메뉴 건너뛰기




Volumn 71, Issue 1, 2009, Pages 66-78

Novel Escherichia coli RF1 mutants with decreased translation termination activity and increased sensitivity to the cytotoxic effect of the bacterial toxins Kid and RelE

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL TOXIN; PROTEIN PRFA; PROTEIN RF 1; TOXIN KID; TOXIN RELE; UNCLASSIFIED DRUG;

EID: 58149107443     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06510.x     Document Type: Article
Times cited : (7)

References (56)
  • 1
    • 0015451273 scopus 로고
    • Pedigrees of some mutant strains of Escherichia coli K-12
    • Bachmann, B.J. (1972) Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol Rev 36 : 525 557.
    • (1972) Bacteriol Rev , vol.36 , pp. 525-557
    • Bachmann, B.J.1
  • 2
    • 0036246053 scopus 로고    scopus 로고
    • Release factor 2 frameshifting sites in different bacteria
    • Baranov, P.V., Gesteland, R.F. Atkins, J.F. (2002) Release factor 2 frameshifting sites in different bacteria. EMBO Rep 3 : 373 377.
    • (2002) EMBO Rep , vol.3 , pp. 373-377
    • Baranov, P.V.1    Gesteland, R.F.2    Atkins, J.F.3
  • 3
    • 0026728290 scopus 로고
    • Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes
    • Bernard, P. Couturier, M. (1992) Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J Mol Biol 226 : 735 745.
    • (1992) J Mol Biol , vol.226 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 4
    • 0024199426 scopus 로고
    • Killing of Escherichia coli cells modulated by components of the stability system ParD of plasmid R1
    • Bravo, A., Ortega, S., de Torrontegui, G. Diaz, R. (1988) Killing of Escherichia coli cells modulated by components of the stability system ParD of plasmid R1. Mol Gen Genet 215 : 146 151.
    • (1988) Mol Gen Genet , vol.215 , pp. 146-151
    • Bravo, A.1    Ortega, S.2    De Torrontegui, G.3    Diaz, R.4
  • 5
    • 0034973583 scopus 로고    scopus 로고
    • Tetracycline antibiotics: Mode of action, applications, molecular biology, and epidemiology of bacterial resistance
    • Chopra, I. Roberts, M. (2001) Tetracycline antibiotics: mode of action, applications, molecular biology, and epidemiology of bacterial resistance. Microbiol Mol Biol Rev 65 : 232 260.
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 232-260
    • Chopra, I.1    Roberts, M.2
  • 6
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • Christensen, S.K., Pedersen, K., Hansen, F.G. Gerdes, K. (2003) Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J Mol Biol 332 : 809 819.
    • (2003) J Mol Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 7
    • 33748309126 scopus 로고    scopus 로고
    • Shutdown decay of mRNA
    • Condon, C. (2006) Shutdown decay of mRNA. Mol Microbiol 61 : 573 583.
    • (2006) Mol Microbiol , vol.61 , pp. 573-583
    • Condon, C.1
  • 8
    • 0024962419 scopus 로고
    • Rates of aminoacyl-tRNA selection at 29 sense codons in vivo
    • Curran, J.F. Yarus, M. (1989) Rates of aminoacyl-tRNA selection at 29 sense codons in vivo. J Mol Biol 209 : 65 77.
    • (1989) J Mol Biol , vol.209 , pp. 65-77
    • Curran, J.F.1    Yarus, M.2
  • 9
    • 4143057005 scopus 로고    scopus 로고
    • Effects of two cis-acting mutations on the regulation and expression of release factor one in Escherichia coli
    • Dahlgren, A. Ryden-Aulin, M. (2004) Effects of two cis-acting mutations on the regulation and expression of release factor one in Escherichia coli. Biochimie 86 : 431 438.
    • (2004) Biochimie , vol.86 , pp. 431-438
    • Dahlgren, A.1    Ryden-Aulin, M.2
  • 10
    • 0024384959 scopus 로고
    • Cloning, genetic characterization, and nucleotide sequence of the hemA-prfA operon of Salmonella typhimurium
    • Elliott, T. (1989) Cloning, genetic characterization, and nucleotide sequence of the hemA-prfA operon of Salmonella typhimurium. J Bacteriol 171 : 3948 3960.
