002. Macromolecular architecture in eukaryotic cells visualized by cryoelectron tomography. Science 298:1209-1213.
    • (2002) Science , vol.298 , pp. 1209-1213
    • Medalia, O.1    Weber, I.2    Frangakis, A.S.3    Nicastro, D.4    Gerish, G.5    Baumeister, W.6
  • 34
    • 0035195799 scopus 로고    scopus 로고
    • Molecular structure of dynein and motility of a giant sperm axoneme provided with only the outer dynein arm
    • Mencarelli C, Lupetti P, Rosetto M, Mercati D, Heuser JE, Dallai R. 2001. Molecular structure of dynein and motility of a giant sperm axoneme provided with only the outer dynein arm. Cell Motil Cytoskeleton 50:129-146.
    • (2001) Cell Motil Cytoskeleton , vol.50 , pp. 129-146
    • Mencarelli, C.1    Lupetti, P.2    Rosetto, M.3    Mercati, D.4    Heuser, J.E.5    Dallai, R.6
  • 35
    • 0028675883 scopus 로고
    • Cell and molecular biology of flagellar dyneins
    • Mitchell DR. 1994. Cell and molecular biology of flagellar dyneins. Int Rev Cytol 155:141-180.
    • (1994) Int Rev Cytol , vol.155 , pp. 141-180
    • Mitchell, D.R.1
  • 36
    • 0028568387 scopus 로고
    • Evaluation of high-resolution shadowing applied to freeze-fractured, deep-etched particles: 3D helical reconstruction of shadowed actin filaments
    • Morris EP, Katayama E, Squire JM. 1994. Evaluation of high-resolution shadowing applied to freeze-fractured, deep-etched particles: 3D helical reconstruction of shadowed actin filaments. J Struct Biol 113:47-55.
    • (1994) J Struct Biol , vol.113 , pp. 47-55
    • Morris, E.P.1    Katayama, E.2    Squire, J.M.3
  • 37
    • 0030754633 scopus 로고    scopus 로고
    • Functional interaction between Chlamydomonas outer arm dynein subunits: The γ subunit suppresses the ATPase activity of the αβ dimer
    • Nakamura K, Wilkerson CG, Witman GB. 1997. Functional interaction between Chlamydomonas outer arm dynein subunits: the γ subunit suppresses the ATPase activity of the αβ dimer. Cell Motil Cytoskeleton 37:338-345.
    • (1997) Cell Motil Cytoskeleton , vol.37 , pp. 338-345
    • Nakamura, K.1    Wilkerson, C.G.2    Witman, G.B.3
  • 38
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure-diverse function
    • Ogura T, Wilkinson AJ. 2001. AAA+ superfamily ATPases: common structure-diverse function. Genes Cells 6:575-597.
    • (2001) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 39
    • 0038159661 scopus 로고    scopus 로고
    • Three-dimensional organization of basal bodies from wild-type and 8-tubulin deletion strains of Chlamydomonas reinhardtii
    • O'Toole ET, Giddings TH, McIntosh JR, Dutcher SK. 2003. Three-dimensional organization of basal bodies from wild-type and 8-tubulin deletion strains of Chlamydomonas reinhardtii. Mol Biol Cell 14:2999-3012.
    • (2003) Mol Biol Cell , vol.14 , pp. 2999-3012
    • O'Toole, E.T.1    Giddings, T.H.2    McIntosh, J.R.3    Dutcher, S.K.4
  • 41
    • 0030027155 scopus 로고    scopus 로고
    • Axonemal dyneins: Assembly, organization, and regulation
    • Porter ME. 1996. Axonemal dyneins: assembly, organization, and regulation. Curr Opin Cell Biol 8:10-17.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 10-17
    • Porter, M.E.1
  • 42
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J. 1987. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J Microsc 146:113-136.
