메뉴 건너뛰기




Volumn 290, Issue 4, 1999, Pages 825-837

Discrimination by Escherichia coli initiation factor IF3 against initiation on non-canonical codons relies on complementarity rules

Author keywords

Control; Initiation; Regulation; Ribosome; Translation

Indexed keywords

ARYLFORMAMIDASE; INITIATION FACTOR 3; LEUCINE TRANSFER RNA; LEUCINE TRANSFER RNA LIGASE; METHIONINE TRANSFER RNA; RNA;

EID: 0032795785     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2881     Document Type: Article
Times cited : (44)

References (53)
  • 1
    • 0027223104 scopus 로고
    • Recognition nucleotides of Escherichia coli transfer RNA(Leu) and its elements facilitating discrimination from transfer RNA(Ser) and transfer RNA(Tyr)
    • Asahara H., Himeno H., Tamura K., Hasegawa T., Watanabe K., Shimizu M. Recognition nucleotides of Escherichia coli transfer RNA(Leu) and its elements facilitating discrimination from transfer RNA(Ser) and transfer RNA(Tyr). J. Mol. Biol. 231:1993;219-229.
    • (1993) J. Mol. Biol. , vol.231 , pp. 219-229
    • Asahara, H.1    Himeno, H.2    Tamura, K.3    Hasegawa, T.4    Watanabe, K.5    Shimizu, M.6
  • 2
    • 0023057311 scopus 로고
    • Formyl-methionyl-tRNA binding to 30S ribosomes programmed with homopolynucleotides and the effect of translational initiation factor 3
    • Berkhout B., van der Laken C. J., van Knippenberg P. H. Formyl-methionyl-tRNA binding to 30S ribosomes programmed with homopolynucleotides and the effect of translational initiation factor 3. Biochim. Biophys. Acta. 866:1986;144-153.
    • (1986) Biochim. Biophys. Acta , vol.866 , pp. 144-153
    • Berkhout, B.1    Van Der Laken, C.J.2    Van Knippenberg, P.H.3
  • 6
    • 0022887593 scopus 로고
    • Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivo
    • Butler J. S., Springer M., Dondon J., Graffe M., Grunberg-Manago M. Escherichia coli protein synthesis initiation factor IF3 controls its own gene expression at the translational level in vivo. J. Mol. Biol. 192:1986;767-780.
    • (1986) J. Mol. Biol. , vol.192 , pp. 767-780
    • Butler, J.S.1    Springer, M.2    Dondon, J.3    Graffe, M.4    Grunberg-Manago, M.5
  • 7
    • 2542445479 scopus 로고
    • AUU to AUG mutation in the initiator codon of the translation initiation factor IF3 abolishes translational autocontrol of its own gene (infC) in vivo
    • Butler J. S., Springer M., Grunberg-Manago M. AUU to AUG mutation in the initiator codon of the translation initiation factor IF3 abolishes translational autocontrol of its own gene (infC) in vivo. Proc. Natl Acad. Sci. USA. 84:1987;4022-4025.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4022-4025
    • Butler, J.S.1    Springer, M.2    Grunberg-Manago, M.3
  • 8
    • 0028904488 scopus 로고
    • AUC is used as start codon in E. coli
    • Chalut C., Egly J. M. AUC is used as start codon in E. coli. Gene. 156:1995;43-45.
    • (1995) Gene , vol.156 , pp. 43-45
    • Chalut, C.1    Egly, J.M.2
  • 9
    • 0025280234 scopus 로고
    • Initiation of in vivo protein synthesis with non-methionine amino acids
    • Chattapadhyay R., Pelka H., Schulman L. Initiation of in vivo protein synthesis with non-methionine amino acids. Biochemistry. 29:1990;4263-4268.