    • (1989) J Bacteriol , vol.171 , pp. 3948-3960
    • Elliott, T.1
  • 11
    • 27244458194 scopus 로고    scopus 로고
    • Crystal structures of complexes between aminoglycosides and decoding a site oligonucleotides: Role of the number of rings and positive charges in the specific binding leading to miscoding
    • Francois, B., Russell, R.J., Murray, J.B., Aboul-ela, F., Masquida, B., Vicens, Q. Westhof, E. (2005) Crystal structures of complexes between aminoglycosides and decoding A site oligonucleotides: role of the number of rings and positive charges in the specific binding leading to miscoding. Nucleic Acids Res 33 : 5677 5690.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5677-5690
    • Francois, B.1    Russell, R.J.2    Murray, J.B.3    Aboul-Ela, F.4    Masquida, B.5    Vicens, Q.6    Westhof, E.7
  • 12
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • Freistroffer, D.V., Pavlov, M.Y., MacDougall, J., Buckingham, R.H. Ehrenberg, M. (1997) Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. EMBO J 16 : 4126 4133.
    • (1997) EMBO J , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 14
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • Frolova, L.Y., Tsivkovskii, R.Y., Sivolobova, G.F., Oparina, N.Y., Serpinsky, O.I., Blinov, V.M., et al. (1999) Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5 : 1014 1020.
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6
  • 15
    • 34249323754 scopus 로고    scopus 로고
    • RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors
    • Gao, H., Zhou, Z., Rawat, U., Huang, C., Bouakaz, L., Wang, C. et al. (2007) RF3 induces ribosomal conformational changes responsible for dissociation of class I release factors. Cell 129 : 929 941.
    • (2007) Cell , vol.129 , pp. 929-941
    • Gao, H.1    Zhou, Z.2    Rawat, U.3    Huang, C.4    Bouakaz, L.5    Wang, C.6
  • 17
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen, M. Gerdes, K. (1998) The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol Microbiol 29 : 1065 1076.
    • (1998) Mol Microbiol , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 18
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J. Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177 : 4121 4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 19
    • 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
  • 20
    • 0038013670 scopus 로고    scopus 로고
    • Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit
    • Hansen, J.L., Moore, P.B. Steitz, T.A. (2003) Structures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit. J Mol Biol 330 : 1061 1075.
    • (2003) J Mol Biol , vol.330 , pp. 1061-1075
    • Hansen, J.L.1    Moore, P.B.2    Steitz, T.A.3
  • 21
    • 0242361562 scopus 로고    scopus 로고
    • Cleavage of the a site mRNA codon during ribosome pausing provides a mechanism for translational quality control
    • Hayes, C.S. Sauer, R.T. (2003) Cleavage of the A site mRNA codon during ribosome pausing provides a mechanism for translational quality control. Mol Cell 12 : 903 911.
    • (2003) Mol Cell , vol.12 , pp. 903-911
    • Hayes, C.S.1    Sauer, R.T.2
  • 22
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide 'anticodon' deciphers stop codons in messenger RNA
    • Ito, K., Uno, M. Nakamura, Y. (2000) A tripeptide 'anticodon' deciphers stop codons in messenger RNA. Nature 403 : 680 684.
    • (2000) Nature , vol.403 , pp. 680-684
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 23
    • 33644766097 scopus 로고    scopus 로고
    • Model for RNA binding and the catalytic site of the RNase Kid of the bacterial parD toxin-antitoxin system
    • Kamphuis, M.B., Bonvin, A.M., Monti, M.C., Lemonnier, M., Munoz-Gomez, A., van den Heuvel, R.H., et al. (2006) Model for RNA binding and the catalytic site of the RNase Kid of the bacterial parD toxin-antitoxin system. J Mol Biol 357 : 115 126.
    • (2006) J Mol Biol , vol.357 , pp. 115-126
    • Kamphuis, M.B.1    Bonvin, A.M.2    Monti, M.C.3    Lemonnier, M.4    Munoz-Gomez, A.5    Van Den Heuvel, R.H.6
  • 24
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • Karimi, R., Pavlov, M.Y., Buckingham, R.H. Ehrenberg, M. (1999) Novel roles for classical factors at the interface between translation termination and initiation. Mol Cell 3 : 601 609.
    • (1999) Mol Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 25
    • 0034426097 scopus 로고    scopus 로고
    • Aminoglycosides: Perspectives on mechanisms of action and resistance and strategies to counter resistance
    • Kotra, L.P., Haddad, J. Mobashery, S. (2000) Aminoglycosides: perspectives on mechanisms of action and resistance and strategies to counter resistance. Antimicrobial Agents Chemother 44 : 3249 3256.
    • (2000) Antimicrobial Agents Chemother , vol.44 , pp. 3249-3256
    • Kotra, L.P.1    Haddad, J.2    Mobashery, S.3
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 0033678964 scopus 로고    scopus 로고
    • Disruption of the F plasmid partition complex in vivo by partition protein SopA
    • Lemonnier, M., Bouet, J.Y., Libante, V. Lane, D. (2000) Disruption of the F plasmid partition complex in vivo by partition protein SopA. Mol Microbiol 38 : 493 505.
