메뉴 건너뛰기




Volumn 35, Issue 20, 2007, Pages 6870-6883

Idiosyncratic features in tRNAs participating in bacterial cell wall synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ALANINE TRANSFER RNA LIGASE; AMINO ACID; AMINOACYLTRANSFERASE; CYTOSINE; PEPTIDOGLYCAN; TRANSFER RNA;

EID: 36749012916     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm778     Document Type: Article
Times cited : (41)

References (37)
  • 1
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje,J.V. (1998) Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev., 62, 181-203.
    • (1998) Microbiol. Mol. Biol. Rev , vol.62 , pp. 181-203
    • Holtje, J.V.1
  • 2
    • 0035018011 scopus 로고    scopus 로고
    • Formation of the glycan chains in the synthesis of bacterial peptidoglycan
    • van Heijenoort,J. (2001) Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology, 11, 25R-36R.
    • (2001) Glycobiology , vol.11
    • van Heijenoort, J.1
  • 3
    • 33746891446 scopus 로고    scopus 로고
    • Penicillin binding proteins: Key players in bacterial cell cycle and drug resistance processes
    • Macheboeuf,P., Contreras-Martel,C., Job,V., Dideberg,O. and Dessen,A. (2006) Penicillin binding proteins: Key players in bacterial cell cycle and drug resistance processes. FEMS Microbiol. Rev., 30, 673-691.
    • (2006) FEMS Microbiol. Rev , vol.30 , pp. 673-691
    • Macheboeuf, P.1    Contreras-Martel, C.2    Job, V.3    Dideberg, O.4    Dessen, A.5
  • 4
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper,D.J. and Strominger,J.L. (1965) Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl Acad. Sci. USA, 54, 1133-1141.
    • (1965) Proc. Natl Acad. Sci. USA , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 5
    • 0036898699 scopus 로고    scopus 로고
    • Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent
    • table of contents
    • Goffin,C. and Ghuysen,J.M. (2002) Biochemistry and comparative genomics of SxxK superfamily acyltransferases offer a clue to the mycobacterial paradox: Presence of penicillin-susceptible target proteins versus lack of efficiency of penicillin as therapeutic agent. Microbiol. Mol. Biol. Rev., 66, 702-738, (table of contents).
    • (2002) Microbiol. Mol. Biol. Rev , vol.66 , pp. 702-738
    • Goffin, C.1    Ghuysen, J.M.2
  • 6
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer,K.H. and Kandler,O. (1972) Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev., 36, 407-477.
    • (1972) Bacteriol. Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 7
    • 0030741917 scopus 로고    scopus 로고
    • Presence of UDP-N acetylmuramyl-hexapeptides and -heptapeptides in enterococci and staphylococci after treatment with ramoplanin, tunicamycin, or vancomycin
    • Billot-Klein,D., Shlaes,D., Bryant,D., Bell,D., Legrand,R., Gutmann,L. and van Heijenoort,J. (1997) Presence of UDP-N acetylmuramyl-hexapeptides and -heptapeptides in enterococci and staphylococci after treatment with ramoplanin, tunicamycin, or vancomycin. J. Bacteriol., 179, 4684-4688.
    • (1997) J. Bacteriol , vol.179 , pp. 4684-4688
    • Billot-Klein, D.1    Shlaes, D.2    Bryant, D.3    Bell, D.4    Legrand, R.5    Gutmann, L.6    van Heijenoort, J.7
  • 8
    • 33744951781 scopus 로고    scopus 로고
    • Aslfm,t the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium
    • Bellais,S., Arthur,M., Dubost,L., Hugonnet,J.E., Gutmann,L., van Heijenoort,J., Legrand,R., Brouard,J.P., Rice,L. et al. (2006) Aslfm,t the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium. J. Biol. Chem., 281, 11586-11594.
    • (2006) J. Biol. Chem , vol.281 , pp. 11586-11594
    • Bellais, S.1    Arthur, M.2    Dubost, L.3    Hugonnet, J.E.4    Gutmann, L.5    van Heijenoort, J.6    Legrand, R.7    Brouard, J.P.8    Rice, L.9
  • 9
    • 0014962512 scopus 로고
    • Biosynthesis of the peptidoglycan of bacterial cell walls. XVII. Biosynthesis of peptidoglycan and of interpeptide bridges in Lactobacillus viridescens
    • Plapp,R. and Strominger,J.L. (1970) Biosynthesis of the peptidoglycan of bacterial cell walls. XVII. Biosynthesis of peptidoglycan and of interpeptide bridges in Lactobacillus viridescens. J. Biol. Chem., 245, 3667-3674.
