메뉴 건너뛰기




Volumn 31, Issue 1, 1999, Pages 163-173

Functional interaction of yeast elongation factor 3 with yeast ribosomes

Author keywords

ABC protein; ATPase; Elongation factor 3; Protein synthesis; Ribosome; rRNA; Saccharomyces cerevisiae

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ELONGATION FACTOR 3; GUANOSINE TRIPHOSPHATE; LYSINE; PROTEIN; TRANSFER RNA;

EID: 0033003952     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(98)00139-3     Document Type: Review
Times cited : (15)

References (50)
  • 1
    • 0021891865 scopus 로고
    • Eukaryotic protein synthesisis
    • K. Moldave, Eukaryotic protein synthesisis, Ann. Rev. Biochem. 54 (1985) 1109-1149.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 1109-1149
    • Moldave, K.1
  • 3
    • 0018338668 scopus 로고
    • Separation and characterization of yeast elongation factors
    • L. Skogerson, Separation and characterization of yeast elongation factors, Methods Enzymol. 60 (1979) 676-685.
    • (1979) Methods Enzymol. , vol.60 , pp. 676-685
    • Skogerson, L.1
  • 4
    • 0019843254 scopus 로고
    • Purification and properties of elongation factor 3 from S. cerevisiae
    • B. Dasmahaptra, K. Chakraburtty, Purification and properties of elongation factor 3 from S. cerevisiae, J. Biol. Chem. 252 (1981) 9999-10004.
    • (1981) J. Biol. Chem. , vol.252 , pp. 9999-10004
    • Dasmahaptra, B.1    Chakraburtty, K.2
  • 6
    • 0344135964 scopus 로고
    • A ribosome-dependent GTPase from yeast distinct from elongation factor 2
    • L. Skogerson, E. Wakatama, A ribosome-dependent GTPase from yeast distinct from elongation factor 2, Proc. Natl. Acad. Sci. USA 73 (1977) 73-76.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 73-76
    • Skogerson, L.1    Wakatama, E.2
  • 7
    • 0010295613 scopus 로고
    • Elongation factor 3: A unique fungal protein
    • P.B. Fernandes (Ed.), Birkhauser, Boston
    • K. Chakraburtty, Elongation factor 3: a unique fungal protein, in: P.B. Fernandes (Ed.), New Approaches to Antifungal Drugs. Birkhauser, Boston, 1992, pp. 114-142.
    • (1992) New Approaches to Antifungal Drugs , pp. 114-142
    • Chakraburtty, K.1
  • 8
    • 0025180478 scopus 로고
    • Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae
    • S. Qin, A. Xie, M.C.M. Bonato, C.S. McLaughlin, Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae, J. Biol. Chem. 265 (1990) 1903-1912.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1903-1912
    • Qin, S.1    Xie, A.2    Bonato, M.C.M.3    McLaughlin, C.S.4
  • 9
    • 0025182923 scopus 로고
    • Protein synthesis in yeast: Structural and functional analysis of the gene encoding elongation factor 3
    • M.G. Sandbaken, J.A. Lupisella, B. DiDomenico, K. Chakraburtty, Protein synthesis in yeast: structural and functional analysis of the gene encoding elongation factor 3, J. Biol. Chem. 265 (1990) 15838-15844.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15838-15844
    • Sandbaken, M.G.1    Lupisella, J.A.2    DiDomenico, B.3    Chakraburtty, K.4
  • 11
    • 0027182421 scopus 로고
    • Translation elongation factor 3: A fungus-specific translation factor?
    • G.P. Belfield, M.F. Tuite, Translation elongation factor 3: a fungus-specific translation factor? Mol. Microbiol. 9 (1993) 411-418.
    • (1993) Mol. Microbiol. , vol.9 , pp. 411-418
    • Belfield, G.P.1    Tuite, M.F.2
  • 12
    • 0029049427 scopus 로고
    • Translational elongation factor-3 (EF-3): An evolving eukaryotic ribosomal protein?