    • (2000) Mol Microbiol , vol.38 , pp. 493-505
    • Lemonnier, M.1    Bouet, J.Y.2    Libante, V.3    Lane, D.4
  • 29
    • 33845685669 scopus 로고    scopus 로고
    • Reduced action of polypeptide release factors induces mRNA cleavage and tmRNA tagging at stop codons in Escherichia coli
    • Li, X., Yokota, T., Ito, K., Nakamura, Y. Aiba, H. (2007) Reduced action of polypeptide release factors induces mRNA cleavage and tmRNA tagging at stop codons in Escherichia coli. Mol Microbiol 63 : 116 126.
    • (2007) Mol Microbiol , vol.63 , pp. 116-126
    • Li, X.1    Yokota, T.2    Ito, K.3    Nakamura, Y.4    Aiba, H.5
  • 31
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • Moore, S.D. Sauer, R.T. (2007) The tmRNA system for translational surveillance and ribosome rescue. Annu Rev Biochem 76 : 101 124.
    • (2007) Annu Rev Biochem , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 32
    • 37249066982 scopus 로고    scopus 로고
    • Methylation of bacterial release factors RF1 and RF2 is required for normal translation termination in vivo
    • Mora, L., Heurgue-Hamard, V., de Zamaroczy, M., Kervestin, S. Buckingham, R.H. (2007) Methylation of bacterial release factors RF1 and RF2 is required for normal translation termination in vivo. J Biol Chem 282 : 35638 35645.
    • (2007) J Biol Chem , vol.282 , pp. 35638-35645
    • Mora, L.1    Heurgue-Hamard, V.2    De Zamaroczy, M.3    Kervestin, S.4    Buckingham, R.H.5
  • 36
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle, J.M. Ramakrishnan, V. (2005) Structural insights into translational fidelity. Annu Rev Biochem 74 : 129 177.
    • (2005) Annu Rev Biochem , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 38
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal a site
    • Pedersen, K., Zavialov, A.V., Pavlov, M.Y., Elf, J., Gerdes, K. Ehrenberg, M. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112 : 131 140.
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 39
    • 29244487090 scopus 로고    scopus 로고
    • Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon
    • Petry, S., Brodersen, D.E., Murphy, F.V.T., Dunham, C.M., Selmer, M., Tarry, M.J., et al. (2005) Crystal structures of the ribosome in complex with release factors RF1 and RF2 bound to a cognate stop codon. Cell 123 : 1255 1266.
    • (2005) Cell , vol.123 , pp. 1255-1266
    • Petry, S.1    Brodersen, D.E.2    Murphy, F.V.T.3    Dunham, C.M.4    Selmer, M.5    Tarry, M.J.6
  • 40
    • 0028821311 scopus 로고
    • The identity of the base following the stop codon determines the efficiency of in vivo translational termination in Escherichia coli
    • Poole, E.S., Brown, C.M. Tate, W.P. (1995) The identity of the base following the stop codon determines the efficiency of in vivo translational termination in Escherichia coli. EMBO J 14 : 151 158.
    • (1995) EMBO J , vol.14 , pp. 151-158
    • Poole, E.S.1    Brown, C.M.2    Tate, W.P.3
  • 41
    • 0018838527 scopus 로고
    • 2-Aminopurine
    • Ronen, A. (1980) 2-Aminopurine. Mutat Res 75 : 1 47.
    • (1980) Mutat Res , vol.75 , pp. 1-47
    • Ronen, A.1
  • 42
    • 0021334017 scopus 로고
    • A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors
    • Ryden, S.M. Isaksson, L.A. (1984) A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors. Mol Gen Genet 193 : 38 45.
    • (1984) Mol Gen Genet , vol.193 , pp. 38-45
    • Ryden, S.M.1    Isaksson, L.A.2
  • 44
    • 0037005943 scopus 로고    scopus 로고
    • Genetic identification of two functional regions in the antitoxin of the parD killer system of plasmid R1
    • Santos-Sierra, S., Pardo-Abarrio, C., Giraldo, R. Diaz-Orejas, R. (2002) Genetic identification of two functional regions in the antitoxin of the parD killer system of plasmid R1. FEMS Microbiol Lett 206 : 115 119.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 115-119
    • Santos-Sierra, S.1    Pardo-Abarrio, C.2    Giraldo, R.3    Diaz-Orejas, R.4
  • 45
    • 0035108209 scopus 로고    scopus 로고
    • Programmed cell death in Escherichia coli: Some antibiotics can trigger mazEF lethality
    • Sat, B., Hazan, R., Fisher, T., Khaner, H., Glaser, G. Engelberg-Kulka, H. (2001) Programmed cell death in Escherichia coli: some antibiotics can trigger mazEF lethality. J Bacteriol 183 : 2041 2045.
