메뉴 건너뛰기




Volumn 5, Issue 5, 2014, Pages

Relaxed substrate specificity leads to extensive tRNA mischarging by Streptococcus pneumoniae class I and class II aminoacyl-tRNA synthetases

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID TRANSFER RNA LIGASE; CLASS I ISOLEUCYL TRANSFER RNA SYNTHETASE; CLASS II LYSYL TANSFER RNA SYNTHETASE; LEUCINE; LYSINE; PEPTIDOGLYCAN; SERINE; UNCLASSIFIED DRUG; VALINE; BACTERIAL DNA; BACTERIAL PROTEIN; PENICILLIN DERIVATIVE; TRANSFER RNA;

EID: 84908439733     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.01656-14     Document Type: Article
Times cited : (8)

References (55)
  • 1
    • 33847016108 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide production and the Fenton reaction on membrane composition of Streptococcus pneumoniae
    • Pesakhov S, Benisty R, Sikron N, Cohen Z, Gomelsky P, Khozin- Goldberg I, Dagan R, Porat N. 2007. Effect of hydrogen peroxide production and the Fenton reaction on membrane composition of Streptococcus pneumoniae. Biochim. Biophys. Acta 1768:590 -597. http:// dx.doi.org/10.1016/j.bbamem.2006.12.016.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 590-597
    • Pesakhov, S.1    Benisty, R.2    Sikron, N.3    Cohen, Z.4    Gomelsky, P.5    Khozin-Goldberg, I.6    Dagan, R.7    Porat, N.8
  • 2
    • 34548583324 scopus 로고    scopus 로고
    • SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model
    • Regev-Yochay G, Trzcinski K, Thompson CM, Lipsitch M, Malley R. 2007. SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model. J. Bacteriol. 189:6532-6539. http://dx.doi.org/10.1128/JB.00813-07.
    • (2007) J. Bacteriol , vol.189 , pp. 6532-6539
    • Regev-Yochay, G.1    Trzcinski, K.2    Thompson, C.M.3    Lipsitch, M.4    Malley, R.5
  • 3
    • 0033945724 scopus 로고    scopus 로고
    • Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract
    • Pericone CD, Overweg K, Hermans PW, Weiser JN. 2000. Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract. Infect. Immun. 68:3990 -3997. http://dx.doi.org/10.1128/IAI.68.7.3990- 3997.2000.
    • (2000) Infect. Immun , vol.68 , pp. 3990-3997
    • Pericone, C.D.1    Overweg, K.2    Hermans, P.W.3    Weiser, J.N.4
  • 5
    • 77749239882 scopus 로고    scopus 로고
    • Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site
    • Ling J, Söll D. 2010. Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site. Proc. Natl. Acad. Sci. U. S. A. 107:4028-4033. http://dx.doi.org/10.1073/ pnas.1000315107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 4028-4033
    • Ling, J.1    Söll, D.2
  • 6
    • 0033118910 scopus 로고    scopus 로고
    • Oxidative stress
    • Storz G, Imlay JA. 1999. Oxidative stress. Curr. Opin. Microbiol. 2:188-194. http://dx.doi.org/10.1016/S1369-5274(99)80033-2.
    • (1999) Curr. Opin. Microbiol , vol.2 , pp. 188-194
    • Storz, G.1    Imlay, J.A.2
  • 7
    • 84875859494 scopus 로고    scopus 로고
    • Streptococcus pneumoniae and reactive oxygen species: An unusual approach to living with radicals
    • Yesilkaya H, Andisi VF, Andrew PW, Bijlsma JJ. 2013. Streptococcus pneumoniae and reactive oxygen species: an unusual approach to living with radicals. Trends Microbiol. 21:187-195. http://dx.doi.org/10.1016/ j.tim.2013.01.004.
    • (2013) Trends Microbiol , vol.21 , pp. 187-195
    • Yesilkaya, H.1    Andisi, V.F.2    Andrew, P.W.3    Bijlsma, J.J.4
  • 8
    • 0027255483 scopus 로고
    • Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases
    • Carter CW, Jr. 1993. Cognition, mechanism, and evolutionary relationships in aminoacyl-tRNA synthetases. Annu. Rev. Biochem. 62:715-748. http://dx.doi.org/10.1146/annurev.bi.62.070193.003435.