    • G.P. Belfield, N.J. Ross-Smith, M.F. Tuite, Translational elongation factor-3 (EF-3): an evolving eukaryotic ribosomal protein? J. Mol. Evol. 41 (1995) 376-387.
    • (1995) J. Mol. Evol. , vol.41 , pp. 376-387
    • Belfield, G.P.1    Ross-Smith, N.J.2    Tuite, M.F.3
  • 13
    • 0031854374 scopus 로고    scopus 로고
    • Yeast elongation factor 3: Structure and function
    • K. Chakraburtty, F.J. Triana-Alonso, Yeast elongation factor 3: structure and function, Biol. Chem. 379 (1998) 831-840.
    • (1998) Biol. Chem. , vol.379 , pp. 831-840
    • Chakraburtty, K.1    Triana-Alonso, F.J.2
  • 15
    • 0023733679 scopus 로고
    • Role of the yeast peptide elongation factor 3 (EF-3) at the aa-tRNA binding step
    • M. Uritani, M. Miyazaki, Role of the yeast peptide elongation factor 3 (EF-3) at the aa-tRNA binding step, J. Biochem. 104 (1988) 118-126.
    • (1988) J. Biochem. , vol.104 , pp. 118-126
    • Uritani, M.1    Miyazaki, M.2
  • 16
    • 0024437753 scopus 로고
    • Role of yeast elongation factor 3 in the elongation cycle
    • A. Kamath, K. Chakraburtty, Role of yeast elongation factor 3 in the elongation cycle, J. Biol. Chem. 264 (1989) 1543-15428.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1543-15428
    • Kamath, A.1    Chakraburtty, K.2
  • 17
    • 0025280137 scopus 로고
    • The allosteric three-site model for the ribosomal elongation cycle: Features and future
    • K.H. Nierhaus, The allosteric three-site model for the ribosomal elongation cycle: features and future, Biochemistry 29 (1990) 4297-4310.
    • (1990) Biochemistry , vol.29 , pp. 4297-4310
    • Nierhaus, K.H.1
  • 18
    • 0343176044 scopus 로고
    • Transfer RNA binding to 80S ribosomes from yeast. Evidence for three sites
    • F.J. Triana, K.H. Nierhaus, K. Chakraburtty, Transfer RNA binding to 80S ribosomes from yeast. Evidence for three sites, Biochem. Mol. Biol. Int. 32 (1994) 336-342.
    • (1994) Biochem. Mol. Biol. Int. , vol.32 , pp. 336-342
    • Triana, F.J.1    Nierhaus, K.H.2    Chakraburtty, K.3
  • 19
    • 0343093240 scopus 로고
    • Defining the function of EF-3: A unique elongation factor in low fungi
    • K.H. Nierhaus (Ed.), Plenum Press, New York
    • F.J. Triana, K.H. Nierhaus, J.A. Ziehler, K. Chakraburtty, Defining the function of EF-3: a unique elongation factor in low fungi, in: K.H. Nierhaus (Ed.), Translational Apparatus, Plenum Press, New York, 1993, pp. 327-338.
    • (1993) Translational Apparatus , pp. 327-338
    • Triana, F.J.1    Nierhaus, K.H.2    Ziehler, J.A.3    Chakraburtty, K.4
  • 20
    • 0029154909 scopus 로고
    • Role of EF-3 in allosteric interactions of A- And E-sites of eukaryotic ribosomes
    • F.J. Triana-Alonso, K. Chakraburtty, K.H. Nierhaus, Role of EF-3 in allosteric interactions of A- and E-sites of eukaryotic ribosomes, J. Biol. Chem. 270 (1995) 20473-20478.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20473-20478
    • Triana-Alonso, F.J.1    Chakraburtty, K.2    Nierhaus, K.H.3
  • 22
    • 0025696479 scopus 로고
    • Soluble factor requirements for the tetrahymena peptide elongation system and the ribosomal ATPase as a counterpart of yeast elongation factor 3 (EF-3)
    • M. Miyazaki, H. Kagiyama, Soluble factor requirements for the tetrahymena peptide elongation system and the ribosomal ATPase as a counterpart of yeast elongation factor 3 (EF-3), J. Biochem. 108 (1990) 1001-1008.