    • (1970) J. Biol. Chem , vol.245 , pp. 3667-3674
    • Plapp, R.1    Strominger, J.L.2
  • 10
    • 0037416970 scopus 로고    scopus 로고
    • FemABX peptidyl transferases: A link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci
    • Rohrer,S. and Berger-Bachi,B. (2003) FemABX peptidyl transferases: A link between branched-chain cell wall peptide formation and beta-lactam resistance in gram-positive cocci. Antimicrob. Agents Chemother., 47, 837-846.
    • (2003) Antimicrob. Agents Chemother , vol.47 , pp. 837-846
    • Rohrer, S.1    Berger-Bachi, B.2
  • 11
    • 1242283845 scopus 로고    scopus 로고
    • Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: Insights into FemABX family substrates recognition
    • Biarrotte-Sorin,S., Maillard,A.P., Delettre,J., Sougakoff,W., Arthur,M. and Mayer,C. (2004) Crystal structures of Weissella viridescens FemX and its complex with UDP-MurNAc-pentapeptide: Insights into FemABX family substrates recognition. Structure, 12, 257-267.
    • (2004) Structure , vol.12 , pp. 257-267
    • Biarrotte-Sorin, S.1    Maillard, A.P.2    Delettre, J.3    Sougakoff, W.4    Arthur, M.5    Mayer, C.6
  • 13
    • 18944398046 scopus 로고    scopus 로고
    • Structure-based site-directed mutagcnesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens
    • Maillard,A.P., Biarrotte-Sorin,S., Villet,R., Mesnage,S., Bouhss,A., Sougakoff,W., Mayer,C. and Arthur,M. (2005) Structure-based site-directed mutagcnesis of the UDP-MurNAc-pentapeptide-binding cavity of the FemX alanyl transferase from Weissella viridescens. J. Bacteriol., 187, 3833-3838.
    • (2005) J. Bacteriol , vol.187 , pp. 3833-3838
    • Maillard, A.P.1    Biarrotte-Sorin, S.2    Villet, R.3    Mesnage, S.4    Bouhss, A.5    Sougakoff, W.6    Mayer, C.7    Arthur, M.8
  • 19
    • 0031659702 scopus 로고    scopus 로고
    • Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: Site-directed mutagenesis and characterization of the mutant enzymes
    • Pompeo,F., van Heijenoort,J. and Mengin-Lecreulx,D. (1998) Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes. J. Bacteriol., 180, 4799-4803.
    • (1998) J. Bacteriol , vol.180 , pp. 4799-4803
    • Pompeo, F.1    van Heijenoort, J.2    Mengin-Lecreulx, D.3
  • 21
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson,J.R. and Uhlenbeck,O.C. (1988) Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl Acad. Sci. USA, 85, 1033-1037.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 22
    • 0028982837 scopus 로고
    • Maturation of pre-tRNA(fMet) by Escherichia coli RNase P is specified by a guanosine of the 5′-flanking sequence
    • Meinnel,T. and Blanquet,S. (1995) Maturation of pre-tRNA(fMet) by Escherichia coli RNase P is specified by a guanosine of the 5′-flanking sequence. J. Biol. Chem., 270, 15908-15914.
    • (1995) J. Biol. Chem , vol.270 , pp. 15908-15914
    • Meinnel, T.1    Blanquet, S.2
  • 23
    • 0015980566 scopus 로고
    • Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var. zymogenes
    • Jacob,A.E. and Hobbs,S.J. (1974) Conjugal transfer of plasmid-borne multiple antibiotic resistance in Streptococcus faecalis var. zymogenes. J. Bacteriol., 117, 360-372.
    • (1974) J. Bacteriol , vol.117 , pp. 360-372
    • Jacob, A.E.1    Hobbs, S.J.2
  • 24
    • 0024822218 scopus 로고
    • The use of 5′-phospho-2 deoxyribocytidylylri-boadenosine as a facile route to chemical aminoacylation of tRNA
    • Robertson,S.A., Noren,C.J., Anthony-Cahill,S.J., Griffith,M.C. and Schultz,P.G. (1989) The use of 5′-phospho-2 deoxyribocytidylylri-boadenosine as a facile route to chemical aminoacylation of tRNA. Nucleic Acids Res., 17, 9649-9660.
    • (1989) Nucleic Acids Res , vol.17 , pp. 9649-9660
    • Robertson, S.A.1    Noren, C.J.2    Anthony-Cahill, S.J.3    Griffith, M.C.4    Schultz, P.G.5
  • 25
    • 0000849316 scopus 로고    scopus 로고
    • Misacylated transfer RNAs having a chemically removable protecting group
    • Lodder,M., Golovine,S., Laikhter,A.L., Karginov,V.A. and Hecht,S.M. (1998) Misacylated transfer RNAs having a chemically removable protecting group. J. Org. Chem., 63, 794-803.