    • (1993) Annu. Rev. Biochem , vol.62 , pp. 715-748
    • Carter, C.W.1
  • 10
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
    • Cusack S, Berthet-Colominas C, Härtlein M, Nassar N, Leberman R. 1990. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347:249 -255. http://dx.doi.org/10.1038/347249a0.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Härtlein, M.3    Nassar, N.4    Leberman, R.5
  • 11
    • 0027851759 scopus 로고
    • Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: An update
    • Cusack S. 1993. Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: an update. Biochimie 75: 1077-1081. http://dx.doi.org/10.1016/0300-9084(93)90006-E.
    • (1993) Biochimie , vol.75 , pp. 1077-1081
    • Cusack, S.1
  • 12
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G, Delarue M, Poch O, Gangloff J, Moras D. 1990. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347:203-206. http://dx.doi.org/10.1038/ 347203a0.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 13
    • 0026075798 scopus 로고
    • Structural relationships and the classification of aminoacyl-tRNA synthetases
    • Burbaum JJ, Schimmel P. 1991. Structural relationships and the classification of aminoacyl-tRNA synthetases. J. Biol. Chem. 266:16965-16968.
    • (1991) J. Biol. Chem , vol.266 , pp. 16965-16968
    • Burbaum, J.J.1    Schimmel, P.2
  • 15
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba M, Soll D. 2000. Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69:617-650. http://dx.doi.org/10.1146/annurev.biochem.69.1.617.
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 17
    • 0037099498 scopus 로고    scopus 로고
    • Class I tyrosyltRNA synthetase has a class II mode of cognate tRNA recognition
    • Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S. 2002. Class I tyrosyltRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J. 21:3829-3840. http://dx.doi.org/10.1093/emboj/cdf373.
    • (2002) EMBO J , vol.21 , pp. 3829-3840
    • Yaremchuk, A.1    Kriklivyi, I.2    Tukalo, M.3    Cusack, S.4
  • 18
    • 0027369542 scopus 로고
    • Rules that govern tRNA identity in protein synthesis
    • McClain WH. 1993. Rules that govern tRNA identity in protein synthesis. J. Mol. Biol. 234:257-280. http://dx.doi.org/10.1006/jmbi.1993.1582.
    • (1993) J. Mol. Biol , vol.234 , pp. 257-280
    • McClain, W.H.1
  • 19
    • 33847023388 scopus 로고    scopus 로고
    • Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase
    • Guth EC, Francklyn CS. 2007. Kinetic discrimination of tRNA identity by the conserved motif 2 loop of a class II aminoacyl-tRNA synthetase. Mol. Cell 25:531-542. http://dx.doi.org/10.1016/j.molcel.2007.01.015.
    • (2007) Mol. Cell , vol.25 , pp. 531-542
    • Guth, E.C.1    Francklyn, C.S.2
  • 20
    • 70349545940 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis and translational quality control
    • Ling J, Reynolds N, Ibba M. 2009. Aminoacyl-tRNA synthesis and translational quality control. Annu. Rev. Microbiol. 63:61-78. http:// dx.doi.org/10.1146/annurev.micro.091208.073210.
    • (2009) Annu. Rev. Microbiol , vol.63 , pp. 61-78
    • Ling, J.1    Reynolds, N.2    Ibba, M.3
  • 21
    • 0017326738 scopus 로고
    • Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase
    • Fersht AR. 1977. Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase. Biochemistry 16:1025-1030. http://dx.doi.org/10.1021/bi00624a034.
    • (1977) Biochemistry , vol.16 , pp. 1025-1030
    • Fersht, A.R.1
  • 23
    • 0015500925 scopus 로고
    • Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine
    • Eldred EW, Schimmel PR. 1972. Rapid deacylation by isoleucyl transfer ribonucleic acid synthetase of isoleucine-specific transfer ribonucleic acid aminoacylated with valine. J. Biol. Chem. 247:2961-2964.