    • (1990) Biochemistry , vol.29 , pp. 4263-4268
    • Chattapadhyay, R.1    Pelka, H.2    Schulman, L.3
  • 10
    • 0028264806 scopus 로고
    • The dsg gene of Myxococcus xanthus encodes a protein similar to translation initiation factor IF3
    • Cheng Y. L., Kalman L. V., Kaiser D. The dsg gene of Myxococcus xanthus encodes a protein similar to translation initiation factor IF3. J. Bacteriol. 176:1994;1427-1433.
    • (1994) J. Bacteriol. , vol.176 , pp. 1427-1433
    • Cheng, Y.L.1    Kalman, L.V.2    Kaiser, D.3
  • 11
    • 0024986686 scopus 로고
    • Control of prokaryotic translation initiation by mRNA secondary structure
    • de Smit M. H., van Duin J. Control of prokaryotic translation initiation by mRNA secondary structure. Prog. Nucl. Acid Res. Mol. Biol. 38:1990;1-35.
    • (1990) Prog. Nucl. Acid Res. Mol. Biol. , vol.38 , pp. 1-35
    • De Smit, M.H.1    Van Duin, J.2
  • 12
    • 0015924558 scopus 로고
    • Formylation of mischarged E. coli rm tRNA rm Metrm f
    • Giegé R., Ebel J. P., Clark B. F. C. Formylation of mischarged E. coli rm tRNA rm Met rm f. FEBS Letters. 30:1973;291-295.
    • (1973) FEBS Letters , vol.30 , pp. 291-295
    • Giegé, R.1    Ebel, J.P.2    Clark, B.F.C.3
  • 15
    • 0029787494 scopus 로고    scopus 로고
    • Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli
    • Guillon J.-M., Heiss S., Soutourina J., Mechulam Y., Laalami S., Grunberg-Manago M., Blanquet S. Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli. J. Biol. Chem. 271:1996;22321-22325.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22321-22325
    • Guillon, J.-M.1    Heiss, S.2    Soutourina, J.3    Mechulam, Y.4    Laalami, S.5    Grunberg-Manago, M.6    Blanquet, S.7
  • 16
    • 0030690291 scopus 로고    scopus 로고
    • IF3-mediated suppression of a GUA initiation codon mutation in the recJ gene of Escherichia Coli
    • Haggerty T. J. IF3-mediated suppression of a GUA initiation codon mutation in the recJ gene of Escherichia Coli. J. Bacteriol. 179:1997;6705-6713.
    • (1997) J. Bacteriol. , vol.179 , pp. 6705-6713
    • Haggerty, T.J.1
  • 17
    • 0024835265 scopus 로고
    • Selection of the initiator tRNA by E. coli initiation factors
    • Hartz D., McPheeters D. S., Gold L. Selection of the initiator tRNA by E. coli initiation factors. Genes Dev. 3:1989;1899-1912.
    • (1989) Genes Dev. , vol.3 , pp. 1899-1912
    • Hartz, D.1    McPheeters, D.S.2    Gold, L.3
  • 18
    • 0025018043 scopus 로고
    • Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by E. coli IF3
    • Hartz D., Binkley J., Hollinsworth T., Gold L. Domains of initiator tRNA and initiation codon crucial for initiator tRNA selection by E. coli IF3. Genes Dev. 4:1990;1790-1800.