    • (1990) J. Biochem. , vol.108 , pp. 1001-1008
    • Miyazaki, M.1    Kagiyama, H.2
  • 23
    • 0027944283 scopus 로고
    • Comparative analysis of ribosome associated ATPase from pig liver and ATPase of elongation factor 3 from S. cerevisiae
    • O. Kovalchuke, K. Chakraburtty, Comparative analysis of ribosome associated ATPase from pig liver and ATPase of elongation factor 3 from S. cerevisiae, Eur. J. Biochem. 266 (1994) 133-140.
    • (1994) Eur. J. Biochem. , vol.266 , pp. 133-140
    • Kovalchuke, O.1    Chakraburtty, K.2
  • 25
    • 0029609276 scopus 로고
    • ATPase associated with Tetrahymena riibosome is not a functional analog of yeast EF-3
    • O. Kovalchuke, J.A. Ziehler, K. Chakraburtty, ATPase associated with Tetrahymena riibosome is not a functional analog of yeast EF-3, Biochemie 71 (1995) 713-718.
    • (1995) Biochemie , vol.71 , pp. 713-718
    • Kovalchuke, O.1    Ziehler, J.A.2    Chakraburtty, K.3
  • 26
    • 0028304633 scopus 로고
    • Why do two EF-Tu molecules act in the elongation cycle of protein syntheses?
    • A. Weijland, A. Parmeggiani, Why do two EF-Tu molecules act in the elongation cycle of protein syntheses? TIBS 19 (1994) 188-192.
    • (1994) TIBS , vol.19 , pp. 188-192
    • Weijland, A.1    Parmeggiani, A.2
  • 27
    • 0028351548 scopus 로고
    • Two GTPs are hydrolyzed on two molecules of EF-Tu for each elongation cycle during code translation
    • J. Scoble, J. Bilgin, M. Ehrenberg, Two GTPs are hydrolyzed on two molecules of EF-Tu for each elongation cycle during code translation, Biochimie 76 (1994) 59-62.
    • (1994) Biochimie , vol.76 , pp. 59-62
    • Scoble, J.1    Bilgin, J.2    Ehrenberg, M.3
  • 29
    • 0031939254 scopus 로고    scopus 로고
    • Identification and kinetic analysis of a functional homolog of elongation factor 3, YEF3 Saccharomyces cerevisiae
    • A.V. Sarthy, T. Mcgonigal, J.O. Capobianco, M. Schmidt, S.R. Green, C.M. Moehle, R.C. Goldman, Identification and kinetic analysis of a functional homolog of elongation factor 3, YEF3 in Saccharomyces cerevisiae, Yeast 14 (1998) 239-253.
    • (1998) Yeast , vol.14 , pp. 239-253
    • Sarthy, A.V.1    Mcgonigal, T.2    Capobianco, J.O.3    Schmidt, M.4    Green, S.R.5    Moehle, C.M.6    Goldman, R.C.7
  • 30
    • 0024674170 scopus 로고
    • Synthesis of ribosomes in Saccharomyces cerevisiae
    • J.R. Warner, Synthesis of ribosomes in Saccharomyces cerevisiae, Microbiol. Rev. 53 (1989) 256-271.