    • (1972) J. Biol. Chem , vol.247 , pp. 2961-2964
    • Eldred, E.W.1    Schimmel, P.R.2
  • 24
    • 0031000512 scopus 로고    scopus 로고
    • Discrete determinants in transfer RNA for editing and aminoacylation
    • Hale SP, Auld DS, Schmidt E, Schimmel P. 1997. Discrete determinants in transfer RNA for editing and aminoacylation. Science 276:1250-1252. http://dx.doi.org/10.1126/science.276.5316.1250.
    • (1997) Science , vol.276 , pp. 1250-1252
    • Hale, S.P.1    Auld, D.S.2    Schmidt, E.3    Schimmel, P.4
  • 25
    • 0033594814 scopus 로고    scopus 로고
    • Lyswith noncognate amino acids by lysyl-tRNA synthetase
    • Lyswith noncognate amino acids by lysyl-tRNA synthetase. Biochemistry 38:8088 - 8093. http:// dx.doi.org/10.1021/bi990629i.
    • (1999) Biochemistry , vol.38 , pp. 8088-8093
    • Jakubowski, H.1
  • 26
    • 84883488074 scopus 로고    scopus 로고
    • Direction of aminoacylated transfer RNAs into antibiotic synthesis and peptidoglycan-mediated antibiotic resistance
    • Shepherd J, Ibba M. 2013. Direction of aminoacylated transfer RNAs into antibiotic synthesis and peptidoglycan-mediated antibiotic resistance. FEBS Lett. 587:2895-2904. http://dx.doi.org/10.1016/ j.febslet.2013.07.036.
    • (2013) FEBS Lett , vol.587 , pp. 2895-2904
    • Shepherd, J.1    Ibba, M.2
  • 27
    • 84883697364 scopus 로고    scopus 로고
    • Lipid II-independent trans editing of mischarged tRNAs by the penicillin resistance factor MurM
    • Shepherd J, Ibba M. 2013. Lipid II-independent trans editing of mischarged tRNAs by the penicillin resistance factor MurM. J. Biol. Chem. 288:25915-25923. http://dx.doi.org/10.1074/jbc.M113.479824.
    • (2013) J. Biol. Chem , vol.288 , pp. 25915-25923
    • Shepherd, J.1    Ibba, M.2
  • 28
    • 0030885191 scopus 로고    scopus 로고
    • Aminoacyl thioester chemistry of class II aminoacyltRNA synthetases
    • Jakubowski H. 1997. Aminoacyl thioester chemistry of class II aminoacyltRNA synthetases. Biochemistry 36:11077-11085. http://dx.doi.org/ 10.1021/bi970589n.
    • (1997) Biochemistry , vol.36 , pp. 11077-11085
    • Jakubowski, H.1
  • 30
    • 0014027087 scopus 로고
    • Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase
    • Baldwin AN, Berg P. 1966. Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase. J. Biol. Chem. 241:839-845.
    • (1966) J. Biol. Chem , vol.241 , pp. 839-845
    • Baldwin, A.N.1    Berg, P.2
  • 31
    • 0033592915 scopus 로고    scopus 로고
    • Nucleotide determinants for tRNA-dependent amino acid discrimination by a class I tRNA synthetase
    • Farrow MA, Nordin BE, Schimmel P. 1999. Nucleotide determinants for tRNA-dependent amino acid discrimination by a class I tRNA synthetase. Biochemistry 38:16898-16903. http://dx.doi.org/10.1021/bi9920782.
    • (1999) Biochemistry , vol.38 , pp. 16898-16903
    • Farrow, M.A.1    Nordin, B.E.2    Schimmel, P.3
  • 33
    • 78449288755 scopus 로고    scopus 로고
    • Cellular mechanisms that control mistranslation
    • Reynolds NM, Lazazzera BA, Ibba M. 2010. Cellular mechanisms that control mistranslation. Nat. Rev. Microbiol. 8:849 - 856. http:// dx.doi.org/10.1038/nrmicro2472.