    • (1990) Genes Dev. , vol.4 , pp. 1790-1800
    • Hartz, D.1    Binkley, J.2    Hollinsworth, T.3    Gold, L.4
  • 20
    • 0023373136 scopus 로고
    • Specialized ribosome system: Preferential translation of a single mRNA species by a subpopulation of mutated ribosomes in E. coli
    • Hui A., de Boer H. A. Specialized ribosome system: preferential translation of a single mRNA species by a subpopulation of mutated ribosomes in E. coli. Proc. Natl Acad. Sci. USA. 84:1987;4762-4766.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4762-4766
    • Hui, A.1    De Boer, H.A.2
  • 21
    • 0002568139 scopus 로고    scopus 로고
    • A comparative view of initiation site selection mechanisms
    • J. W. B. Heshey, & M. B. Mathews. Cold Spring Harbor: Cold Spring Harbor Laboratory Press
    • Jackson R. J. A comparative view of initiation site selection mechanisms. Heshey J. W. B., Mathews M. B. Translational Control. 1996;71-112 Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (1996) Translational Control , pp. 71-112
    • Jackson, R.J.1
  • 22
    • 0025954907 scopus 로고
    • Initiation of translation at an AUA codon for an archebacterial protein gene expressed in E. coli
    • Köpke A. K. E., Leggatt P. A. Initiation of translation at an AUA codon for an archebacterial protein gene expressed in E. coli. Nucl. Acids Res. 19:1991;5169-5172.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 5169-5172
    • Köpke, A.K.E.1    Leggatt, P.A.2
  • 23
    • 0027151981 scopus 로고
    • Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression
    • la Teana A., Pon C. L., Gualerzi C. O. Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression. Proc. Natl Acad. Sci. USA. 90:1993;4161-4165.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4161-4165
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 24
    • 0026095269 scopus 로고
    • Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem
    • Lee C. P., Seong B. L., RajBhandary U. L. Structural and sequence elements important for recognition of Escherichia coli formylmethionine tRNA by methionyl-tRNA transformylase are clustered in the acceptor stem. J. Biol. Chem. 266:1991;18012-18017.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18012-18017
    • Lee, C.P.1    Seong, B.L.2    Rajbhandary, U.L.3
  • 25
    • 0029017739 scopus 로고
    • Mutants of E. coli initiator tRNA defective in initiation
    • Mangroo D., RajBhandary U. T. Mutants of E. coli initiator tRNA defective in initiation. J. Biol. Chem. 270:1995;12203-12209.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12203-12209
    • Mangroo, D.1    Rajbhandary, U.T.2
  • 26
    • 0028173550 scopus 로고
    • Prokaryotic translation: The interactive pathway leading to initiation
    • McCarthy J. E. G., Brimacombe R. Prokaryotic translation: the interactive pathway leading to initiation. Trends Genet. 10:1994;402-407.
    • (1994) Trends Genet. , vol.10 , pp. 402-407
    • McCarthy, J.E.G.1    Brimacombe, R.2
  • 28
    • 0028982837 scopus 로고
    • fMet by E. coli RNase P is specified by a guanosine of the 5′ flanking sequence
    • fMet by E. coli RNase P is specified by a guanosine of the 5′ flanking sequence. J. Biol. Chem. 270:1995;15906-15914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15906-15914
    • Meinnel, T.1    Blanquet, S.2
  • 32
  • 33
    • 0029051704 scopus 로고
    • Specific protection of 16 S rRNA by translational initiation factors
    • Moazed D., Samaha R. R., Gualerzi C., Noller H. F. Specific protection of 16 S rRNA by translational initiation factors. J. Mol. Biol. 248:1995;207-210.
    • (1995) J. Mol. Biol. , vol.248 , pp. 207-210
    • Moazed, D.1    Samaha, R.R.2    Gualerzi, C.3    Noller, H.F.4
  • 35
    • 0017357987 scopus 로고
    • Chemical measurement of steady-state levels of ten aminoacyl-transfer Ribonucleic Acid synthetases in E.coli
    • Neidhardt F.C., Bloch P.L., Pedersen S., Reeh S. Chemical measurement of steady-state levels of ten aminoacyl-transfer Ribonucleic Acid synthetases in E.coli. J.Bacteriol. 129:1977;378-387.
    • (1977) J.Bacteriol , vol.129 , pp. 378-387
    • Neidhardt, F.C.1    Bloch, P.L.2    Pedersen, S.3    Reeh, S.4
  • 36
    • 0002084108 scopus 로고
    • Initiator tRNAs and initiation of protein synthesis
    • D. Söll, & U. RajBhandary. Washington: American Society for Microbiology
    • RajBhandary U. L., Chow C. M. Initiator tRNAs and initiation of protein synthesis. Söll D., RajBhandary U. tRNA. 1995;511-528 American Society for Microbiology, Washington.
