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Volumn 378, Issue 5, 1997, Pages 363-372

Topography of ribosomes and initiation complexes from rat liver as revealed by atomic force microscopy

Author keywords

Atomic force microscopy; Eukaryotic initiation factor; Eukaryotic ribosome; Native 40S ribosomal subunit; Topography

Indexed keywords

INITIATION FACTOR 1; INITIATION FACTOR 2;

EID: 0030997878     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.5.363     Document Type: Article
Times cited : (10)

References (60)
  • 1
    • 0023053025 scopus 로고
    • Three-dimensional structure of the regular surface layer (HPI Layer) of Deinococcus radio-durans
    • Baumeister, W., Barth, M., Hegerl, R., Guckenberger, R., Hahn, M., and Saxton, W.O. (1986). Three-dimensional structure of the regular surface layer (HPI Layer) of Deinococcus radio-durans. J. MoIl Biol. 187, 241-254.
    • (1986) J. Mol. Biol. , vol.187 , pp. 241-254
    • Baumeister, W.1    Barth, M.2    Hegerl, R.3    Guckenberger, R.4    Hahn, M.5    Saxton, W.O.6
  • 2
    • 0018401487 scopus 로고
    • Protein synthesis initiation factors from rabbit recutiloytes: Purification, characterization and radiochemical labelling
    • Benne, R., Brown, L.M., and Hershey, J.W. (1979). Protein synthesis initiation factors from rabbit recutiloytes: Purification, characterization and radiochemical labelling. Methods Enzymol. 60, 15-35.
    • (1979) Methods Enzymol. , vol.60 , pp. 15-35
    • Benne, R.1    Brown, L.M.2    Hershey, J.W.3
  • 3
    • 0018095166 scopus 로고
    • The mechanism of action of protein synthesis initiation factor from rabbit reticulocytes
    • Benne, R., and Hershey, J.W. (1978). The mechanism of action of protein synthesis initiation factor from rabbit reticulocytes. J. Biol. Chem. 253, 3078-3087.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3078-3087
    • Benne, R.1    Hershey, J.W.2
  • 4
    • 0012618901 scopus 로고
    • Atomic force microscope
    • Bining, G., and Quate, C.F. (1986). Atomic force microscope. Phys. Rev. Lett. 56, 930-933.
    • (1986) Phys. Rev. Lett. , vol.56 , pp. 930-933
    • Bining, G.1    Quate, C.F.2
  • 6
    • 0026043416 scopus 로고
    • Eucaryotic initiation factor elF-2 and elF-3 interaction, structure and location in ribosomal initiation complex
    • Bommer, U.A., Lutsch, G., Stahl, J., and Bielka, H. (1991). Eucaryotic initiation factor elF-2 and elF-3 interaction, structure and location in ribosomal initiation complex. Biochimie 73, 1007-1019.
    • (1991) Biochimie , vol.73 , pp. 1007-1019
    • Bommer, U.A.1    Lutsch, G.2    Stahl, J.3    Bielka, H.4
  • 7
    • 0024278336 scopus 로고
    • Position of S2, S13, S16, S17, S19 in the 30S ribosomal subunit of Escherichia coli
    • Capel, M.S., Kjeldaard, M., Engelman, D.M., and Moore, P.B. (1988a). Position of S2, S13, S16, S17, S19 in the 30S ribosomal subunit of Escherichia coli. J. Mol. Biol. 200, 65-87.
    • (1988) J. Mol. Biol. , vol.200 , pp. 65-87
    • Capel, M.S.1    Kjeldaard, M.2    Engelman, D.M.3    Moore, P.B.4
  • 8
    • 0024271791 scopus 로고
    • Neutron-scattering topography of proteins of the small ribosomal subunit
    • Capel, M.S., and Ramakrishnan, V. (1988b). Neutron-scattering topography of proteins of the small ribosomal subunit. Methods Enzymol. 64, 117-131.
