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Volumn 127, Issue 2, 2000, Pages 221-231

Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation

Author keywords

80S ribosomes; ATPase; GTPase; Peptide elongation; Polysomes

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINOACYL TRANSFER RNA; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 2; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; RIBOSOME RNA;

EID: 0034052296     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022598     Document Type: Article
Times cited : (3)

References (41)
  • 1
    • 0021891865 scopus 로고
    • Eukaryotic protein synthesis
    • Moldave, K. (1985) Eukaryotic protein synthesis. Annu. Rev. Biochem. 54, 1109-1149
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1109-1149
    • Moldave, K.1
  • 2
    • 0014288703 scopus 로고
    • Comparison of amino acid polymerization factors isolated from rat liver and rabbit reticulocyte
    • Felcetti, L. and Lipmann, F. (1968) Comparison of amino acid polymerization factors isolated from rat liver and rabbit reticulocyte. Arch. Biochem. Biophys. 125, 548-557
    • (1968) Arch. Biochem. Biophys. , vol.125 , pp. 548-557
    • Felcetti, L.1    Lipmann, F.2
  • 3
    • 0016811614 scopus 로고
    • GTP degradation to guanine catalyzed by ribosomal subunits and microsomal-wash factors
    • Grummt, F. and Speckbacher, M. (1975) GTP degradation to guanine catalyzed by ribosomal subunits and microsomal-wash factors. Eur. J. Biochem. 57, 579-585
    • (1975) Eur. J. Biochem. , vol.57 , pp. 579-585
    • Grummt, F.1    Speckbacher, M.2
  • 5
    • 0027944283 scopus 로고
    • Comparative analysis of ribosome-associated adenosine-triphosphatase (ATPase) from pig liver and ATPase of elongation factor 3 from Saccharomyces cerevisiae
    • Kovalchuke, O. and Chakraburtty, K. (1994) Comparative analysis of ribosome-associated adenosine-triphosphatase (ATPase) from pig liver and ATPase of elongation factor 3 from Saccharomyces cerevisiae. Eur. J. Biochem. 226, 133-140
    • (1994) Eur. J. Biochem. , vol.226 , pp. 133-140
    • Kovalchuke, O.1    Chakraburtty, K.2
  • 6
    • 0031912054 scopus 로고    scopus 로고
    • ATPase associated with ribosomal 30S-5SRNP particles and 40S subunits of rat liver
    • Ogata, K., Ohno, R., Terao, K., Iwasaki, K., and Endo, Y. (1998) ATPase associated with ribosomal 30S-5SRNP particles and 40S subunits of rat liver. J. Biochem. 123, 294-304
    • (1998) J. Biochem. , vol.123 , pp. 294-304
    • Ogata, K.1    Ohno, R.2    Terao, K.3    Iwasaki, K.4    Endo, Y.5
  • 7
    • 0020210289 scopus 로고
    • Interaction of 5SRNA-L5 protein complex with 40S subunits in rat liver ribosomes
    • Terao, K., Uchiumi, T., and Ogata, K. (1982) Interaction of 5SRNA-L5 protein complex with 40S subunits in rat liver ribosomes. J. Biochem. 92, 1663-1666
    • (1982) J. Biochem. , vol.92 , pp. 1663-1666
    • Terao, K.1    Uchiumi, T.2    Ogata, K.3
  • 8
    • 0018338343 scopus 로고
    • Analytical methods for ribosomal protein of rat liver 40S and 60S by "three-dimensional acrylamide gel electrophoresis"
    • (Moldav, K. and Grossman, L., eds.) Academic Press, New York
    • Ogata, K. and Terao, K. (1979) Analytical methods for ribosomal protein of rat liver 40S and 60S by "three-dimensional acrylamide gel electrophoresis" in Methods in Enzymology (Moldav, K. and Grossman, L., eds.) Vol. 59, pp. 502-515, Academic Press, New York
    • (1979) Methods in Enzymology , vol.59 , pp. 502-515
    • Ogata, K.1    Terao, K.2
  • 10
    • 0014945408 scopus 로고
    • Structure and function of mammalian ribosomes. I. Isolation and characterization of active liver ribosomal subunits
    • Falvey, A.K. and Staehelin, T. (1970) Structure and function of mammalian ribosomes. I. Isolation and characterization of active liver ribosomal subunits. J. Mol. Biol. 53, 1-19
    • (1970) J. Mol. Biol. , vol.53 , pp. 1-19
    • Falvey, A.K.1    Staehelin, T.2
