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Volumn 16, Issue 8, 1996, Pages 4248-4256

The A1 · U72 base pair conserved in eukaryotic initiator tRNAs is important specifically for binding to the eukaryotic translation initiation factor eIF2

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATE; METHIONINE TRANSFER RNA; PUROMYCIN; TRANSCRIPTION FACTOR; INITIATION FACTOR 2; METHIONINE TRANSFER RNA LIGASE; PRIMER DNA; RNA BINDING PROTEIN;

EID: 0029666095     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.8.4248     Document Type: Article
Times cited : (35)

References (53)
  • 1
    • 0018180547 scopus 로고
    • Transformation of yeast by a replicating hybrid plasmid
    • Beggs, J. D. 1978. Transformation of yeast by a replicating hybrid plasmid. Nature (London) 275:104-109.
    • (1978) Nature (London) , vol.275 , pp. 104-109
    • Beggs, J.D.1
  • 3
    • 0025900055 scopus 로고
    • Function of eukaryotic initiation factor 5 in the formation of an 80S ribosomal polypeptide chain initiation complex
    • Chakrabarti, A., and U. Maitra. 1991. Function of eukaryotic initiation factor 5 in the formation of an 80S ribosomal polypeptide chain initiation complex. J. Biol. Chem. 266:14039-14045.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14039-14045
    • Chakrabarti, A.1    Maitra, U.2
  • 4
    • 0026579205 scopus 로고
    • Initiator methionine tRNA is essential for Ty1 transposition in yeast
    • Chapman, K. B., A. S. Byström, and J. D. Boeke. 1992. Initiator methionine tRNA is essential for Ty1 transposition in yeast. Proc. Natl. Acad. Sci. USA 89:3236-3240.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3236-3240
    • Chapman, K.B.1    Byström, A.S.2    Boeke, J.D.3
  • 5
    • 0019887986 scopus 로고
    • Characterization of eukaryotic initiation factor 2 containing two polypeptide chains of Mr = 48,000 and 38,000
    • Chaudhuri, A., E. A. Stringer, D. Valenzuela, and U. Maitra. 1981. Characterization of eukaryotic initiation factor 2 containing two polypeptide chains of Mr = 48,000 and 38,000. J. Biol. Chem. 256:3988-3944.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3988-13944
    • Chaudhuri, A.1    Stringer, E.A.2    Valenzuela, D.3    Maitra, U.4
  • 6
    • 0028365706 scopus 로고
    • Purification and characterization of bacterially expressed mammalian translation initiation factor 5 (eIF-5): Demonstration that eIF-5 forms a specific complex with eIF-2
    • Chaudhuri, J., K. Das, and U. Maitra. 1994. Purification and characterization of bacterially expressed mammalian translation initiation factor 5 (eIF-5): demonstration that eIF-5 forms a specific complex with eIF-2. Biochemistry 33:4794-4799.
    • (1994) Biochemistry , vol.33 , pp. 4794-4799
    • Chaudhuri, J.1    Das, K.2    Maitra, U.3
  • 7
    • 0027198021 scopus 로고
    • Characterization of mammalian translation initiation factor 5 (eIF-5)
    • Chevesich, J., J. Chaudhuri, and U. Maitra. 1993. Characterization of mammalian translation initiation factor 5 (eIF-5). J. Biol. Chem. 268:20659-20667.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20659-20667
    • Chevesich, J.1    Chaudhuri, J.2    Maitra, U.3
  • 8
    • 0024280899 scopus 로고
    • i functions in directing the scanning ribosome to the start site of translocation
    • i functions in directing the scanning ribosome to the start site of translocation. Science 242:93-97.
    • (1988) Science , vol.242 , pp. 93-97
    • Cigan, A.M.1    Feng, L.2    Donahue, T.F.3
  • 9
    • 0025787133 scopus 로고
    • Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase
    • Despons, L., P. Walter, B. Senger, J. Ebel, and F. Fasiolo. 1991. Identification of potential amino acid residues supporting anticodon recognition in yeast methionyl-tRNA synthetase. FEBS Lett. 289:217-220.