    • (1989) Microbiol. Rev. , vol.53 , pp. 256-271
    • Warner, J.R.1
  • 32
    • 0026608524 scopus 로고
    • Elongation factor 3 (EF-3) from Candida albicans shows both structural and functional similarity to EF-3 from Saccharomyces cerevisiae
    • D.R. Colthurst, B.S. Schander, M.V. Hayes, M.F. Tuite, Elongation factor 3 (EF-3) from Candida albicans shows both structural and functional similarity to EF-3 from Saccharomyces cerevisiae, Mol. Microbiol. 6 (1992) 1025-1033.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1025-1033
    • Colthurst, D.R.1    Schander, B.S.2    Hayes, M.V.3    Tuite, M.F.4
  • 33
    • 0026521867 scopus 로고
    • Isolation and sequence analysis of the gene encoding translation elongation factor 3 from Candida albicans
    • B.J. DiDomenico, J.A. Lupisella, M.G. Sandbaken, K. Chakraburtty, Isolation and sequence analysis of the gene encoding translation elongation factor 3 from Candida albicans, Yeast 8 (1992) 337-352.
    • (1992) Yeast , vol.8 , pp. 337-352
    • DiDomenico, B.J.1    Lupisella, J.A.2    Sandbaken, M.G.3    Chakraburtty, K.4
  • 34
    • 0026535292 scopus 로고
    • Isolation and sequence analysis of the gene for translation elongation factor 3 from Candida albicans
    • K.K. Myers, W.A. Fonzi, P.S. Sypherd, Isolation and sequence analysis of the gene for translation elongation factor 3 from Candida albicans, NAR 20 (1992) 1705-1710.
    • (1992) NAR , vol.20 , pp. 1705-1710
    • Myers, K.K.1    Fonzi, W.A.2    Sypherd, P.S.3
  • 35
    • 0026649547 scopus 로고
    • Fungus-specific translation elongation factor 3 gene present in Pneumocystis carinii
    • M.F. Ypma-Wong, W.A. Fonzi, P.S. Sypherd, Fungus-specific translation elongation factor 3 gene present in Pneumocystis carinii, Infect. Immun. 60 (1992) 4140-4145.
    • (1992) Infect. Immun. , vol.60 , pp. 4140-4145
    • Ypma-Wong, M.F.1    Fonzi, W.A.2    Sypherd, P.S.3
  • 36
    • 0027373539 scopus 로고
    • Expression of the gene encoding a translational elongation factor 3 homolog of chlorella virus CVK2
    • T. Yamada, T. Fukuda, K. Tamura, S. Furukawa, P. Songari, Expression of the gene encoding a translational elongation factor 3 homolog of chlorella virus CVK2, Virology 197 (1993) 742-750.
    • (1993) Virology , vol.197 , pp. 742-750
    • Yamada, T.1    Fukuda, T.2    Tamura, K.3    Furukawa, S.4    Songari, P.5
  • 38
    • 0027458116 scopus 로고
    • ATP-dependent transport systems in bacteria and humans: Relevance to cystic fibrosis and multidrug resistance
    • C.A. Doige, G.F.-L. Ames, ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance, Ann. Rev. Microbiol. 47 (1993) 291-319.
    • (1993) Ann. Rev. Microbiol. , vol.47 , pp. 291-319
    • Doige, C.A.1    Ames, G.F.-L.2
  • 39
    • 0001607723 scopus 로고
    • Distantly related sequences in the a and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • J.E. Walker, M. Saraste, M.J. Runswick, N.J. Gay, Distantly related sequences in the a and β-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, EMBO. J. 1 (1982) 945-951.
    • (1982) EMBO. J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 41
    • 0030891728 scopus 로고    scopus 로고
    • Functional subdomains of yeast elongation factor 3: Localization of the ribosome-binding domain
    • R. Kambampati, K. Chakraburtty, Functional subdomains of yeast elongation factor 3: localization of the ribosome-binding domain, J. Biol. Chem. 272 (1997) 6377-6381.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6377-6381
    • Kambampati, R.1    Chakraburtty, K.2
  • 43
    • 0025935551 scopus 로고
    • The conformation of the α-sarcin/ricin loop from 28S ribosomal RNA
    • A.A. Szewczak, Y.L. Chan, P.B. Moore, I.G. Wool, The conformation of the α-sarcin/ricin loop from 28S ribosomal RNA, Biochemie 73 (1991) 871-877.
