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Volumn 191, Issue 7, 2009, Pages 2042-2050

Genetic analysis of the invariant residue G791 in Escherichia coli 16S rRNA implicates RelA in ribosome function

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CHLORAMPHENICOL ACETYLTRANSFERASE; GUANOSINE TRIPHOSPHATE 3' DIPHOSPHATE; GUANOSINE TRIPHOSPHATE DERIVATIVE; MESSENGER RNA; MUTANT PROTEIN; RNA 16S; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG; BACTERIAL RNA; ESCHERICHIA COLI PROTEIN; GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; GUANOSINE 3',5' POLYPHOSPHATE SYNTHETASES; GUANOSINE 3',5'-POLYPHOSPHATE SYNTHETASES; LIGASE;

EID: 64049087228     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00904-08     Document Type: Article
Times cited : (6)

References (43)
  • 1
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coliK-12
    • Bachmann, B. J. 1972. Pedigrees of some mutant strains of Escherichia coliK-12. Bacteriol. Rev. 36:525-557.
    • (1972) Bacteriol. Rev , vol.36 , pp. 525-557
    • Bachmann, B.J.1
  • 3
    • 0003174053 scopus 로고    scopus 로고
    • The stringent response
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, American Society for Microbiology, Washington, DC
    • Cashel, M., D. R. Gentry, V. J. Hernandez, and D. Vinella. 1996. The stringent response, p. 1458-1496. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1458-1496
    • Cashel, M.1    Gentry, D.R.2    Hernandez, V.J.3    Vinella, D.4
  • 4
    • 0032881809 scopus 로고    scopus 로고
    • X-ray crystal structures of 70S ribosome functional complexes
    • Cate, J. H., M. M. Yusupov, G. Z. Yusupova, T. N. Earnest, and H. F. Noller. 1999. X-ray crystal structures of 70S ribosome functional complexes. Science 285:2095-2104.
    • (1999) Science , vol.285 , pp. 2095-2104
    • Cate, J.H.1    Yusupov, M.M.2    Yusupova, G.Z.3    Earnest, T.N.4    Noller, H.F.5
  • 6
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 7
    • 0016284355 scopus 로고
    • Stringent control of ribosomal protein gene expression in Escherichia coli
    • Dennis, P., and M. Nomura. 1974. Stringent control of ribosomal protein gene expression in Escherichia coli. Proc. Natl. Acad. Sci. USA 71:3819- 3823.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3819-3823
    • Dennis, P.1    Nomura, M.2
  • 8
    • 1642564526 scopus 로고    scopus 로고
    • Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: The universally conserved residues G693 and C795 regulate P-site RNA binding
    • Dinos, G., D. N. Wilson, Y. Teraoka, W. Szaflarski, P. Fucini, D. Kalpaxis, and K. H. Nierhaus. 2004. Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: the universally conserved residues G693 and C795 regulate P-site RNA binding. Mol. Cell 13:113-124.
    • (2004) Mol. Cell , vol.13 , pp. 113-124
    • Dinos, G.1    Wilson, D.N.2    Teraoka, Y.3    Szaflarski, W.4    Fucini, P.5    Kalpaxis, D.6    Nierhaus, K.H.7
  • 9
    • 0022495417 scopus 로고
    • Elongation factor Tu · guanosine 3′-diphosphate 5′-diphosphate complex increases the fidelity of proofreading in protein biosynthesis
    • Dix, D. B., and R. C. Thompson. 1986. Elongation factor Tu · guanosine 3′-diphosphate 5′-diphosphate complex increases the fidelity of proofreading in protein biosynthesis. Proc. Natl. Acad. Sci. USA 83:2027-2031.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2027-2031
    • Dix, D.B.1    Thompson, R.C.2
  • 10
    • 0035150018 scopus 로고    scopus 로고
    • Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain
    • Gropp, M., Y. Strausz, M. Gross, and G. Glaser. 2001. Regulation of Escherichia coli RelA requires oligomerization of the C-terminal domain. J. Bacteriol. 183:570-579.
    • (2001) J. Bacteriol , vol.183 , pp. 570-579
    • Gropp, M.1    Strausz, Y.2    Gross, M.3    Glaser, G.4
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 0007825206 scopus 로고
    • Synthesis of guanosine tetra and pentaphosphate requires the codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes
    • Haseltine, W. A., and R. Block. 1973. Synthesis of guanosine tetra and pentaphosphate requires the codon-specific, uncharged transfer ribonucleic acid in the acceptor site of ribosomes. Proc. Natl. Acad. Sci. USA 70:1564- 1568.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 1564-1568
    • Haseltine, W.A.1    Block, R.2
  • 13
    • 0015515019 scopus 로고
    • MSI and MSII made on ribosome in idling step of protein synthesis
    • Haseltine, W. A., R. Block, W. Gilbert, and K. Weber. 1972. MSI and MSII made on ribosome in idling step of protein synthesis. Nature 238:381-384.