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 849-856
    • Reynolds, N.M.1    Lazazzera, B.A.2    Ibba, M.3
  • 34
    • 0017072607 scopus 로고
    • Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing
    • Fersht AR, Kaethner MM. 1976. Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing. Biochemistry 15:3342-3346. http://dx.doi.org/10.1021/ bi00660a026.
    • (1976) Biochemistry , vol.15 , pp. 3342-3346
    • Fersht, A.R.1    Kaethner, M.M.2
  • 35
    • 8144228074 scopus 로고    scopus 로고
    • The role of pneumolysin in pneumococcal pneumonia and meningitis
    • Hirst RA, Kadioglu A, O'Callaghan C, Andrew PW. 2004. The role of pneumolysin in pneumococcal pneumonia and meningitis. Clin. Exp. Immunol. 138:195-201. http://dx.doi.org/10.1111/j.1365- 2249.2004.02611.x.
    • (2004) Clin. Exp. Immunol , vol.138 , pp. 195-201
    • Hirst, R.A.1    Kadioglu, A.2    O'Callaghan, C.3    Andrew, P.W.4
  • 37
    • 0015157385 scopus 로고
    • Tissue amino acid flux after exposure of rats to Diplococcus pneumoniae
    • Wannemacher RW, Jr, Powanda MC, Pekarek RS, Beisel WR. 1971. Tissue amino acid flux after exposure of rats to Diplococcus pneumoniae. Infect. Immun. 4:556-562.
    • (1971) Infect. Immun , vol.4 , pp. 556-562
    • Wannemacher, R.W.1    Powanda, M.C.2    Pekarek, R.S.3    Beisel, W.R.4
  • 38
    • 0016257451 scopus 로고
    • Amino acid flux and protein synthesis after exposure of rats to either Diplococcus pneumoniae or Salmonella typhimurium
    • Wannemacher RW, Jr, Powanda MC, Dinterman RE. 1974. Amino acid flux and protein synthesis after exposure of rats to either Diplococcus pneumoniae or Salmonella typhimurium. Infect. Immun. 10:60-65.
    • (1974) Infect. Immun , vol.10 , pp. 60-65
    • Wannemacher, R.W.1    Powanda, M.C.2    Dinterman, R.E.3
  • 39
    • 0017698423 scopus 로고
    • Key role of various individual amino acids in host response to infection
    • Wannemacher RW, Jr. 1977. Key role of various individual amino acids in host response to infection. Am. J. Clin. Nutr. 30:1269-1280.
    • (1977) Am. J. Clin. Nutr , vol.30 , pp. 1269-1280
    • Wannemacher, R.W.1
  • 42
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou YM, Schimmel P. 1988. A simple structural feature is a major determinant of the identity of a transfer RNA. Nature 333:140-145. http:// dx.doi.org/10.1038/333140a0.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.M.1    Schimmel, P.2
  • 43
    • 0024295537 scopus 로고
    • Association of transfer RNA acceptor identity with a helical irregularity
    • McClain WH, Chen YM, Foss K, Schneider J. 1988. Association of transfer RNA acceptor identity with a helical irregularity. Science 242: 1681-1684. http://dx.doi.org/10.1126/science.2462282.
    • (1988) Science , vol.242 , pp. 1681-1684
    • McClain, W.H.1    Chen, Y.M.2    Foss, K.3    Schneider, J.4
  • 45
    • 0030886446 scopus 로고    scopus 로고
    • Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase
    • Beuning PJ, Yang F, Schimmel P, Musier-Forsyth K. 1997. Specific atomic groups and RNA helix geometry in acceptor stem recognition by a tRNA synthetase. Proc. Natl. Acad. Sci. U. S. A. 94:10150-10154. http:// dx.doi.org/10.1073/pnas.94.19.10150.
    • (1997) Proc. Natl. Acad. Sci. U. S. A , vol.94 , pp. 10150-10154
    • Beuning, P.J.1    Yang, F.2    Schimmel, P.3    Musier-Forsyth, K.4
  • 46
    • 0344624843 scopus 로고    scopus 로고
    • Increased overall antibiotic susceptibility in Staphylococcus aureus femAB null mutants
    • Ling B, Berger-Bächi B. 1998. Increased overall antibiotic susceptibility in Staphylococcus aureus femAB null mutants. Antimicrob. Agents Chemother. 42:936-938.