    • (1991) FEBS Lett. , vol.289 , pp. 217-220
    • Despons, L.1    Walter, P.2    Senger, B.3    Ebel, J.4    Fasiolo, F.5
  • 11
    • 0023664637 scopus 로고
    • The isolation and characterization from rabbit reticulocytes of two forms of eukaryotic initiation factor 2 having different β polypeptides
    • Dholakia, J. N., and A. J. Wanna. 1987. The isolation and characterization from rabbit reticulocytes of two forms of eukaryotic initiation factor 2 having different β polypeptides. J. Biol. Chem. 262:10164-10170.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10164-10170
    • Dholakia, J.N.1    Wanna, A.J.2
  • 12
    • 0024297814 scopus 로고
    • Mutations at a Zn(II) linger motif in the yeast eIF-2b gene alter ribosomal start-site selection during the scanning process
    • Donahue, T. F., A. M. Cigan, E. K. Pabich, and B. Castilho-Valavicius. 1988. Mutations at a Zn(II) linger motif in the yeast eIF-2b gene alter ribosomal start-site selection during the scanning process. Cell 54:621-632.
    • (1988) Cell , vol.54 , pp. 621-632
    • Donahue, T.F.1    Cigan, A.M.2    Pabich, E.K.3    Castilho-Valavicius, B.4
  • 13
    • 0027423265 scopus 로고
    • The role of nucleotides conserved in eukaryotic initiator methionine tRNAs in initiation of protein synthesis
    • Drabkin, H. J., B. Helk, and U. L. RajBhandary. 1993. The role of nucleotides conserved in eukaryotic initiator methionine tRNAs in initiation of protein synthesis. J. Biol. Chem. 268:25221-25228.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25221-25228
    • Drabkin, H.J.1    Helk, B.2    RajBhandary, U.L.3
  • 14
    • 0021875706 scopus 로고
    • Attempted expression of a human initiator tRNA in Saccharomyces cerevisiae
    • Drabkin, H. J., and U. L. RajBhandary. 1985. Attempted expression of a human initiator tRNA in Saccharomyces cerevisiae. J. Biol. Chem. 260:5596-5602.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5596-5602
    • Drabkin, H.J.1    RajBhandary, U.L.2
  • 16
    • 0021028478 scopus 로고
    • The presence of a defective LEU2 gene on 2-μ DNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number
    • Erhart, H., and C. P. Hollenberg. 1983. The presence of a defective LEU2 gene on 2-μ DNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number. J. Bacteriol. 156:625-635.
    • (1983) J. Bacteriol. , vol.156 , pp. 625-635
    • Erhart, H.1    Hollenberg, C.P.2
  • 18
    • 0025110827 scopus 로고
    • Expression and function of a human initiator tRNA gene in the yeast Saccharomyces cerevisiae
    • Francis, M., and U. L. RajBhandary. 1990. Expression and function of a human initiator tRNA gene in the yeast Saccharomyces cerevisiae. Mol. Cell. Biol. 10:4486-4494.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 4486-4494
    • Francis, M.1    RajBhandary, U.L.2
  • 19
    • 0016688390 scopus 로고
    • Nucleotide sequence of human placenta cytoplasmic initiator tRNA
    • Gillum, A. M., B. Roe, M. P. J. S. Anandraj, and U. L. RajBhandary. 1975. Nucleotide sequence of human placenta cytoplasmic initiator tRNA. Cell 6:407-413.
    • (1975) Cell , vol.6 , pp. 407-413
    • Gillum, A.M.1    Roe, B.2    Anandraj, M.P.J.S.3    RajBhandary, U.L.4
  • 20
    • 0016788897 scopus 로고
    • Nucleotide sequence of salmon testes and salmon liver cytoplasmic initiator tRNA
    • Gillum, A. M., N. Urquhart, M. Smith, and U. L. RajBhandary. 1975. Nucleotide sequence of salmon testes and salmon liver cytoplasmic initiator tRNA. Cell 6:395-405.