    • (1991) Biochemie , vol.73 , pp. 871-877
    • Szewczak, A.A.1    Chan, Y.L.2    Moore, P.B.3    Wool, I.G.4
  • 44
    • 0026764794 scopus 로고
    • The two main states of the elongating ribosome and the role of the α-sarcin stem-loop structure of 23S RNA
    • K.H. Nierhaus, S. Schiling-Bartetzko, T. Twardowski, The two main states of the elongating ribosome and the role of the α-sarcin stem-loop structure of 23S RNA, Biochemie 74 (1992) 403-410.
    • (1992) Biochemie , vol.74 , pp. 403-410
    • Nierhaus, K.H.1    Schiling-Bartetzko, S.2    Twardowski, T.3
  • 45
    • 0028263814 scopus 로고
    • A functional site of the GTPase-associated center within 28S ribosomal RNA probed with an anti-RNA autoantibody
    • T. Uchiumi, R. Kominami, A functional site of the GTPase-associated center within 28S ribosomal RNA probed with an anti-RNA autoantibody, EMBO J. 13 (1994) 3389-3394.
    • (1994) EMBO J. , vol.13 , pp. 3389-3394
    • Uchiumi, T.1    Kominami, R.2
  • 47
    • 0029456005 scopus 로고
    • Interaction of Yeast EF-3 with polynucleotides, ribosomal rna and ribosomal subunits
    • O. Kovalchuke, K. Chakraburtty, Interaction of Yeast EF-3 with polynucleotides, ribosomal rna and ribosomal subunits, Indian J. Biochem. Biophys. 32 (1995) 336-342.
    • (1995) Indian J. Biochem. Biophys. , vol.32 , pp. 336-342
    • Kovalchuke, O.1    Chakraburtty, K.2
  • 48
    • 2642610571 scopus 로고    scopus 로고
    • A monoclonal antibody specific for carboxy-terminal region of yeast translation elongation factor-3 inhibits ribosome-activated ATPase but not intrinsic ATPase activity
    • M. Uritani, A. Tabata, K. Nakayama, M. Izuta, M. lizumi, M. Arisawa, A monoclonal antibody specific for carboxy-terminal region of yeast translation elongation factor-3 inhibits ribosome-activated ATPase but not intrinsic ATPase activity, Biochem. Mol. Biol. Int. 1039 (1996) 227-234.
    • (1996) Biochem. Mol. Biol. Int. , vol.1039 , pp. 227-234
    • Uritani, M.1    Tabata, A.2    Nakayama, K.3    Izuta, M.4    Lizumi, M.5    Arisawa, M.6
  • 49
    • 0032562689 scopus 로고    scopus 로고
    • The N-terminus of eukaryotic translation factor 3 interacts with 18S rRNA and 80S ribosomes
    • R.R. Gontarek, H. Li, K. Nurse, C.D. Prescott, The N-terminus of eukaryotic translation factor 3 interacts with 18S rRNA and 80S ribosomes, J. Biol. Chem. 273 (1998) 10249-10252.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10249-10252
    • Gontarek, R.R.1    Li, H.2    Nurse, K.3    Prescott, C.D.4
  • 50
    • 0028609495 scopus 로고
    • Interaction sites of ribosome-bound eukaryotic elongation factor 2 in 185 and 285 rRNA
    • L. Holmberg, O. Nygard, Interaction sites of ribosome-bound eukaryotic elongation factor 2 in 185 and 285 rRNA, Biochemistry 33 (1994) 15159-15167.
    • (1994) Biochemistry , vol.33 , pp. 15159-15167
    • Holmberg, L.1    Nygard, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.