    • (1988) Methods Enzymol. , vol.64 , pp. 117-131
    • Capel, M.S.1    Ramakrishnan, V.2
  • 10
    • 0017881505 scopus 로고
    • Localization of eucaryotic initiation factor on native small ribosomal subunits
    • Emanuilov, I., Sabatini, D., Lake, J., and Freienstein, C. (1978). Localization of eucaryotic initiation factor on native small ribosomal subunits. Proc. Natl. Acad. Sci. USA 75, 1389-1393.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1389-1393
    • Emanuilov, I.1    Sabatini, D.2    Lake, J.3    Freienstein, C.4
  • 11
    • 0025855016 scopus 로고
    • Biological applications of scanning probe microscope
    • Engel, A. (1991). Biological applications of scanning probe microscope. Ann. Rev. Biophys. Biomol. Chem. 20, 79-108.
    • (1991) Ann. Rev. Biophys. Biomol. Chem. , vol.20 , pp. 79-108
    • Engel, A.1
  • 12
    • 0028309424 scopus 로고
    • Adhesion force between individual ligand-receptor
    • Florin, E.L., Moy, V.T., and Gaub, H.E. (1994). Adhesion force between individual ligand-receptor. Science 264, 415-417.
    • (1994) Science , vol.264 , pp. 415-417
    • Florin, E.L.1    Moy, V.T.2    Gaub, H.E.3
  • 13
    • 0026045381 scopus 로고
    • Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: The distribution of ribosomal RNA
    • Frank, J., Penczek, P., Grassucci, R., and Srivastava, S. (1991). Three-dimensional reconstruction of the 70S Escherichia coli ribosome in ice: The distribution of ribosomal RNA. J. Cell Biol. 115, 597-605.
    • (1991) J. Cell Biol. , vol.115 , pp. 597-605
    • Frank, J.1    Penczek, P.2    Grassucci, R.3    Srivastava, S.4
  • 14
    • 0024244421 scopus 로고
    • Studying ribosome structure by electron microscopy and computer image processing
    • Frank, J., Radermacher, T., Wagenech, T., and Verschoop, A. (1988). Studying ribosome structure by electron microscopy and computer image processing. Methods Enzymol. 164, 1-234.
    • (1988) Methods Enzymol. , vol.164 , pp. 1-234
    • Frank, J.1    Radermacher, T.2    Wagenech, T.3    Verschoop, A.4
  • 15
    • 0000234155 scopus 로고
    • Morphologies of eubacterial and eucaryotic ribosomes as determined by three-dimension electron microscopy
    • W.E. Hill et al., eds (Washington, D.C.: American Society of Microbiology)
    • Frank, J., Verschorr, A., Radermacher, M., and Wagenknecht, T. (1990). Morphologies of eubacterial and eucaryotic ribosomes as determined by three-dimension electron microscopy. In: Ribosome Structure, Function and Evolution. W.E. Hill et al., eds (Washington, D.C.: American Society of Microbiology), pp. 107-113.
    • (1990) Ribosome Structure, Function and Evolution , pp. 107-113
    • Frank, J.1    Verschorr, A.2    Radermacher, M.3    Wagenknecht, T.4
  • 17
    • 0005432472 scopus 로고
    • Use of eucaryotic native ribosomal subunits for the translation of globin messenger RNA
    • Freienstein, C., and Bloble, G. (1974). Use of eucaryotic native ribosomal subunits for the translation of globin messenger RNA. Proc. Natl. Acad. Sci. USA 71, 3435-3439.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3435-3439
    • Freienstein, C.1    Bloble, G.2
  • 18
    • 0028364295 scopus 로고
    • Bimolecular imaging with the atomic force microscope
    • Hansma, H.G. (1994). Bimolecular imaging with the atomic force microscope. Annu. Rev. Biophys. Biomol. Struct. 23, 115-139.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 115-139
    • Hansma, H.G.1
  • 20
    • 0026784795 scopus 로고
    • Actin filament dynamics in living glial cells imaged by atomic force microscopy
    • Henderson, E., Haydon, P.G., and Sakaguchi, K. (1992). Actin filament dynamics in living glial cells imaged by atomic force microscopy. Science 257, 1994-1946.