    • (1995) TRNA , pp. 511-528
    • Rajbhandary, U.L.1    Chow, C.M.2
  • 37
    • 0017077686 scopus 로고
    • Specificity and properties of the destabilization, induced by initiation factor IF-3, of ternary complexes of the 30-S ribosomal subunit, aminoacyl-tRNA and polynucleotides
    • Risuleo G., Gualerzi C., Pon C. Specificity and properties of the destabilization, induced by initiation factor IF-3, of ternary complexes of the 30-S ribosomal subunit, aminoacyl-tRNA and polynucleotides. Eur. J. Biochem. 67:1976;603-613.
    • (1976) Eur. J. Biochem. , vol.67 , pp. 603-613
    • Risuleo, G.1    Gualerzi, C.2    Pon, C.3
  • 38
    • 0026289515 scopus 로고
    • Initiation of translation at AUC, AUA and AUU codons in E. coli
    • Romero A., Garcia P. Initiation of translation at AUC, AUA and AUU codons in E. coli. FEMS Microbiol. Letters. 84:1991;325-330.
    • (1991) FEMS Microbiol. Letters , vol.84 , pp. 325-330
    • Romero, A.1    Garcia, P.2
  • 39
    • 0020338446 scopus 로고
    • Sequence of a 1.26-kb DNA fragment containing the structural gene for initiation factor IF3: Presence of an AUU initiator codon
    • Sacerdot C., Fayat G., Dessen P., Springer M., Plumbridge J. A., Grunberg-Manago M., Blanquet S. Sequence of a 1.26-kb DNA fragment containing the structural gene for initiation factor IF3: presence of an AUU initiator codon. EMBO J. 1:1982;311-315.
    • (1982) EMBO J. , vol.1 , pp. 311-315
    • Sacerdot, C.1    Fayat, G.2    Dessen, P.3    Springer, M.4    Plumbridge, J.A.5    Grunberg-Manago, M.6    Blanquet, S.7
  • 40
    • 0029742167 scopus 로고    scopus 로고
    • The role of the AUU initiation codon in the negative feedback regulation of the gene for translation initiation factor IF3 in E. coli
    • Sacerdot C., Chiaruttini C., Engst K., Graffe M., Milet M., Mathy N., Dondon J., Springer M. The role of the AUU initiation codon in the negative feedback regulation of the gene for translation initiation factor IF3 in E. coli. Mol. Microbiol. 21:1996;331-346.
    • (1996) Mol. Microbiol. , vol.21 , pp. 331-346
    • Sacerdot, C.1    Chiaruttini, C.2    Engst, K.3    Graffe, M.4    Milet, M.5    Mathy, N.6    Dondon, J.7    Springer, M.8
  • 41
    • 0033591240 scopus 로고    scopus 로고
    • Mutations that alter initiation codon discrimination by E. coli initiation factor IF3
    • Sacerdot C., de Cock E., Engst K., Graffe M., Dardel F., Springer M. Mutations that alter initiation codon discrimination by E. coli initiation factor IF3. J. Mol. Biol. 288:1999;803-810.
    • (1999) J. Mol. Biol. , vol.288 , pp. 803-810
    • Sacerdot, C.1    De Cock, E.2    Engst, K.3    Graffe, M.4    Dardel, F.5    Springer, M.6
  • 43
    • 0029959716 scopus 로고    scopus 로고
    • Molecular recognition governing the initiation of translation in Escherichia coli. A review
    • Schmitt E., Guillon J.-M., Meinnel T., Mechulam Y., Dardel F., Blanquet S. Molecular recognition governing the initiation of translation in Escherichia coli. A review. Biochimie. 78:1996;543-554.
