메뉴 건너뛰기




Volumn 334, Issue 3, 2003, Pages 349-361

Regulation of translation of the head protein of T4 bacteriophage by specific binding of EF-Tu to a leader sequence

Author keywords

EF Tu; GroEL; T4 head protein; Translation regulation

Indexed keywords

BETA GALACTOSIDASE; CHAPERONIN; ELONGATION FACTOR TU; HYBRID PROTEIN; PEPTIDE; PEPTIDE GOL; UNCLASSIFIED DRUG;

EID: 0242579203     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.063     Document Type: Article
Times cited : (10)

References (33)
  • 1
    • 0013915374 scopus 로고
    • Separation of three microbial amino acid polymerization factors
    • Lucas-Lenard J., Lipmann F. Separation of three microbial amino acid polymerization factors. Proc. Natl Acad. Sci. USA. 55:1966;1562-1566.
    • (1966) Proc. Natl Acad. Sci. USA , vol.55 , pp. 1562-1566
    • Lucas-Lenard, J.1    Lipmann, F.2
  • 3
    • 0026588965 scopus 로고
    • Refined structure of elongation factor EF-Tu from Escherichia coli
    • Kjeldegaard M., Nyborg J. Refined structure of elongation factor EF-Tu from Escherichia coli. J. Mol. Biol. 223:1992;721-742.
    • (1992) J. Mol. Biol. , vol.223 , pp. 721-742
    • Kjeldegaard, M.1    Nyborg, J.2
  • 4
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 Å resolution
    • Kawashima T., Berthet-Colominas C., Wulff M., Cusack S., Leberman R. The structure of the Escherichia coli EF-Tu-EF-Ts complex at 2.5 Å resolution. Nature. 379:1996;511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colominas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 5
    • 0028238349 scopus 로고
    • Elongation factor Tu: A regulatory GTPase with an integrated effector
    • Sprinzl M. Elongation factor Tu: a regulatory GTPase with an integrated effector. Trends Biochem. Sci. 19:1994;245-250.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 245-250
    • Sprinzl, M.1
  • 6
    • 0031448932 scopus 로고    scopus 로고
    • Renaturation of rhodanese by translational elongation factor (EF) Tu
    • Kudlicki W., Coffman A., Kramer G., Hardesty B. Renaturation of rhodanese by translational elongation factor (EF) Tu. J. Biol. Chem. 272:1997;32206-32210.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32206-32210
    • Kudlicki, W.1    Coffman, A.2    Kramer, G.3    Hardesty, B.4
  • 7
    • 0032496137 scopus 로고    scopus 로고
    • Chaperone properties of bacterial elongation factor Tu
    • Caldas T.D., El Yaagoubi A., Richarme G. Chaperone properties of bacterial elongation factor Tu. J. Biol. Chem. 273:1998;11478-11482.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11478-11482
    • Caldas, T.D.1    El Yaagoubi, A.2    Richarme, G.3
  • 8
    • 0028136693 scopus 로고
    • Protein synthesis elongation factor EF-1α is essential for ubiquitin-dependent degradation of certain Nα-acetylated proteins and may be substituted by bacterial elongation factor EF-Tu
    • Gonen H., Smith C.E., Siegel N.R., Kahana C., Merrick W.C., Chakraburtty K., et al. Protein synthesis elongation factor EF-1α is essential for ubiquitin-dependent degradation of certain Nα-acetylated proteins and may be substituted by bacterial elongation factor EF-Tu. Proc. Natl Acad. Sci USA. 91:1994;7648-7652.
    • (1994) Proc. Natl Acad. Sci USA , vol.91 , pp. 7648-7652
    • Gonen, H.1    Smith, C.E.2    Siegel, N.R.3    Kahana, C.4    Merrick, W.C.5    Chakraburtty, K.6
  • 9
    • 0017187684 scopus 로고
    • Abundance and membrane association of elongation factor Tu in E. coli
    • Jacobson G.R., Rosenbusch J.P. Abundance and membrane association of elongation factor Tu in E. coli. Nature. 261:1976;23-26.
    • (1976) Nature , vol.261 , pp. 23-26
    • Jacobson, G.R.1    Rosenbusch, J.P.2
  • 10
    • 0028988998 scopus 로고
    • Elongation factor 1, translation and the cytoskeleton
    • Condeelis J. Elongation factor 1, translation and the cytoskeleton. Trends Biochem. Sci. 20:1995;169-170.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 169-170
    • Condeelis, J.1
  • 11
    • 0032989103 scopus 로고    scopus 로고
    • Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 gag polyprotein
    • Cimarelli A., Luban J. Translation elongation factor 1-alpha interacts specifically with the human immunodeficiency virus type 1 gag polyprotein. J. Virol. 73:1999;5388-5401.
    • (1999) J. Virol. , vol.73 , pp. 5388-5401
    • Cimarelli, A.1    Luban, J.2
  • 12
    • 0008279471 scopus 로고
    • Bacteriophage Qβ replicase contains the protein biosynthesis elongation factors EF-Tu and EF-Ts
    • Blumenthal T., Landers T.A., Weber K. Bacteriophage Qβ replicase contains the protein biosynthesis elongation factors EF-Tu and EF-Ts. Proc. Natl Acad. Sci USA. 228:1972;748-751.
    • (1972) Proc. Natl Acad. Sci USA , vol.228 , pp. 748-751
    • Blumenthal, T.1    Landers, T.A.2    Weber, K.3
  • 13
    • 0034725704 scopus 로고    scopus 로고
    • The major head protein of bacteriophage T4 binds specifically to elongation factor Tu
    • Bingham R., Ekunwe S.N., Falk S., Snyder L., Kleanthous C. The major head protein of bacteriophage T4 binds specifically to elongation factor Tu. J. Biol. Chem. 275:2000;23219-23226.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23219-23226