  • 11
    • 0017231488 scopus 로고
    • Interaction of the low molecular weight form of elongation factor 1 with guanine nucleotide and aminoacyl tRNA
    • Nagata, S., Iwasaki, K., and Kagiro, Y. (1976) Interaction of the low molecular weight form of elongation factor 1 with guanine nucleotide and aminoacyl tRNA. Arch.Biochem.Biophys. 172, 168-177
    • (1976) Arch.biochem.biophys. , vol.172 , pp. 168-177
    • Nagata, S.1    Iwasaki, K.2    Kagiro, Y.3
  • 12
    • 0017695859 scopus 로고
    • Purification and properties of polypeptide chain elongation factor-1α from pig liver
    • Nagata, S., Iwasaki, K., and Kajiro, Y. (1977) Purification and properties of polypeptide chain elongation factor-1α from pig liver. J. Biochem. 82, 1633-1646
    • (1977) J. Biochem. , vol.82 , pp. 1633-1646
    • Nagata, S.1    Iwasaki, K.2    Kajiro, Y.3
  • 13
    • 0017688569 scopus 로고
    • Purification and properties of polypeptide chain elongation factor-1βγ from pig liver
    • Motoyoshi, K., Iwasaki, K., and Kajiro, Y. (1977) Purification and properties of polypeptide chain elongation factor-1βγ from pig liver. J. Biochem. 82, 145-155
    • (1977) J. Biochem. , vol.82 , pp. 145-155
    • Motoyoshi, K.1    Iwasaki, K.2    Kajiro, Y.3
  • 14
    • 0016186659 scopus 로고
    • Studies on polypeptide elongation factor 2 from pig liver. I. Purification and properties
    • Mizumoto, K., Iwasaki, K., Tanaka, M., and Kaziro, Y. (1974) Studies on polypeptide elongation factor 2 from pig liver I. Purification and properties. J. Biochem. 75, 1047-1056
    • (1974) J. Biochem. , vol.75 , pp. 1047-1056
    • Mizumoto, K.1    Iwasaki, K.2    Tanaka, M.3    Kaziro, Y.4
  • 15
  • 16
    • 0022916176 scopus 로고
    • Characterization of the elongation factors from calf brain. 3. Properties of GTPase activity of EF-1α and mode of action of kirromycin
    • Crechet, J.-B. and Parmeggiani, A. (1986) Characterization of the elongation factors from calf brain. 3. Properties of GTPase activity of EF-1α and mode of action of kirromycin. Eur. J. Biochem. 161, 655-660
    • (1986) Eur. J. Biochem. , vol.161 , pp. 655-660
    • Crechet, J.-B.1    Parmeggiani, A.2
  • 18
    • 0030845290 scopus 로고    scopus 로고
    • Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotes
    • El'skaya, A.V., Ovcharenko, G.V., Palchevskii, S.S., Petrushenko, Z.M., Triana-Alonso, F.J., and Nierhause, K.H. (1997) Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotes. Biochemistry 36, 10492-10497
    • (1997) Biochemistry , vol.36 , pp. 10492-10497
    • El'skaya, A.V.1    Ovcharenko, G.V.2    Palchevskii, S.S.3    Petrushenko, Z.M.4    Triana-Alonso, F.J.5    Nierhause, K.H.6
  • 20
    • 0015239188 scopus 로고
    • Amino-transferase II from rat liver. I. Purification and enzymatic properties
    • Raeburn, S., Collins, J.F., Mo Moon, H., and Maxwell, E.S. (1971) Amino-transferase II from rat liver. I. Purification and enzymatic properties. J. Biol. Chem. 246, 1041-1048
    • (1971) J. Biol. Chem. , vol.246 , pp. 1041-1048
    • Raeburn, S.1    Collins, J.F.2    Mo Moon, H.3    Maxwell, E.S.4
  • 21
    • 0021111843 scopus 로고
    • Binding of eucariotic elongation factor Tu to nucleic acids
    • Slobin, L.J. (1983) Binding of eucariotic elongation factor Tu to nucleic acids. J. Biol. Chem. 258, 4895-4900
    • (1983) J. Biol. Chem. , vol.258 , pp. 4895-4900
    • Slobin, L.J.1
  • 22
    • 78651145301 scopus 로고
    • Characterization of a ribosome-linked guanosine triphosphase in Escherichia coli extracts
    • Conway, T.W. and Lipmann, F. (1974) Characterization of a ribosome-linked guanosine triphosphase in Escherichia coli extracts. Proc. Natl. Acad. Sci. USA 52, 1462-1469
    • (1974) Proc. Natl. Acad. Sci. USA , vol.52 , pp. 1462-1469
    • Conway, T.W.1    Lipmann, F.2
  • 23
    • 0024147065 scopus 로고
    • Mechanism of ribosome-mediated translation in protein synthesis