    • (1996) Biochimie , vol.78 , pp. 543-554
    • Schmitt, E.1    Guillon, J.-M.2    Meinnel, T.3    Mechulam, Y.4    Dardel, F.5    Blanquet, S.6
  • 46
    • 0022515311 scopus 로고
    • Genetic definition of the translational operator of the threonine tRNA ligase gene in Escherichia coli
    • Springer M., Graffe M., Butler J. S., Grunberg-Manago M. Genetic definition of the translational operator of the threonine tRNA ligase gene in Escherichia coli. Proc Natl Acad. Sci. USA. 83:1986;4384-4388.
    • (1986) Proc Natl Acad. Sci. USA , vol.83 , pp. 4384-4388
    • Springer, M.1    Graffe, M.2    Butler, J.S.3    Grunberg-Manago, M.4
  • 47
    • 0017161337 scopus 로고
    • Interaction of bacterial initiation factor IF2 with initiator tRNA
    • Sundari R. M., Stringer E. A., Schulman L. H., Maitra U. Interaction of bacterial initiation factor IF2 with initiator tRNA. J. Biol. Chem. 251:1976;3338-3345.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3338-3345
    • Sundari, R.M.1    Stringer, E.A.2    Schulman, L.H.3    Maitra, U.4
  • 48
    • 0029745401 scopus 로고    scopus 로고
    • E. coli translation initiation factor 3 discriminates the initiation codon in vivo
    • Sussman J. K. L. S. E., Simons R. W. E. coli translation initiation factor 3 discriminates the initiation codon in vivo. Mol. Microbiol. 21:1996;347-360.
    • (1996) Mol. Microbiol. , vol.21 , pp. 347-360
    • Sussman, J.K.L.S.E.1    Simons, R.W.2
  • 49
    • 0024331948 scopus 로고
    • The solution structure of the E. coli initiator tRNA and its interaction with initiation factor IF2 and the ribosomal 30S subunit
    • Wakao H., Romby P., Westhof E., Laalami S., Grunberg-Manago M., Ebel J. P., Ehresmann C., Ehresmann B. The solution structure of the E. coli initiator tRNA and its interaction with initiation factor IF2 and the ribosomal 30S subunit. J. Biol. Chem. 264:1990;20363-20367.
    • (1990) J. Biol. Chem. , vol.264 , pp. 20363-20367
    • Wakao, H.1    Romby, P.2    Westhof, E.3    Laalami, S.4    Grunberg-Manago, M.5    Ebel, J.P.6    Ehresmann, C.7    Ehresmann, B.8
  • 50
    • 0031026590 scopus 로고    scopus 로고
    • Effects of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome
    • Wu X. Q., RajBhandary U. L. Effects of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome. J. Biol. Chem. 272:1997;1891-1895.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1891-1895
    • Wu, X.Q.1    Rajbhandary, U.L.2
  • 51
    • 0029835702 scopus 로고    scopus 로고
    • Ribosome-initiator tRNA complex as an intermediate in translation initiation in Escherichia coli revealed by use of mutant initiator tRNAs and specialized ribosomes
    • Wu X. Q., Iyengar P., RajBhandary U. L. Ribosome-initiator tRNA complex as an intermediate in translation initiation in Escherichia coli revealed by use of mutant initiator tRNAs and specialized ribosomes. EMBO J. 15:1996;4734-4739.
    • (1996) EMBO J. , vol.15 , pp. 4734-4739
    • Wu, X.Q.1    Iyengar, P.2    Rajbhandary, U.L.3
  • 53
    • 0023051839 scopus 로고
    • Binding of Escherichia coli protein synthesis initiation factor IF1 to 30S ribosomal subunits measured by fluorescence polarization
    • Zucker F. H., Hershey J. W. Binding of Escherichia coli protein synthesis initiation factor IF1 to 30S ribosomal subunits measured by fluorescence polarization. Biochemistry. 25:1986;3682-3690.
    • (1986) Biochemistry , vol.25 , pp. 3682-3690
    • Zucker, F.H.1    Hershey, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.