메뉴 건너뛰기




Volumn 39, Issue 10, 2011, Pages 4475-4489

Cyclodipeptide synthases, a family of class-I aminoacyl-tRNA synthetase-like enzymes involved in non-ribosomal peptide synthesis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; BACTERIAL PROTEIN; CYCLODIPEPTIDE SYNTHASE; MONOMER; PHENYLALANINE TRANSFER RNA; PROTEIN ALBC; PROTEIN TRPRSS; PROTEIN TYRRSS; SERINE; TRANSFER RNA; TYROSINE; UNCLASSIFIED DRUG; AMINOACYL TRANSFER RNA; CYCLOPEPTIDE; DIPEPTIDE; PEPTIDE SYNTHASE;

EID: 79961180475     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkr027     Document Type: Article
Times cited : (69)

References (59)
  • 2
    • 0034818822 scopus 로고    scopus 로고
    • Cyclic dipeptide oxidase from Streptomyces noursei: Isolation, purification and partial characterization of a novel, amino acyl α,β-dehydrogenase
    • DOI 10.1046/j.1432-1327.2001.02038.x
    • Gondry, M., Lautru, S., Fusai, G., Meunier, G., Ménez, A. and Genet, R. (2001) Cyclic dipeptide oxidase from Streptomyces noursei. Isolation, purification and partial characterization of a novel, amino acyl alpha, beta-dehydrogenase. Eur. J. Biochem., 268, 1712-1721. (Pubitemid 32862706)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.6 , pp. 1712-1721
    • Gondry, M.1    Lautru, S.2    Fusai, G.3    Meunier, G.4    Menez, A.5    Genet, R.6
  • 4
    • 65949089018 scopus 로고    scopus 로고
    • Charged tRNAs charge into secondary metabolism
    • von Döhren, H. (2009) Charged tRNAs charge into secondary metabolism. Nat. Chem. Biol., 5, 374-375.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 374-375
    • Von Döhren, H.1
  • 7
    • 71549148346 scopus 로고    scopus 로고
    • TRNA as an active chemical scaffold for diverse chemical transformations
    • Francklyn, C.S. and Minajigi, A. (2010) tRNA as an active chemical scaffold for diverse chemical transformations. FEBS Lett., 584, 366-375.
    • (2010) FEBS Lett. , vol.584 , pp. 366-375
    • Francklyn, C.S.1    Minajigi, A.2
  • 8
    • 39149095622 scopus 로고    scopus 로고
    • Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria
    • DOI 10.1111/j.1574-6976.2007.00097.x
    • Mainardi, J.L., Villet, R., Bugg, T.D., Mayer, C. and Arthur, M. (2008) Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria. FEMS Microbiol. Rev., 32, 386-408. (Pubitemid 351257816)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 386-408
    • Mainardi, J.-L.1    Villet, R.2    Bugg, T.D.3    Mayer, C.4    Arthur, M.5
  • 9
    • 35348938968 scopus 로고    scopus 로고
    • Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase
    • DOI 10.1038/nature06167, PII NATURE06167
    • Watanabe, K., Toh, Y., Suto, K., Shimizu, Y., Oka, N., Wada, T. and Tomita, K. (2007) Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase. Nature, 449, 867-871. (Pubitemid 47598606)
    • (2007) Nature , vol.449 , Issue.7164 , pp. 867-871
    • Watanabe, K.1    Toh, Y.2    Suto, K.3    Shimizu, Y.4    Oka, N.5    Wada, T.6    Tomita, K.7
  • 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
    • DOI 10.1016/S0969-2126(04)00009-7
    • Biarrotte-Sorin, S., Maillard, A.P., Delettré, 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. (Pubitemid 38224548)
    • (2004) Structure , vol.12 , Issue.2 , pp. 257-267
    • Biarrotte-Sorin, S.1    Maillard, A.P.2    Delettre, J.3    Sougakoff, W.4    Arthur, M.5    Mayer, C.6
  • 12
    • 77958156544 scopus 로고    scopus 로고
    • The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase
    • Vetting, M.W., Hegde, S.S. and Blanchard, J.S. (2010) The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase. Nat. Chem. Biol., 6, 797-799.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 797-799
    • Vetting, M.W.1    Hegde, S.S.2    Blanchard, J.S.3
  • 13
    • 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. and Moras, D. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature, 347, 203-206.