    • Bingham, R.1    Ekunwe, S.N.2    Falk, S.3    Snyder, L.4    Kleanthous, C.5
  • 14
    • 0023906534 scopus 로고
    • The lit gene product which blocks bacteriophage T4 late gene expression is a membrane protein encoded by a cryptic DNA element e14
    • Kao C., Snyder L. The lit gene product which blocks bacteriophage T4 late gene expression is a membrane protein encoded by a cryptic DNA element e14. J. Bacteriol. 170:1988;2056-2062.
    • (1988) J. Bacteriol. , vol.170 , pp. 2056-2062
    • Kao, C.1    Snyder, L.2
  • 15
    • 0021895121 scopus 로고
    • Excision and reintegration of the Escherichia coli element e14
    • Brody H., Greener A., Hill C.W. Excision and reintegration of the Escherichia coli element e14. J. Bacteriol. 161:1985;1112-1117.
    • (1985) J. Bacteriol. , vol.161 , pp. 1112-1117
    • Brody, H.1    Greener, A.2    Hill, C.W.3
  • 16
    • 0028120890 scopus 로고
    • Translation elongation factor Tu cleaved by a phage exclusion system
    • Yu Y.-T.N., Snyder L. Translation elongation factor Tu cleaved by a phage exclusion system. Proc. Natl Acad. Sci. USA. 91:1994;802-806.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 802-806
    • Yu, Y.-T.N.1    Snyder, L.2
  • 18
    • 0025309798 scopus 로고
    • A site in the T4 bacteriophage major head protein gene which can promote the inhibition of all translation in E. coli
    • Bergsland K.J., Kao C., Yu Y.-T.N., Gulati R., Snyder L. A site in the T4 bacteriophage major head protein gene which can promote the inhibition of all translation in E. coli. J. Mol. Biol. 213:1990;477-494.
    • (1990) J. Mol. Biol. , vol.213 , pp. 477-494
    • Bergsland, K.J.1    Kao, C.2    Yu, Y.-T.N.3    Gulati, R.4    Snyder, L.5
  • 19
    • 0031588902 scopus 로고    scopus 로고
    • The genome of the pseudo T-even bacteriophages, a diverse group that resembles T4
    • Monod C., Repoila F., Kutateladze M., Tetart F., Krisch H.M. The genome of the pseudo T-even bacteriophages, a diverse group that resembles T4. J. Mol. Biol. 267:1997;237-249.
    • (1997) J. Mol. Biol. , vol.267 , pp. 237-249
    • Monod, C.1    Repoila, F.2    Kutateladze, M.3    Tetart, F.4    Krisch, H.M.5
  • 21
    • 0027468285 scopus 로고
    • Sequence analysis and phenotypic characterization of groE mutations that block λ and T4 bacteriophage growth
    • Zeilstra-Ryalls J., Fayet O., Baird L., Georgopoulos C. Sequence analysis and phenotypic characterization of groE mutations that block λ and T4 bacteriophage growth. J. Bacteriol. 175:1993;1134-1143.
    • (1993) J. Bacteriol. , vol.175 , pp. 1134-1143
    • Zeilstra-Ryalls, J.1    Fayet, O.2    Baird, L.3    Georgopoulos, C.4
  • 24
    • 0031854151 scopus 로고    scopus 로고
    • Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors
    • Brock S., Szkaradklewicz K., Sprinzl M. Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors. Mol. Microbiol. 29:1998;409-417.
    • (1998) Mol. Microbiol. , vol.29 , pp. 409-417
    • Brock, S.1    Szkaradklewicz, K.2    Sprinzl, M.3
  • 25
    • 0029975504 scopus 로고    scopus 로고
    • Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: TRNA-protein mimicry hypothesis
    • Ito K., Ebihara K., Uno M., Nakamura Y. Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc. Natl Acad. Sci. USA. 93:1996;5443-5448.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5443-5448
    • Ito, K.1    Ebihara, K.2    Uno, M.3    Nakamura, Y.4
  • 26
    • 0030017819 scopus 로고    scopus 로고
    • Limited proteolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu
    • Zeidler W., Schirmer N.K., Egle C., Ribeiro S., Kreutzer R., Sprinzl M. Limited proteolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu. Eur. J. Biochem. 239:1996;265-271.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 265-271
    • Zeidler, W.1    Schirmer, N.K.2    Egle, C.3    Ribeiro, S.4    Kreutzer, R.5    Sprinzl, M.6
  • 28
    • 0032545392 scopus 로고    scopus 로고
    • Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding
    • Andreadis J.D., Black L.W. Substrate mutations that bypass a specific Cpn10 chaperonin requirement for protein folding. J. Biol. Chem. 273:1998;34075-34086.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34075-34086
    • Andreadis, J.D.1    Black, L.W.2
  • 29
    • 0034967287 scopus 로고    scopus 로고
    • Identification of important amino acid residues that modulate binding of Escherichia coli GroEL to its various cochaperones
    • Klein G., Georgopoulos C. Identification of important amino acid residues that modulate binding of Escherichia coli GroEL to its various cochaperones. Genetics. 158:2001;507-517.
    • (2001) Genetics , vol.158 , pp. 507-517
    • Klein, G.1    Georgopoulos, C.2
  • 30
    • 0031947172 scopus 로고    scopus 로고
    • Efficiency of T4 gene 60 translational bypassing
    • Maldonado R., Herr A.J. Efficiency of T4 gene 60 translational bypassing. J. Bacteriol. 180:1998;1822-1830.
    • (1998) J. Bacteriol. , vol.180 , pp. 1822-1830
    • Maldonado, R.1    Herr, A.J.2
  • 32
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller J.H. Experiments in Molecular Genetics. 1972;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.