    • (1975) Cell , vol.6 , pp. 395-405
    • Gillum, A.M.1    Urquhart, N.2    Smith, M.3    RajBhandary, U.L.4
  • 21
    • 0021153752 scopus 로고
    • Halobacterium volcanii tRNAs
    • Gupta, R. 1984. Halobacterium volcanii tRNAs. J. Biol. Chem. 259:9461-9471.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9461-9471
    • Gupta, R.1
  • 22
    • 0024797894 scopus 로고
    • Protein phosphorylation controls translation rates
    • Hershey, J. W. B. 1989. Protein phosphorylation controls translation rates. J. Biol. Chem. 264:20823-20826.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20823-20826
    • Hershey, J.W.B.1
  • 25
    • 0029036154 scopus 로고
    • Archaea: Narrowing the gap between prokaryotes and eukaryotes
    • Keeling, P. J., and W. F. Doolittle. 1995. Archaea: narrowing the gap between prokaryotes and eukaryotes. Proc. Natl. Acad. Sci. USA 92:5761-5767.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5761-5767
    • Keeling, P.J.1    Doolittle, W.F.2
  • 27
    • 0021099278 scopus 로고
    • Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange factor activity during protein synthesis initiation
    • Konieczny, A., and B. Safer. 1983. Purification of the eukaryotic initiation factor 2-eukaryotic initiation factor 2B complex and characterization of its guanine nucleotide exchange factor activity during protein synthesis initiation. J. Biol. Chem. 258:3402-3408.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3402-3408
    • Konieczny, A.1    Safer, B.2
  • 28
    • 0020570527 scopus 로고
    • Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles
    • Kozak, M. 1983. Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles. Microbiol. Rev. 4:1-45.
    • (1983) Microbiol. Rev. , vol.4 , pp. 1-45
    • Kozak, M.1
  • 29
    • 0024546509 scopus 로고
    • The scanning model for translation: An update
    • Kozak, M. 1989. The scanning model for translation: an update. J. Cell Biol. 108:229-241.
    • (1989) J. Cell Biol. , vol.108 , pp. 229-241
    • Kozak, M.1
  • 30
    • 0026490544 scopus 로고
    • Use of gel retardation to analyze protein-nucleic acid interactions
    • Lane, D., P. Prentki, and M. Chandler. 1992. Use of gel retardation to analyze protein-nucleic acid interactions. Microbiol. Rev. 56:509-528.
    • (1992) Microbiol. Rev. , vol.56 , pp. 509-528
    • Lane, D.1    Prentki, P.2    Chandler, M.3
  • 31
    • 0026757771 scopus 로고
    • Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by E. coli methionyl-tRNA synthetase and methionyl-tRNA transformylase
    • Lee, C.-P., M. Dyson, N. Mandal, U. Varshney, B. Bahramian, and U. L. RajBhandary. 1992. Striking effects of coupling mutations in the acceptor stem on recognition of tRNAs by E. coli methionyl-tRNA synthetase and methionyl-tRNA transformylase. Proc. Natl. Acad. Sci. USA 89:9262-9266.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9262-9266
    • Lee, C.-P.1    Dyson, M.2    Mandal, N.3    Varshney, U.4    Bahramian, B.5    RajBhandary, U.L.6
  • 32
    • 0022423187 scopus 로고
    • Evaluation and significance of kinetic parameters governing function of protein synthesis initiation factors eIF-2 and eIF-2B
    • Manchester, K. L. 1985. Evaluation and significance of kinetic parameters governing function of protein synthesis initiation factors eIF-2 and eIF-2B. FEBS Lett. 182:15-19.
    • (1985) FEBS Lett. , vol.182 , pp. 15-19
    • Manchester, K.L.1
  • 33
    • 0018400571 scopus 로고
    • Assays for eukaryotic protein synthesis
    • Merrick, W. C. 1979. Assays for eukaryotic protein synthesis. Methods Enzymol. 60:108-123.