    • (1972) Nature , vol.238 , pp. 381-384
    • Haseltine, W.A.1    Block, R.2    Gilbert, W.3    Weber, K.4
  • 14
    • 85016731055 scopus 로고
    • Using PCR to engineer DNA
    • H. A. Erlich ed, Stockton Press, New York, NY
    • Higuchi, R. 1989. Using PCR to engineer DNA, p. 61-70. In H. A. Erlich (ed.), PCR technology. Stockton Press, New York, NY.
    • (1989) PCR technology , pp. 61-70
    • Higuchi, R.1
  • 15
    • 0013830963 scopus 로고
    • Mode of action of herbicide, 3-amino-1,2,4-triazole (amitrole): Inhibition of an enzyme of histidine biosynthesis
    • Hilton, J. P., P. C. Kearney, and B. N. Ames. 1965. Mode of action of herbicide, 3-amino-1,2,4-triazole (amitrole): inhibition of an enzyme of histidine biosynthesis. Arch. Biochem. Biophys. 112:544-547.
    • (1965) Arch. Biochem. Biophys , vol.112 , pp. 544-547
    • Hilton, J.P.1    Kearney, P.C.2    Ames, B.N.3
  • 16
    • 0023614950 scopus 로고
    • Directing ribosomes to a single mRNA species: A method to study rRNA mutations and their effects on translation of a single messenger in Escherichia coli
    • Hui, A., P. Jhurani, and H. A. de Boer. 1987. Directing ribosomes to a single mRNA species: a method to study rRNA mutations and their effects on translation of a single messenger in Escherichia coli. Methods Enzymol. 153:432-452.
    • (1987) Methods Enzymol , vol.153 , pp. 432-452
    • Hui, A.1    Jhurani, P.2    de Boer, H.A.3
  • 17
    • 0021348009 scopus 로고
    • Promoter selectivity of Escherichia coliRNA polymerase. Differential stringent control of the multiple promoters from ribosomal RNA and protein operons
    • Kajitani, M., and A. Ishihama. 1984. Promoter selectivity of Escherichia coliRNA polymerase. Differential stringent control of the multiple promoters from ribosomal RNA and protein operons. J. Biol. Chem. 259:1951-1957.
    • (1984) J. Biol. Chem , vol.259 , pp. 1951-1957
    • Kajitani, M.1    Ishihama, A.2
  • 18
    • 0015238989 scopus 로고
    • The control of ribonucleic acid synthesis during amino acid deprivation in Escherichia coli
    • Lazzarini, R., and A. Dahlberg. 1971. The control of ribonucleic acid synthesis during amino acid deprivation in Escherichia coli. J. Biol. Chem. 246:420-429.
    • (1971) J. Biol. Chem , vol.246 , pp. 420-429
    • Lazzarini, R.1    Dahlberg, A.2
  • 19
    • 0029905958 scopus 로고    scopus 로고
    • Genetic analysis of the Shine-Dalgarno interaction: Selection of alternative functional mRNA-rRNA combinations
    • Lee, K., C. A. Holland-Staley, and P. R. Cunningham. 1996. Genetic analysis of the Shine-Dalgarno interaction: selection of alternative functional mRNA-rRNA combinations. RNA 2:1270-1285.
    • (1996) RNA , vol.2 , pp. 1270-1285
    • Lee, K.1    Holland-Staley, C.A.2    Cunningham, P.R.3
  • 20
    • 0031588021 scopus 로고    scopus 로고
    • In vivodetermination of RNA structure-function relationships: Analysis of the 790 loop in ribosomal RNA
    • Lee, K., S. Varma, J. Santalucia, Jr., and P. R. Cunningham. 1997. In vivodetermination of RNA structure-function relationships: analysis of the 790 loop in ribosomal RNA. J. Mol. Biol. 269:732-743.
    • (1997) J. Mol. Biol , vol.269 , pp. 732-743
    • Lee, K.1    Varma, S.2    Santalucia Jr., J.3    Cunningham, P.R.4
  • 21
    • 0035513584 scopus 로고    scopus 로고
    • Genetic approaches to studying protein synthesis: Effects of mutations at 516 and A535 in Escherichia coli 16S rRNA
    • Lee, K., C. A. Holland-Staley, and P. R. Cunningham. 2001. Genetic approaches to studying protein synthesis: Effects of mutations at 516 and A535 in Escherichia coli 16S rRNA. J. Nutr. 131:2994S-3004S.