    • (1992) Science , vol.257 , pp. 1994-11946
    • Henderson, E.1    Haydon, P.G.2    Sakaguchi, K.3
  • 21
    • 0015797119 scopus 로고
    • The ribosome cycle in mammalian protein synthesis
    • Hirsch, C., Cox, M.A., Venrooil, W., and Henshaw, E. (1973). The ribosome cycle in mammalian protein synthesis. J. Biol. Chem. 248, 4377-4385.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4377-4385
    • Hirsch, C.1    Cox, M.A.2    Venrooil, W.3    Henshaw, E.4
  • 22
    • 0343299035 scopus 로고
    • Studies on native ribosomal subunit from rat livers
    • Huang, K.H., Fairclough, R.H., and Cantor, C.R. (1975). Studies on native ribosomal subunit from rat livers. J. Mol. Biol. 145, 443-451.
    • (1975) J. Mol. Biol. , vol.145 , pp. 443-451
    • Huang, K.H.1    Fairclough, R.H.2    Cantor, C.R.3
  • 23
    • 0018882777 scopus 로고
    • Evidence for a lower molecular weight ribosomal dissociation factor
    • Jones, R., Sandnik, L., Thompson, H., and Modave, K. (1980). Evidence for a lower molecular weight ribosomal dissociation factor. Arch. Biochem. Biophys. 199, 277-285.
    • (1980) Arch. Biochem. Biophys. , vol.199 , pp. 277-285
    • Jones, R.1    Sandnik, L.2    Thompson, H.3    Modave, K.4
  • 24
    • 0343290977 scopus 로고
    • Specific binding of eucaryotic initiation factor 2 to satellite tobacco necrosis virus RNA at 5′-terminal sequence comprising the ribosome binding site
    • Kaempfer, R., Emmelo, J., and Fiers, W. (1981). Specific binding of eucaryotic initiation factor 2 to satellite tobacco necrosis virus RNA at 5′-terminal sequence comprising the ribosome binding site. Proc. Natl. Acad. Sci. USA 78, 1542-1548.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1542-1548
    • Kaempfer, R.1    Emmelo, J.2    Fiers, W.3
  • 25
    • 0026206391 scopus 로고
    • Reconstruction of SFM and AFM image by size tip
    • Keller, D. (1991). Reconstruction of SFM and AFM image by size tip. Surface Sci. 253, 353-364.
    • (1991) Surface Sci. , vol.253 , pp. 353-364
    • Keller, D.1
  • 26
    • 0021093443 scopus 로고
    • Cross-link between ribosomal protein of 30S subunit in 70S tight couples and in 30S subunits
    • Lambert, J.M., Borleau, G., Cover, J.A., and Traut, R.R. (1983). Cross-link between ribosomal protein of 30S subunit in 70S tight couples and in 30S subunits. Biochemistry 22, 3913-3920.
    • (1983) Biochemistry , vol.22 , pp. 3913-3920
    • Lambert, J.M.1    Borleau, G.2    Cover, J.A.3    Traut, R.R.4
  • 27
    • 0022704950 scopus 로고
    • Structure and location of initiation factor elF-3 within native small subunits for eucaryotes
    • Lutsch, G., Benndrof, R., Westermann, P., Bommer, U.A., and Bielka, H. (1986). Structure and location of initiation factor elF-3 within native small subunits for eucaryotes. Eur. J. Cell Biol. 40, 257-265.