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 14
    • 0025043116 scopus 로고
    • A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5A
    • Cusack, S., Berthet-Colominas, C., Härtlein, M., Nassar, N. and Leberman, R. (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5A . Nature, 347, 249-255.
    • (1990) Nature , vol.347 , pp. 249-255
    • Cusack, S.1    Berthet-Colominas, C.2    Härtlein, M.3    Nassar, N.4    Leberman, R.5
  • 15
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • DOI 10.1016/S0968-0004(97)01052-9, PII S0968000497010529
    • Arnez, J.G. and Moras, D. (1997) Structural and functional considerations of the aminoacylation reaction. Trends Biochem. Sci., 22, 211-216. (Pubitemid 27246637)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.6 , pp. 211-216
    • Arnez, J.G.1    Moras, D.2
  • 16
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthesis
    • Ibba, M. and Söll, D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem., 69, 617-650.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 617-650
    • Ibba, M.1    Söll, D.2
  • 20
    • 37549039510 scopus 로고    scopus 로고
    • A short history of SHELX
    • Sheldrick, G.M. (2008) A short history of SHELX. Acta Crystallogr. A, 64, 112-122.
    • (2008) Acta Crystallogr. A , vol.64 , pp. 112-122
    • Sheldrick, G.M.1
  • 21
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein, C., Blanc, E., Roversi, P. and Bricogne, G. (2007) Automated structure solution with autoSHARP. Methods Mol. Biol., 364, 215-230. (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 22
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S.X., Lamzin, V.S. and Perrakis, A. (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7. Nat. Protoc., 3, 1171-1179.
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 25
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Krissinel, E. and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D Biol. Crystallogr., 60, 2256-2268. (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. and Richards, F.M. (1971) The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol., 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 27
    • 0015834475 scopus 로고
    • Comparison of super-secondary structures in proteins
    • Rao, S.T. and Rossmann, M.G. (1973) Comparison of super-secondary structures in proteins. J. Mol. Biol., 76, 241-256.
    • (1973) J. Mol. Biol. , vol.76 , pp. 241-256
    • Rao, S.T.1    Rossmann, M.G.2
  • 28
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • DOI 10.1006/jmbi.1993.1489
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol., 233, 123-138. (Pubitemid 23288916)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.1 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 30
    • 17744373680 scopus 로고    scopus 로고
    • Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L-tyrosine
    • DOI 10.1110/ps.041239305
    • Zhang, Y., Wang, L., Schultz, P.G. and Wilson, I.A. (2005) Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-Ltyrosine. Protein Sci., 14, 1340-1349. (Pubitemid 40577813)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1340-1349
    • Zhang, Y.1    Wang, L.2    Schultz, P.G.3    Wilson, I.A.4
  • 32
    • 33745794737 scopus 로고    scopus 로고
    • Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity
    • Shen, N., Guo, L., Yang, B., Jin, Y. and Ding, J. (2006) Structure of human tryptophanyl-tRNA synthetase in complex with tRNATrp reveals the molecular basis of tRNA recognition and specificity. Nucleic Acids Res., 34, 3246-3258.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3246-3258
    • Shen, N.1    Guo, L.2    Yang, B.3    Jin, Y.4    Ding, J.5
  • 33
    • 77953723081 scopus 로고    scopus 로고
    • Crystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: New insights into the mechanism of tryptophan activation and implications for anti-fungal drug design
    • Zhou, M., Dong, X., Shen, N., Zhong, C. and Ding, J. (2010) Crystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design. Nucleic Acids Res., 38, 3399-3413.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3399-3413
    • Zhou, M.1    Dong, X.2    Shen, N.3    Zhong, C.4    Ding, J.5
  • 34
    • 0023110653 scopus 로고
    • Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine
    • DOI 10.1016/0022-2836(87)90376-7
    • Brick, P. and Blow, D.M. (1987) Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine. J. Mol. Biol., 194, 287-297. (Pubitemid 17044524)
    • (1987) Journal of Molecular Biology , vol.194 , Issue.2 , pp. 287-297
    • Brick, P.1    Blow, D.M.2
  • 35
    • 0029643793 scopus 로고
    • Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase
    • Doublié, S., Bricogne, G., Gilmore, C. and Carter, C.W. Jr (1995) Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase. Structure, 3, 17-31.