    • (1987) J Microsc , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 43
    • 0022401659 scopus 로고
    • The substructure of isolated and in situ outer dynein arms of sea urchin sperm flagella
    • Sale WS, Goodenough UW, Heuser JE. 1985. The substructure of isolated and in situ outer dynein arms of sea urchin sperm flagella. J Cell Biol 101:1400-1412.
    • (1985) J Cell Biol , vol.101 , pp. 1400-1412
    • Sale, W.S.1    Goodenough, U.W.2    Heuser, J.E.3
  • 44
    • 0032513004 scopus 로고    scopus 로고
    • Structural characterization of a dynein motor domain
    • Samsó M, Radermaker M, Frank J, Koonce MP. 1998. Structural characterization of a dynein motor domain. J Mol Biol 276:927-937.
    • (1998) J Mol Biol , vol.276 , pp. 927-937
    • Samsó, M.1    Radermaker, M.2    Frank, J.3    Koonce, M.P.4
  • 45
    • 0037333340 scopus 로고    scopus 로고
    • The next ice age: Cryo-electron tomography of intact cells
    • Steven AC, Aebi U. 2003. The next ice age: cryo-electron tomography of intact cells. Trends Cell Biol 13:107-110.
    • (2003) Trends Cell Biol , vol.13 , pp. 107-110
    • Steven, A.C.1    Aebi, U.2
  • 46
    • 3042548142 scopus 로고    scopus 로고
    • Three-dimensional electron microscopy at molecular resolution
    • Subramaniam S, Milne JLS. 2004. Three-dimensional electron microscopy at molecular resolution. Annu Rev Biophys Biomol Struct 33:141-155.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 141-155
    • Subramaniam, S.1    Milne, J.L.S.2
  • 47
    • 0036199035 scopus 로고    scopus 로고
    • The outer dynein arm-docking complex: Composition and characterization of a subunit (Odal) necessary for outer arm assembly
    • Takada S, Wilkerson CG, Wakabaiashi K, Kamiya R, Witman GB. 2002. The outer dynein arm-docking complex: composition and characterization of a subunit (Odal) necessary for outer arm assembly. Mol Biol Cell 13:1115-1129.
    • (2002) Mol Biol Cell , vol.13 , pp. 1115-1129
    • Takada, S.1    Wilkerson, C.G.2    Wakabaiashi, K.3    Kamiya, R.4    Witman, G.B.5
  • 48
    • 25144443009 scopus 로고
    • Tilting stage for biological applications
    • Frank J, editor. NY: Plenum
    • Turner JN, Valdrè U. 1992. Tilting stage for biological applications. In: Frank J, editor. Electron Tomography. NY: Plenum, p 167-196.
    • (1992) Electron Tomography , pp. 167-196
    • Turner, J.N.1    Valdrè, U.2
  • 49
    • 0024284804 scopus 로고
    • Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia
    • Vale RD, Toyoshima YY. 1988. Rotation and translocation of microtubules in vitro induced by dyneins from Tetrahymena cilia. Cell 52:459-469.
    • (1988) Cell , vol.52 , pp. 459-469
    • Vale, R.D.1    Toyoshima, Y.Y.2
  • 50
    • 0023090371 scopus 로고
    • Similarity measures between images
    • van Heel M. 1987. Similarity measures between images. Ultramicroscopy 21:95-100.
    • (1987) Ultramicroscopy , vol.21 , pp. 95-100
    • Van Heel, M.1
  • 52
    • 2542500559 scopus 로고    scopus 로고
    • Oda5p, a novel axonemal protein required for assembly of the outer dynein arm and an associated adenylate kinase
    • Wirschell M, Pazour G, Yoda A, Hirono M, Kamiya R, Witman GB. 2004. Oda5p, a novel axonemal protein required for assembly of the outer dynein arm and an associated adenylate kinase. Mol Biol Cell 15:2729-2741.
    • (2004) Mol Biol Cell , vol.15 , pp. 2729-2741
    • Wirschell, M.1    Pazour, G.2    Yoda, A.3    Hirono, M.4    Kamiya, R.5    Witman, G.B.6


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