    • (1986) Eur. J. Cell Biol. , vol.40 , pp. 257265
    • Lutsch, G.1    Benndrof, R.2    Westermann, P.3    Bommer, U.A.4    Bielka, H.5
  • 28
    • 0021158357 scopus 로고
    • Structure of ribosomal RNA
    • Noller, H.F. (1984). Structure of ribosomal RNA. Annu. Rev. Biochem. 53, 119-162.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 119-162
    • Noller, H.F.1
  • 29
  • 30
    • 0020493817 scopus 로고
    • Purification of protein synthesis initiation factor elF-3 from rat livers microsomes by affinity chromatography on rRNA-cellulose
    • Nygard, O., and Westermann, P. (1982). Purification of protein synthesis initiation factor elF-3 from rat livers microsomes by affinity chromatography on rRNA-cellulose. Biochem. Biophys. Acta. 697, 263-269.
    • (1982) Biochem. Biophys. Acta. , vol.697 , pp. 263-269
    • Nygard, O.1    Westermann, P.2
  • 32
    • 0024297795 scopus 로고
    • Structure of β-subunit of translation Factor-2 elF-2
    • Pathak, V.K., Nielsen, P.J. Trachsel, H., and Hersey, J.W.B. (1988). Structure of β-subunit of translation Factor-2 elF-2. Cell 54, 633-639.
    • (1988) Cell , vol.54 , pp. 633-639
    • Pathak, V.K.1    Nielsen, P.J.2    Trachsel, H.3    Hersey, J.W.B.4
  • 33
    • 0018786531 scopus 로고
    • Binding and relase of radiolable eucaryotic initiation factor-2 and 3, during 80 initiation complex formation
    • Peterson, D.T., Merrik, W.C., and Safer, B. (1979). Binding and relase of radiolable eucaryotic initiation factor-2 and 3, during 80 initiation complex formation. J. Biol. Chem. 254, 2509-2518.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2509-2518
    • Peterson, D.T.1    Merrik, W.C.2    Safer, B.3
  • 34
    • 0342429418 scopus 로고
    • mRNA and mRNP
    • F. Trachsel, ed. (London: CRC Press)
    • Rhoads, R. (1991). mRNA and mRNP. In: Translation in Eucaryotes. F. Trachsel, ed. (London: CRC Press) pp. 111-148.
    • (1991) Translation in Eucaryotes , pp. 111-148
    • Rhoads, R.1
  • 36
    • 0017701040 scopus 로고
    • Initiation of mammalian protein synthesis
    • Schreier, M., Erni, H., and Steachelin, H. (1977). Initiation of mammalian protein synthesis. J. Mol. Biol. 116, 727-735.
    • (1977) J. Mol. Biol. , vol.116 , pp. 727-735
    • Schreier, M.1    Erni, H.2    Steachelin, H.3
  • 37
    • 0343299016 scopus 로고
    • Fractionation and partial characterization of protein synthesis of wheat germ
    • Seal, S., Schmidt, A., and Marcus, A. (1983). Fractionation and partial characterization of protein synthesis of wheat germ. J. Biol. Chem. 258, 716-727.
    • (1983) J. Biol. Chem. , vol.258 , pp. 716-727
    • Seal, S.1    Schmidt, A.2    Marcus, A.3
  • 38
    • 0002477677 scopus 로고
    • Isolation and analysis of ribosomes from prokaryotes, eukaryotes and organelles
    • G. Spedding, ed. (New York: IRL Press)
    • Spedding, G. (1990). Isolation and analysis of ribosomes from prokaryotes, eukaryotes and organelles. In: Ribosomes and Protein Synthesis, Practical Approach. G. Spedding, ed. (New York: IRL Press), pp. 1-29.
    • (1990) Ribosomes and Protein Synthesis, Practical Approach , pp. 1-29
    • Spedding, G.1
  • 40
    • 0000866854 scopus 로고
    • Isolation of mammalian ribosome subunits active in polypeptide synthesis
    • Staechlin, T., and Falvey, A. (1971). Isolation of mammalian ribosome subunits active in polypeptide synthesis. Methods Enzymol. 22, 433-446.