    • (2001) J. Nutr , vol.131
    • Lee, K.1    Holland-Staley, C.A.2    Cunningham, P.R.3
  • 22
    • 0030660210 scopus 로고    scopus 로고
    • Pactamycin resistance mutations in functional sites of 16S rRNA
    • Mankin, A. S. 1997. Pactamycin resistance mutations in functional sites of 16S rRNA. J. Mol. Biol. 274:8-15.
    • (1997) J. Mol. Biol , vol.274 , pp. 8-15
    • Mankin, A.S.1
  • 23
    • 0022916242 scopus 로고
    • Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes
    • Moazed, D., and H. F. Noller. 1986. Transfer RNA shields specific nucleotides in 16S ribosomal RNA from attack by chemical probes. Cell 47:985- 994.
    • (1986) Cell , vol.47 , pp. 985-994
    • Moazed, D.1    Noller, H.F.2
  • 24
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed, D., and H. F. Noller. 1987. Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327:389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 25
    • 0029051704 scopus 로고
    • Specific protection of 16 S rRNA by translational initiation factors
    • Moazed, D., R. R. Samaha, C. Gualerzi, and H. F. Noller. 1995. Specific protection of 16 S rRNA by translational initiation factors. J. Mol. Biol. 248:207-210.
    • (1995) J. Mol. Biol , vol.248 , pp. 207-210
    • Moazed, D.1    Samaha, R.R.2    Gualerzi, C.3    Noller, H.F.4
  • 26
    • 0024974085 scopus 로고
    • Escherichia coli initiation factor 3 protein binding to 30 S ribosomal subunits alters the accessibility of nucleotides within the conserved central region of 16S rRNA
    • Muralikrishna, P., and E. Wickstrom. 1989. Escherichia coli initiation factor 3 protein binding to 30 S ribosomal subunits alters the accessibility of nucleotides within the conserved central region of 16S rRNA. Biochemistry 28:7505-7510.
    • (1989) Biochemistry , vol.28 , pp. 7505-7510
    • Muralikrishna, P.1    Wickstrom, E.2
  • 27
    • 0017403108 scopus 로고
    • Analysis of the relA gene product of Escherichia coli
    • Pedersen, F. S., and N. O. Kjeldgaard. 1977. Analysis of the relA gene product of Escherichia coli. Eur. J. Biochem. 76:91-97.
    • (1977) Eur. J. Biochem , vol.76 , pp. 91-97
    • Pedersen, F.S.1    Kjeldgaard, N.O.2
  • 28
    • 2442563845 scopus 로고
    • Localization of the stringent protein of Escherichia coli on the 50S ribosomal subunit
    • Ramagopal, S., and B. D. Davis. 1974. Localization of the stringent protein of Escherichia coli on the 50S ribosomal subunit. Proc. Natl. Acad. Sci. USA 71:820-824.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 820-824
    • Ramagopal, S.1    Davis, B.D.2
  • 29
    • 0023772262 scopus 로고
    • Basal ppGpp level adjustment shown by new spoT mutants affect steady state growth rates and rrnA ribosomal promoter regulation in Escherichia coli
    • Sarubbi, E., K. R. Rudd, and M. Cashel. 1988. Basal ppGpp level adjustment shown by new spoT mutants affect steady state growth rates and rrnA ribosomal promoter regulation in Escherichia coli. Mol. Gen. Genet. 213:214- 222.
    • (1988) Mol. Gen. Genet , vol.213 , pp. 214-222
    • Sarubbi, E.1    Rudd, K.R.2    Cashel, M.3
  • 31
    • 55749101368 scopus 로고    scopus 로고
    • Identification of amino acid residues in the catalytic domain of RNase E essential for survival of Escherichia coli: Functional analysis of DNase I subdomain
    • Shin, E., H. Go, J.-H. Yeom, M. Won, J. Bae, S. H. Han, K. Han, Y. Lee, N.-C. Ha, C. J. Moore, B. Sohlberg, S. N. Cohen, and K. Lee. 2008. Identification of amino acid residues in the catalytic domain of RNase E essential for survival of Escherichia coli: functional analysis of DNase I subdomain. Genetics 179:1871-1879.