    • (1979) Methods Enzymol. , vol.60 , pp. 108-123
    • Merrick, W.C.1
  • 34
    • 0026718508 scopus 로고
    • Mechanism and regulation of eukaryotic protein synthesis
    • Merrick, W. C. 1992. Mechanism and regulation of eukaryotic protein synthesis. Microbiol. Rev. 56:291-315.
    • (1992) Microbiol. Rev. , vol.56 , pp. 291-315
    • Merrick, W.C.1
  • 35
    • 0027112088 scopus 로고
    • Evaluation of control strategies for high cell density fermentation
    • O'Connor, G. M., F. Sanchez-Riera, and C. L. Cooney. 1992. Evaluation of control strategies for high cell density fermentation. Biotechnol. Bioeng. 39:293-304.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 293-304
    • O'Connor, G.M.1    Sanchez-Riera, F.2    Cooney, C.L.3
  • 36
    • 0028125575 scopus 로고
    • Initiator transfer RNAs
    • RajBhandary, U. L. 1994. Initiator transfer RNAs. J. Bacteriol. 176:547-552.
    • (1994) J. Bacteriol. , vol.176 , pp. 547-552
    • RajBhandary, U.L.1
  • 37
    • 0002084108 scopus 로고
    • Initiator tRNAs and initiation of protein synthesis
    • D. Söll and U. L. RajBhandary (ed.), American Society for Microbiology, Washington, D.C.
    • RajBhandary, U. L., and C. M. Chow. 1995. Initiator tRNAs and initiation of protein synthesis, p. 511-528. In D. Söll and U. L. RajBhandary (ed.), tRNA: structure, biosynthesis, and function. American Society for Microbiology, Washington, D.C.
    • (1995) tRNA: Structure, Biosynthesis, and Function , pp. 511-528
    • RajBhandary, U.L.1    Chow, C.M.2
  • 38
    • 0014669517 scopus 로고
    • Studies of polynucleotides. XCI. Yeast methionine transfer ribonucleic acids: Purification, properties, and terminal nucleotide sequences
    • RajBhandary, U. L., and H. P. Ghosh. 1969. Studies of polynucleotides. XCI. Yeast methionine transfer ribonucleic acids: purification, properties, and terminal nucleotide sequences. J. Biol. Chem. 244:1104-1113.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1104-1113
    • RajBhandary, U.L.1    Ghosh, H.P.2
  • 39
    • 0003697893 scopus 로고
    • The AVI Publishing Co., Inc., Westport, Conn.
    • Reed, G., and H. J. Peppler. 1973. Yeast technology. The AVI Publishing Co., Inc., Westport, Conn.
    • (1973) Yeast Technology
    • Reed, G.1    Peppler, H.J.2
  • 40
    • 0023708505 scopus 로고
    • Natural mRNA is required for directing Met-tRNAr binding to 40S ribosomal subunits in animal cells. Involvement of Co-eIF-2A in natural mRNA-directed initiation complex formation
    • Roy, A. L., D. Chakrabarti, B. Datta, R. E. Hileman, and N. K. Gupta. 1988. Natural mRNA is required for directing Met-tRNAr binding to 40S ribosomal subunits in animal cells. Involvement of Co-eIF-2A in natural mRNA-directed initiation complex formation. Biochemistry 27:8203-8209.
    • (1988) Biochemistry , vol.27 , pp. 8203-8209
    • Roy, A.L.1    Chakrabarti, D.2    Datta, B.3    Hileman, R.E.4    Gupta, N.K.5
  • 41
    • 0025932660 scopus 로고
    • Recognition of tRNAs by aminoacyl-tRNA synthetase
    • Schulman, L. H. 1991. Recognition of tRNAs by aminoacyl-tRNA synthetase. Prog. Nucleic Acid Res. Mol. Biol. 41:23-87.