    • (1971) Methods Enzymol. , vol.22 , pp. 433-446
    • Staechlin, T.1    Falvey, A.2
  • 41
    • 0002440518 scopus 로고
    • Immuno electron microscopy on Escherichia coli ribosomes
    • B. Hardesty and G. Karmer, eds., (New York: Springer-Verlag)
    • Stöffler, G., and Stöffler, M. (1986). Immuno electron microscopy on Escherichia coli ribosomes. In: Structure, Function and Genetics of Ribosomes. B. Hardesty and G. Karmer, eds., (New York: Springer-Verlag), pp. 28-46.
    • (1986) Structure, Function and Genetics of Ribosomes , pp. 28-46
    • Stöffler, G.1    Stöffler, M.2
  • 42
    • 0016273550 scopus 로고
    • Initiation factor activity associated with free 40S subunit from rat liver and rabbit reticuloytes
    • Sundkvist, I., Mckeehan, W., Schreier, M., and Staechlin, T. (1974). Initiation factor activity associated with free 40S subunit from rat liver and rabbit reticuloytes. J. Biol. Chem. 249, 6512-6515.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6512-6515
    • Sundkvist, I.1    Mckeehan, W.2    Schreier, M.3    Staechlin, T.4
  • 43
    • 0016622605 scopus 로고
    • Structure and function of free 40S ribosomal subunits characterization of initiation factors
    • Sundkvist, I., and Staechlin, T. (1975). Structure and function of free 40S ribosomal subunits characterization of initiation factors. J. Mol. Biol. 99, 401-418.
    • (1975) J. Mol. Biol. , vol.99 , pp. 401-418
    • Sundkvist, I.1    Staechlin, T.2
  • 44
    • 0019643971 scopus 로고
    • Ribosomal protein cross-linked to natural mRNA by UV irradiation of rat liver polysomes
    • Takahashi, Y., and Ogat, K. (1981). Ribosomal protein cross-linked to natural mRNA by UV irradiation of rat liver polysomes. J. Biochem. 90, 1549-1552.
    • (1981) J. Biochem. , vol.90 , pp. 1549-1552
    • Takahashi, Y.1    Ogat, K.2
  • 45
    • 0021783435 scopus 로고
    • Comparative electron microscopic studies on single biomolecules negatively stained and freeze-dried metal-shadowed
    • Tesche, B., and Schmiady, H. (1985). Comparative electron microscopic studies on single biomolecules negatively stained and freeze-dried metal-shadowed. Ultramicroscopy 16, 423-435.
    • (1985) Ultramicroscopy , vol.16 , pp. 423-435
    • Tesche, B.1    Schmiady, H.2
  • 46
    • 0018883323 scopus 로고
    • The mechanism of actin of eucaryotic initiation factor 4C in protein synthesis
    • Thomas, A., Goumans, H., Voorma, H.O., and Benne, R. (1980). The mechanism of actin of eucaryotic initiation factor 4C in protein synthesis. Eur. J. Biochem. 107, 39-42.
    • (1980) Eur. J. Biochem. , vol.107 , pp. 39-42
    • Thomas, A.1    Goumans, H.2    Voorma, H.O.3    Benne, R.4
  • 50
    • 0343299012 scopus 로고
    • Functional site determination in three dimension on eucaryotic and eubacterial ribosomes
    • K.H. Nierhaus et al., eds., (New York: Plenum Press)
    • Verschoor, A., Srivastava, S., Radermacher, M., Frank, J., Traut, R.R., Stöffler-Meilicker, M., and Glitz, D. (1993). Functional site determination in three dimension on eucaryotic and eubacterial ribosomes. In: The Translational Apparatus. K.H. Nierhaus et al., eds., (New York: Plenum Press), pp. 411-420.
    • (1993) The Translational Apparatus , pp. 411-420
    • Verschoor, A.1    Srivastava, S.2    Radermacher, M.3    Frank, J.4    Traut, R.R.5    Stöffler-Meilicker, M.6    Glitz, D.7
  • 51
    • 0342864016 scopus 로고
    • Cross-linking of initiation factor elF-2 to proteins of the small subunit of rat liver ribosomes
    • Westermann, P., Heumann, W., Bommer, U.A., Bielka, H., Nygard, O., and Hulti, T. (1979). Cross-linking of initiation factor elF-2 to proteins of the small subunit of rat liver ribosomes. FEBS Lett. 9, 2387-2396.