    • (2008) Genetics , vol.179 , pp. 1871-1879
    • Shin, E.1    Go, H.2    Yeom, J.-H.3    Won, M.4    Bae, J.5    Han, S.H.6    Han, K.7    Lee, Y.8    Ha, N.-C.9    Moore, C.J.10    Sohlberg, B.11    Cohen, S.N.12    Lee, K.13
  • 33
    • 0016825910 scopus 로고
    • Guanosine 5-diphosphate 3-diphosphate (ppGpp) positive effector for histidine operon transcription and general signal for amino-acid deficiency
    • Stephens, J. C., S. W. Artz, and B. N. Ames. 1975. Guanosine 5-diphosphate 3-diphosphate (ppGpp) positive effector for histidine operon transcription and general signal for amino-acid deficiency. Proc. Natl. Acad. Sci. USA 72:4389-4393.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4389-4393
    • Stephens, J.C.1    Artz, S.W.2    Ames, B.N.3
  • 34
    • 0015578636 scopus 로고
    • Identification of the synthesis of guanosine tetraphosphate (MS I) as insertion of a pyrophosphoryl group into the 3-position in guanosine 5-diphosphate
    • Sy, J., and F. Lipmann. 1973. Identification of the synthesis of guanosine tetraphosphate (MS I) as insertion of a pyrophosphoryl group into the 3-position in guanosine 5-diphosphate. Proc. Natl. Acad. Sci. USA 70:306- 309.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 306-309
    • Sy, J.1    Lipmann, F.2
  • 35
    • 1842403743 scopus 로고
    • Mutation at position 791 in Escherichia coli 16S ribosomal RNA affects processes involved in the initiation of protein synthesis
    • Tapprich, W. E., D. J. Goss, and A. E. Dahlberg. 1989. Mutation at position 791 in Escherichia coli 16S ribosomal RNA affects processes involved in the initiation of protein synthesis. Proc. Natl. Acad. Sci. USA 86:4927-4931.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4927-4931
    • Tapprich, W.E.1    Goss, D.J.2    Dahlberg, A.E.3
  • 37
    • 0033553439 scopus 로고    scopus 로고
    • Wimberly, B. T., R. Guymon, J. P. McCutcheon, S. W. White, and V. Ramakrishnan. 1999. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell 97:491-502.
    • Wimberly, B. T., R. Guymon, J. P. McCutcheon, S. W. White, and V. Ramakrishnan. 1999. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell 97:491-502.
  • 39
    • 0034751687 scopus 로고    scopus 로고
    • Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli
    • Yang, X., and E. E. Ishiguro. 2001. Involvement of the N terminus of ribosomal protein L11 in regulation of the RelA protein of Escherichia coli. J. Bacteriol. 183:6532-6537.
    • (2001) J. Bacteriol , vol.183 , pp. 6532-6537
    • Yang, X.1    Ishiguro, E.E.2
  • 40
    • 0013898139 scopus 로고
    • Intracellular condition of Escherichia coli transfer RNA
    • Yegian, C. D., G. S. Stent, and E. M. Martin. 1966. Intracellular condition of Escherichia coli transfer RNA. Proc. Natl. Acad. Sci. USA 55:839-846.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.55 , pp. 839-846
    • Yegian, C.D.1    Stent, G.S.2    Martin, E.M.3
  • 41
    • 33744509312 scopus 로고    scopus 로고
    • RraA rescues Escherichia coli cells overproducing RNase E from growth arrest by modulating the ribonucleolytic activity
    • Yeom, J.-H., and K. Lee. 2006. RraA rescues Escherichia coli cells overproducing RNase E from growth arrest by modulating the ribonucleolytic activity. Biochem. Biophys. Res. Commun. 345:1372-1376.
    • (2006) Biochem. Biophys. Res. Commun , vol.345 , pp. 1372-1376
    • Yeom, J.-H.1    Lee, K.2
  • 42
    • 47349133364 scopus 로고    scopus 로고
    • Inhibitory effects of RraA and RraB on RNase E-related enzymes imply conserved functions in the regulated enzymatic cleavage of RNA
    • Yeom, J. H., H. Go, E. Shin, H. L. Kim, S. H. Han, C. J. Moore, J. Bae, and K. Lee. 2008. Inhibitory effects of RraA and RraB on RNase E-related enzymes imply conserved functions in the regulated enzymatic cleavage of RNA. FEMS Microbiol. Lett. 285:10-15.
    • (2008) FEMS Microbiol. Lett , vol.285 , pp. 10-15
    • Yeom, J.H.1    Go, H.2    Shin, E.3    Kim, H.L.4    Han, S.H.5    Moore, C.J.6    Bae, J.7    Lee, K.8


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