    • (2001) J Bacteriol , vol.183 , pp. 2041-2045
    • Sat, B.1    Hazan, R.2    Fisher, T.3    Khaner, H.4    Glaser, G.5    Engelberg-Kulka, H.6
  • 47
    • 1842596222 scopus 로고    scopus 로고
    • Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli
    • Sunohara, T., Jojima, K., Tagami, H., Inada, T. Aiba, H. (2004) Ribosome stalling during translation elongation induces cleavage of mRNA being translated in Escherichia coli. J Biol Chem 279 : 15368 15375.
    • (2004) J Biol Chem , vol.279 , pp. 15368-15375
    • Sunohara, T.1    Jojima, K.2    Tagami, H.3    Inada, T.4    Aiba, H.5
  • 48
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • Takagi, H., Kakuta, Y., Okada, T., Yao, M., Tanaka, I. Kimura, M. (2005) Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects. Nat Struct Mol Biol 12 : 327 331.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 49
    • 34548227759 scopus 로고    scopus 로고
    • A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis
    • Trobro, S. Aqvist, J. (2007) A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis. Mol Cell 27 : 758 766.
    • (2007) Mol Cell , vol.27 , pp. 758-766
    • Trobro, S.1    Aqvist, J.2
  • 50
    • 29144499347 scopus 로고    scopus 로고
    • The SAXS solution structure of RF1 differs from its crystal structure and is similar to its ribosome bound cryo-EM structure
    • Vestergaard, B., Sanyal, S., Roessle, M., Mora, L., Buckingham, R.H., Kastrup, J.S., et al. (2005) The SAXS solution structure of RF1 differs from its crystal structure and is similar to its ribosome bound cryo-EM structure. Mol Cell 20 : 929 938.
    • (2005) Mol Cell , vol.20 , pp. 929-938
    • Vestergaard, B.1    Sanyal, S.2    Roessle, M.3    Mora, L.4    Buckingham, R.H.5    Kastrup, J.S.6
  • 51
    • 36248994061 scopus 로고    scopus 로고
    • Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release
    • Youngman, E.M., He, S.L., Nikstad, L.J. Green, R. (2007) Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release. Mol Cell 28 : 533 543.
    • (2007) Mol Cell , vol.28 , pp. 533-543
    • Youngman, E.M.1    He, S.L.2    Nikstad, L.J.3    Green, R.4
  • 52
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov, A.V., Buckingham, R.H. Ehrenberg, M. (2001) A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell 107 : 115 124.
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 53
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • Zavialov, A.V., Mora, L., Buckingham, R.H. Ehrenberg, M. (2002) Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol Cell 10 : 789 798.
    • (2002) Mol Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 54
    • 2442690258 scopus 로고    scopus 로고
    • Interference of mRNA function by sequence-specific endoribonuclease PemK
    • Zhang, J., Zhang, Y., Zhu, L., Suzuki, M. Inouye, M. (2004) Interference of mRNA function by sequence-specific endoribonuclease PemK. J Biol Chem 279 : 20678 20684.
    • (2004) J Biol Chem , vol.279 , pp. 20678-20684
    • Zhang, J.1    Zhang, Y.2    Zhu, L.3    Suzuki, M.4    Inouye, M.5
  • 55
    • 0028117647 scopus 로고
    • Genetic implication for an interaction between release factor one and ribosomal protein L7/L12 in vivo
    • Zhang, S., Ryden-Aulin, M., Kirsebom, L.A. Isaksson, L.A. (1994) Genetic implication for an interaction between release factor one and ribosomal protein L7/L12 in vivo. J Mol Biol 242 : 614 618.
    • (1994) J Mol Biol , vol.242 , pp. 614-618
    • Zhang, S.1    Ryden-Aulin, M.2    Kirsebom, L.A.3    Isaksson, L.A.4
  • 56
    • 0242361323 scopus 로고    scopus 로고
    • MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli
    • Zhang, Y., Zhang, J., Hoeflich, K.P., Ikura, M., Qing, G. Inouye, M. (2003) MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell 12 : 913 923.
    • (2003) Mol Cell , vol.12 , pp. 913-923
    • Zhang, Y.1    Zhang, J.2    Hoeflich, K.P.3    Ikura, M.4    Qing, G.5    Inouye, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.