    • (1998) Antimicrob. Agents Chemother , vol.42 , pp. 936-938
    • Ling, B.1    Berger-Bächi, B.2
  • 48
    • 0344628644 scopus 로고    scopus 로고
    • Cell wall branches, penicillin resistance and the secrets of theMurMprotein
    • Fiser A, Filipe SR, Tomasz A. 2003. Cell wall branches, penicillin resistance and the secrets of theMurMprotein. Trends Microbiol. 11:547-553. http://dx.doi.org/10.1016/j.tim.2003.10.003.
    • (2003) Trends Microbiol , vol.11 , pp. 547-553
    • Fiser, A.1    Filipe, S.R.2    Tomasz, A.3
  • 49
    • 0034712839 scopus 로고    scopus 로고
    • Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes
    • Filipe SR, Tomasz A. 2000. Inhibition of the expression of penicillin resistance in Streptococcus pneumoniae by inactivation of cell wall muropeptide branching genes. Proc. Natl. Acad. Sci. U. S. A. 97:4891-4896. http://dx.doi.org/10.1073/pnas.080067697.
    • (2000) Proc. Natl. Acad. Sci. U. S. A , vol.97 , pp. 4891-4896
    • Filipe, S.R.1    Tomasz, A.2
  • 50
    • 0037022333 scopus 로고    scopus 로고
    • The murMN operon: A functional link between antibiotic resistance and antibiotic tolerance in Streptococcuspneumoniae
    • Filipe SR, Severina E, Tomasz A. 2002. The murMN operon: a functional link between antibiotic resistance and antibiotic tolerance in Streptococcuspneumoniae. Proc. Natl. Acad. Sci. U. S. A. 99:1550 -1555. http:// dx.doi.org/10.1073/pnas.032671699.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 1550-1555
    • Filipe, S.R.1    Severina, E.2    Tomasz, A.3
  • 51
    • 84888601034 scopus 로고    scopus 로고
    • Adaptive translation as a mechanism of stress response and adaptation
    • Pan T. 2013. Adaptive translation as a mechanism of stress response and adaptation. Annu. Rev. Genet. 47:121-137. http://dx.doi.org/10.1146/ annurev-genet-111212-133522.
    • (2013) Annu. Rev. Genet , vol.47 , pp. 121-137
    • Pan, T.1
  • 52
  • 53
    • 10644277147 scopus 로고    scopus 로고
    • Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase
    • Roy H, Ling J, Irnov M, Ibba M. 2004. Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase. EMBO J. 23:4639-4648. http://dx.doi.org/10.1038/sj.emboj.7600474.
    • (2004) EMBO J , vol.23 , pp. 4639-4648
    • Roy, H.1    Ling, J.2    Irnov, M.3    Ibba, M.4
  • 54
    • 17844402985 scopus 로고    scopus 로고
    • A mutation in T7 RNA polymerase that facilitates promoter clearance
    • Guillerez J, Lopez PJ, Proux F, Launay H, Dreyfus M. 2005. A mutation in T7 RNA polymerase that facilitates promoter clearance. Proc. Natl. Acad. Sci. U. S. A. 102:5958 -5963. http://dx.doi.org/10.1073/ pnas.0407141102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 5958-5963
    • Guillerez, J.1    Lopez, P.J.2    Proux, F.3    Launay, H.4    Dreyfus, M.5
  • 55
    • 0021107943 scopus 로고
    • Site-directed mutagenesis as a probe of enzyme structure and catalysis: Tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation
    • Wilkinson AJ, Fersht AR, Blow DM, Winter G. 1983. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry 22: 3581-3586. http://dx.doi.org/10.1021/bi00284a007.
    • (1983) Biochemistry , vol.22 , pp. 3581-3586
    • Wilkinson, A.J.1    Fersht, A.R.2    Blow, D.M.3    Winter, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.