    • (1991) Prog. Nucleic Acid Res. Mol. Biol. , vol.41 , pp. 23-87
    • Schulman, L.H.1
  • 42
    • 0022392095 scopus 로고
    • In vitro conversion of a methionine to a glutamine tRNA
    • Schulman, L. H., and H. Pelka. 1985. In vitro conversion of a methionine to a glutamine tRNA. Biochemistry 24:7309-7314.
    • (1985) Biochemistry , vol.24 , pp. 7309-7314
    • Schulman, L.H.1    Pelka, H.2
  • 44
    • 0015514185 scopus 로고
    • The primary structure of yeast initiator transfer RNA
    • Simsek, M., and U. L. RajBhandary. 1972. The primary structure of yeast initiator transfer RNA. Biochem. Biophys. Res. Commun. 49:508-515.
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 508-515
    • Simsek, M.1    RajBhandary, U.L.2
  • 45
    • 0016253586 scopus 로고
    • Nucleotide sequence of rabbit liver and sheep mammary gland cytoplasmic initiator tRNAs
    • Simsek, M., U. L. RajBhandary, M. Boisnard, and G. Petrissant. 1974. Nucleotide sequence of rabbit liver and sheep mammary gland cytoplasmic initiator tRNAs. Nature (London) 247:518-520.
    • (1974) Nature (London) , vol.247 , pp. 518-520
    • Simsek, M.1    RajBhandary, U.L.2    Boisnard, M.3    Petrissant, G.4
  • 46
    • 0014951549 scopus 로고
    • Cytoplasmic methionine transfer RNAs from eukaryotes
    • Smith, A., and K. A. Marcker. 1970. Cytoplasmic methionine transfer RNAs from eukaryotes. Nature (London) 226:607-610.
    • (1970) Nature (London) , vol.226 , pp. 607-610
    • Smith, A.1    Marcker, K.A.2
  • 47
    • 0027134561 scopus 로고
    • Remarks on the mechanism of ribosome binding to eukaryotic mRNAs
    • Sonenberg, N. 1993. Remarks on the mechanism of ribosome binding to eukaryotic mRNAs. Gene Expr. 3:317-323.
    • (1993) Gene Expr. , vol.3 , pp. 317-323
    • Sonenberg, N.1
  • 49
    • 0027244036 scopus 로고
    • Compilation of tRNA sequences and sequences of tRNA genes
    • Steinberg, S., A. Misch, and M. Sprinzl. 1993. Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res. 21:3011-3015.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3011-3015
    • Steinberg, S.1    Misch, A.2    Sprinzl, M.3
  • 50
    • 0026350896 scopus 로고
    • Direct analysis of aminoacylation levels of tRNAs in vivo
    • Varshney, U., C. P. Lee, and U. L. RajBhandary. 1991. Direct analysis of aminoacylation levels of tRNAs in vivo. J. Biol. Chem. 266:24712-24718.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24712-24718
    • Varshney, U.1    Lee, C.P.2    RajBhandary, U.L.3
  • 51
    • 0025015230 scopus 로고
    • Initiation of protein synthesis using a termination codon
    • Varshney, U., and U. L. RajBhandary. 1990. Initiation of protein synthesis using a termination codon. Proc. Natl. Acad. Sci. USA 87:1586-1590.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1586-1590
    • Varshney, U.1    RajBhandary, U.L.2
  • 52
    • 0026528473 scopus 로고
    • Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae
    • von Pawel-Rammingen, U., S. Aström, and A. S. Byström. 1992. Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae. Mol. Cell. Biol. 12:1432-1442.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1432-1442
    • Von Pawel-Rammingen, U.1    Aström, S.2    Byström, A.S.3
  • 53
    • 0021337227 scopus 로고
    • Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis
    • Wagner, T., M. Gross, and P. B. Sigler. 1984. Isoleucyl initiator tRNA does not initiate eucaryotic protein synthesis. J. Biol. Chem. 259:4706-4709.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4706-4709
    • Wagner, T.1    Gross, M.2    Sigler, P.B.3


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