    • (1998) J. Org. Chem , vol.63 , pp. 794-803
    • Lodder, M.1    Golovine, S.2    Laikhter, A.L.3    Karginov, V.A.4    Hecht, S.M.5
  • 26
    • 0033571581 scopus 로고    scopus 로고
    • Synthesis of aspartyl-tRNA(Asp) in Escherichia coli - a snapshot of the second step
    • Eiler,S., Dock-Bregeon,A., Moulinier,L., Thierry,J.C. and Moras,D. (1999) Synthesis of aspartyl-tRNA(Asp) in Escherichia coli - a snapshot of the second step. EMBO J., 18, 6532-6541.
    • (1999) EMBO J , vol.18 , pp. 6532-6541
    • Eiler, S.1    Dock-Bregeon, A.2    Moulinier, L.3    Thierry, J.C.4    Moras, D.5
  • 27
    • 33845706511 scopus 로고    scopus 로고
    • Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
    • Suto,K., Shimizu,Y., Watanabe,K., Ueda,T., Fukai,S., Nureki,O. and Tomita,K. (2006) Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog. EMBO J. 25, 5942-5950.
    • (2006) EMBO J , vol.25 , pp. 5942-5950
    • Suto, K.1    Shimizu, Y.2    Watanabe, K.3    Ueda, T.4    Fukai, S.5    Nureki, O.6    Tomita, K.7
  • 30
    • 0000932115 scopus 로고
    • A general and efficient route for chemical aminoacylation of transfer RNAs
    • Robertson,S.A., Ellman,J.A. and Schultz,P.G. (1991) A general and efficient route for chemical aminoacylation of transfer RNAs. J. Am. Chem. Soc., 113, 2722-2729.
    • (1991) J. Am. Chem. Soc , vol.113 , pp. 2722-2729
    • Robertson, S.A.1    Ellman, J.A.2    Schultz, P.G.3
  • 31
    • 3643114575 scopus 로고    scopus 로고
    • Universal rules and idiosyncratic features in tRNA identity
    • Giege,R., Sissler,M. and Florentz,C. (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res., 26 5017-5035.
    • (1998) Nucleic Acids Res , vol.26 , pp. 5017-5035
    • Giege, R.1    Sissler, M.2    Florentz, C.3
  • 32
    • 0024959463 scopus 로고    scopus 로고
    • Aminoacylation of RNA minihelices with alanine
    • Francklyn,C. and Schimmel,P. (1999) Aminoacylation of RNA minihelices with alanine. Nature, 337, 478-481.
    • (1999) Nature , vol.337 , pp. 478-481
    • Francklyn, C.1    Schimmel, P.2
  • 33
    • 1842526080 scopus 로고    scopus 로고
    • Positional recognition of a tRNA determinant dependent on a peptide insertion
    • Lovato,M.A., Swairjo,M.A. and Schimmel,P. (2004) Positional recognition of a tRNA determinant dependent on a peptide insertion. Mol. Cell, 13, 843-851.
    • (2004) Mol. Cell , vol.13 , pp. 843-851
    • Lovato, M.A.1    Swairjo, M.A.2    Schimmel, P.3
  • 35
    • 0344142531 scopus 로고    scopus 로고
    • Crystal structure of acceptor stem of tRNA(Ala) from Escherichia coli shows unique G.U wobble base pair at 1.16 A resolution
    • Mueller,U., Schubel,H., Sprinzl,M. and Heinemann,U. (1999) Crystal structure of acceptor stem of tRNA(Ala) from Escherichia coli shows unique G.U wobble base pair at 1.16 A resolution. RNA, 5 670-677.
    • (1999) RNA , vol.5 , pp. 670-677
    • Mueller, U.1    Schubel, H.2    Sprinzl, M.3    Heinemann, U.4
  • 36
    • 34248993209 scopus 로고    scopus 로고
    • The 51-63 base pair of tRNA confers specificity for binding by EF-Tu
    • Sanderson,L.E. and Uhlenbeck,O.C. (2007) The 51-63 base pair of tRNA confers specificity for binding by EF-Tu. RNA, 13, 835-840.
    • (2007) RNA , vol.13 , pp. 835-840
    • Sanderson, L.E.1    Uhlenbeck, O.C.2
  • 37
    • 0034762821 scopus 로고    scopus 로고
    • Recent advances in the formation of the bacterial peptidoglycan monomer unit
    • van Heijenoort,J. (2001) Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep., 18, 503-519.
    • (2001) Nat. Prod. Rep , vol.18 , pp. 503-519
    • van Heijenoort, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.