    • Burma, D.P. (1988) Mechanism of ribosome-mediated translation in protein synthesis. Indian J. Biochem. Biophys. 25, 467-471
    • (1988) Indian J. Biochem. Biophys. , vol.25 , pp. 467-471
    • Burma, D.P.1
  • 24
    • 0028227364 scopus 로고
    • Structural dynamics of translating ribosomes; 16S ribosomal RNA bases that may move twice during translation
    • Laughren, M. (1994) Structural dynamics of translating ribosomes; 16S ribosomal RNA bases that may move twice during translation. Mol. Microbiol. 11, 999-1007
    • (1994) Mol. Microbiol. , vol.11 , pp. 999-1007
    • Laughren, M.1
  • 25
    • 0029810022 scopus 로고    scopus 로고
    • Sites of ribosomal RNAs involved in the subunit association of tight and loose couple ribosomes
    • Agrawal, R.K. and Burma, D.P. (1996) Sites of ribosomal RNAs involved in the subunit association of tight and loose couple ribosomes. J. Biol. Chem. 271, 21285-21291
    • (1996) J. Biol. Chem. , vol.271 , pp. 21285-21291
    • Agrawal, R.K.1    Burma, D.P.2
  • 26
    • 0032484130 scopus 로고    scopus 로고
    • Protection patterns of tRNAs do not change during ribosomal translation
    • Dabrowski, M., Spahn, M.T., Schäfer, M.A., Patzke, S., and Nierhause, K.H. (1998) Protection patterns of tRNAs do not change during ribosomal translation. J. Biol. Chem. 273, 32793-32800
    • (1998) J. Biol. Chem. , vol.273 , pp. 32793-32800
    • Dabrowski, M.1    Spahn, M.T.2    Schäfer, M.A.3    Patzke, S.4    Nierhause, K.H.5
  • 27
    • 0033548692 scopus 로고    scopus 로고
    • Structure and structural variations of the Escherichia coli 30s ribosomal subunit as revealed by three-dimensional cryo-electron microscopy
    • Gabashvili, I.S., Agrawal, R.K., Grassucci, R., and Frank, J. (1999) Structure and structural variations of the Escherichia coli 30S ribosomal subunit as revealed by three-dimensional cryo-electron microscopy. J. Mol. Biol. 286, 1285-1291
    • (1999) J. Mol. Biol. , vol.286 , pp. 1285-1291
    • Gabashvili, I.S.1    Agrawal, R.K.2    Grassucci, R.3    Frank, J.4
  • 28
    • 0023038717 scopus 로고
    • Cross-linking study on localization of the binding site for elongation factor 1α on rat liver ribosomes
    • Uchiumi, T. and Ogata, K. (1986) Cross-linking study on localization of the binding site for elongation factor 1α on rat liver ribosomes. J. Biol. Chem. 261, 9668-9671
    • (1986) J. Biol. Chem. , vol.261 , pp. 9668-9671
    • Uchiumi, T.1    Ogata, K.2
  • 29
    • 0022701927 scopus 로고
    • Cross-linking of elongation factor 2 to rat liver ribosomal proteins by 2-iminothiolane
    • Uchiumi, T., Kikuchi, M., Terao, K., Iwasaki, K., and Ogata, K. (1986) Cross-linking of elongation factor 2 to rat liver ribosomal proteins by 2-iminothiolane. Eur. J. Biochem. 156, 37-48
    • (1986) Eur. J. Biochem. , vol.156 , pp. 37-48
    • Uchiumi, T.1    Kikuchi, M.2    Terao, K.3    Iwasaki, K.4    Ogata, K.5
  • 30
    • 0023154926 scopus 로고
    • The ribosomal binding site for eukaryotic elongation factor EF-2 contains 5S ribosomal RNA
    • Nygård, O. and Nilsson, L. (1987) The ribosomal binding site for eukaryotic elongation factor EF-2 contains 5S ribosomal RNA. Biochim. Biophys. Acta 908, 46-53
    • (1987) Biochim. Biophys. Acta , vol.908 , pp. 46-53
    • Nygård, O.1    Nilsson, L.2
  • 31
    • 0023648543 scopus 로고
    • Characterization of ribosomal binding sites for eukaryotic elongation factor 2 by chemical cross-linking
    • Nygard, O. and Nilsson, L. (1987) Characterization of ribosomal binding sites for eukaryotic elongation factor 2 by chemical cross-linking. Biochim. Biophys. Acta 910, 245-253
    • (1987) Biochim. Biophys. Acta , vol.910 , pp. 245-253
    • Nygard, O.1    Nilsson, L.2
  • 32
    • 0025291205 scopus 로고
    • Translational dynamics: Interaction between the translational factors, tRNA, ribosomes during eukaryotic protein synthesis
    • Nygård, O. and Nilsson, L. (1990) Translational dynamics: Interaction between the translational factors, tRNA, ribosomes during eukaryotic protein synthesis. Eur. J. Biochem. 191, 1-17