    • (1979) FEBS Lett. , vol.9 , pp. 2387-2396
    • Westermann, P.1    Heumann, W.2    Bommer, U.A.3    Bielka, H.4    Nygard, O.5    Hulti, T.6
  • 53
    • 0021760787 scopus 로고
    • Cross-linking of mRNA to initiation factor of elF-3, 24 kDa cap binding protein and ribosomal protein S1, S3/3a and S11 within 48S pre-initiation complex
    • Westermann, P., and Nygard, O. (1984). Cross-linking of mRNA to initiation factor of elF-3, 24 kDa cap binding protein and ribosomal protein S1, S3/3a and S11 within 48S pre-initiation complex. Nucleic. Acids Res. 12, 8887-8897.
    • (1984) Nucleic. Acids Res. , vol.12 , pp. 8887-8897
    • Westermann, P.1    Nygard, O.2
  • 54
    • 0021660568 scopus 로고
    • The effects of air-drying and freeze on the structure of a regular protein layer
    • Wildhaber, I., Gross, H., Engel, A., and Baumeister, W. (1985). The effects of air-drying and freeze on the structure of a regular protein layer. Ultramicroscopy 16, 411-422.
    • (1985) Ultramicroscopy , vol.16 , pp. 411-422
    • Wildhaber, I.1    Gross, H.2    Engel, A.3    Baumeister, W.4
  • 55
    • 0002344009 scopus 로고
    • A model of the tRNA binding sites on the Escherichia coli ribosome
    • K.H. Nierhaus et al., eds., (New York: Plenum Press)
    • Wower, J., Lee, A.S., Rosen, K.V., Hixson, S.S., and Zimmermann, R.A. (1993). A model of the tRNA binding sites on the Escherichia coli ribosome. In: The Translational Apparatus. K.H. Nierhaus et al., eds., (New York: Plenum Press), pp. 455-463.
    • (1993) The Translational Apparatus , pp. 455-463
    • Wower, J.1    Lee, A.S.2    Rosen, K.V.3    Hixson, S.S.4    Zimmermann, R.A.5
  • 56
    • 0027406608 scopus 로고
    • New approach for atomic force microscopy of membrane proteins
    • Yang, J., Lukas, K., Tamm, M., Tillact, T.W., and Shao, Z.F. (1993). New approach for atomic force microscopy of membrane proteins. J. Mol. Biol. 229, 286-290.
    • (1993) J. Mol. Biol. , vol.229 , pp. 286-290
    • Yang, J.1    Lukas, K.2    Tamm, M.3    Tillact, T.W.4    Shao, Z.F.5
  • 58
    • 0023212383 scopus 로고
    • A tunnel in the large ribosomal subunit reveal by the three-dimensional image reconstruction
    • Yonath, A., Leonard, K.R., and Wittmans, H.G. (1987a). A tunnel in the large ribosomal subunit reveal by the three-dimensional image reconstruction. Science 236, 813-816.
    • (1987) Science , vol.236 , pp. 813-816
    • Yonath, A.1    Leonard, K.R.2    Wittmans, H.G.3
  • 59
    • 0023518995 scopus 로고
    • Approaches to the determination of the three-dimensional architecture of ribosomal particles
    • Yonath, A., Leonard, K.R., and Wittmans, H.G. (1987b). Approaches to the determination of the three-dimensional architecture of ribosomal particles. Cold Spring Harbour Symp. Quant. Biol. 52, 729-741.
    • (1987) Cold Spring Harbour Symp. Quant. Biol. , vol.52 , pp. 729-741
    • Yonath, A.1    Leonard, K.R.2    Wittmans, H.G.3


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