    • (1990) Eur. J. Biochem. , vol.191 , pp. 1-17
    • Nygård, O.1    Nilsson, L.2
  • 33
    • 0020479406 scopus 로고
    • The site of action of α-sarcin on eucaryotic ribosomes. The sequence of the α-sarcin cleavage site in 28S ribosomal ribonucleic acid
    • Endo, Y. and Wool, I.G. (1982) The site of action of α-sarcin on eucaryotic ribosomes. The sequence of the α-sarcin cleavage site in 28S ribosomal ribonucleic acid. J. Biol. Chem. 257, 9054-9060
    • (1982) J. Biol. Chem. , vol.257 , pp. 9054-9060
    • Endo, Y.1    Wool, I.G.2
  • 34
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eucaryotic ribosomes. The site and characteristics of the modification in 28S ribosomal RNA caused by the toxins
    • Endo, Y., Mitsui, K., Motizuki, M., and Tsurugi, K. (1987) The mechanism of action of ricin and related toxic lectins on eucaryotic ribosomes. The site and characteristics of the modification in 28S ribosomal RNA caused by the toxins. J. Biol. Chem. 262, 5908-5912
    • (1987) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 35
    • 0025815177 scopus 로고
    • A human autoantibody specific for a unique conserved region of 28S ribosomal RNA inhibits the interaction of elongation factors 1 and 2 with ribosomes
    • Uchiumi, T., Traut, R.R., Elkon, K., and Kominami, R. (1991) A human autoantibody specific for a unique conserved region of 28S ribosomal RNA inhibits the interaction of elongation factors 1 and 2 with ribosomes. J. Biol. Chem. 266, 2054-2062
    • (1991) J. Biol. Chem. , vol.266 , pp. 2054-2062
    • Uchiumi, T.1    Traut, R.R.2    Elkon, K.3    Kominami, R.4
  • 36
    • 0024287862 scopus 로고
    • Ricin and α-sarcin alter the conformation of 60S ribosomal subunits at neighboring but different sites
    • Terao, K., Uchiumi, T., Endo, Y., and Ogata, K. (1988) Ricin and α-sarcin alter the conformation of 60S ribosomal subunits at neighboring but different sites. Eur. J. Biochem. 174, 459-463
    • (1988) Eur. J. Biochem. , vol.174 , pp. 459-463
    • Terao, K.1    Uchiumi, T.2    Endo, Y.3    Ogata, K.4
  • 37
    • 0344135964 scopus 로고
    • A ribosome-dependent GTPase from yeast distinct from elongation factor 2
    • Skogerson, L. and Wakatama, E. (1976) A ribosome-dependent GTPase from yeast distinct from elongation factor 2. Proc. Natl. Acad. Sci. USA 73, 73-76
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 73-76
    • Skogerson, L.1    Wakatama, E.2
  • 38
    • 0027182421 scopus 로고
    • Translation elongation factor 3: A fungus-specific-translation factor?
    • Belfield, G.P. and Tuite, M.F. (1993) Translation elongation factor 3: a fungus-specific-translation factor? Mol. Microbiol. 9, 411-418
    • (1993) Mol. Microbiol. , vol.9 , pp. 411-418
    • Belfield, G.P.1    Tuite, M.F.2
  • 39
    • 0023733679 scopus 로고
    • Role of elongation factor 3 (EF-3) at AA-tRNA binding step
    • Uritani, M. and Miyazaki, M. (1988) Role of elongation factor 3 (EF-3) at AA-tRNA binding step. J. Biochem. 104, 118-126
    • (1988) J. Biochem. , vol.104 , pp. 118-126
    • Uritani, M.1    Miyazaki, M.2
  • 40
    • 0024437753 scopus 로고
    • Role of yeast elongation factor 3 in the elongation cycle
    • Kamath, A. and Chakraburtty, K. (1989) Role of yeast elongation factor 3 in the elongation cycle. J. Biol. Chem. 264, 15423-15428
    • (1989) J. Biol. Chem. , vol.264 , pp. 15423-15428
    • Kamath, A.1    Chakraburtty, K.2
  • 41
    • 0029154909 scopus 로고
    • The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor
    • Triana-Alonso, F.J., Chakraburtty, K., and Nierhaus, K.H. (1995) The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J. Biol. Chem. 270, 20473-20478
    • (1995) J. Biol. Chem. , vol.270 , pp. 20473-20478
    • Triana-Alonso, F.J.1    Chakraburtty, K.2    Nierhaus, K.H.3


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