    • (1995) Structure , vol.3 , pp. 17-31
    • Doublié, S.1    Bricogne, G.2    Gilmore, C.3    Carter Jr., C.W.4
  • 36
    • 0021746195 scopus 로고
    • Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase
    • Webster, T., Tsai, H., Kula, M., Mackie, G.A. and Schimmel, P. (1984) Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science, 226, 1315-1317. (Pubitemid 15215582)
    • (1984) Science , vol.226 , Issue.4680 , pp. 1315-1317
    • Webster, T.1    Tsai, H.2    Kula, M.3
  • 37
    • 0023645279 scopus 로고
    • Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases
    • Ludmerer, S.W. and Schimmel, P. (1987) Gene for yeast glutamine tRNA synthetase encodes a large amino-terminal extension and provides a strong confirmation of the signature sequence for a group of the aminoacyl-tRNA synthetases. J. Biol. Chem., 262, 10801-10806.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10801-10806
    • Ludmerer, S.W.1    Schimmel, P.2
  • 38
    • 0024392753 scopus 로고
    • Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution
    • Rould, M.A., Perona, J.J., Söll, D. and Steitz, T.A. (1989) Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8A resolution. Science, 246, 1135-1142. (Pubitemid 20012769)
    • (1989) Science , vol.246 , Issue.4934 , pp. 1135-1142
    • Rould, M.A.1    Perona, J.J.2    Soll, D.3    Steitz, T.A.4
  • 39
    • 0020992450 scopus 로고
    • Deletion mutagenesis using an 'M13 splint': The N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate
    • Waye, M.M., Winter, G., Wilkinson, A.J. and Fersht, A.R. (1983) Deletion mutagenesis using an 'M13 splint': the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate. EMBO J., 2, 1827-1829.
    • (1983) EMBO J. , vol.2 , pp. 1827-1829
    • Waye, M.M.1    Winter, G.2    Wilkinson, A.J.3    Fersht, A.R.4
  • 40
    • 0029788178 scopus 로고    scopus 로고
    • Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase
    • DOI 10.1074/jbc.271.37.22901
    • Abramochkin, G. and Shrader, T.E. (1996) Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase. J. Biol. Chem., 271, 22901-22907. (Pubitemid 26304741)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.37 , pp. 22901-22907
    • Abramochkin, G.1    Shrader, T.E.2
  • 42
    • 0022447254 scopus 로고
    • A model of synthetase/transfer RNA interaction as deduced by protein engineering
    • Bedouelle, H. and Winter, G. (1986) A model of synthetase/transfer RNA interaction as deduced by protein engineering. Nature, 320, 371-373. (Pubitemid 16077281)
    • (1986) Nature , vol.320 , Issue.6060 , pp. 371-373
    • Bedouelle, H.1    Winter, G.2
  • 43
    • 0024564289 scopus 로고
    • Structural and kinetic bases for the recognition of tRNA(Tyr) by tyrosyl-tRNA synthetase
    • DOI 10.1016/0022-2836(89)90317-3
    • Labouze, E. and Bedouelle, H. (1989) Structural and kinetic bases for the recognition of tRNATyr by tyrosyl-tRNA synthetase. J. Mol. Biol., 205, 729-735. (Pubitemid 19079344)
    • (1989) Journal of Molecular Biology , vol.205 , Issue.4 , pp. 729-735
    • Labouze, E.1    Bedouelle, H.2
  • 44
    • 0037099498 scopus 로고    scopus 로고
    • Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition
    • DOI 10.1093/emboj/cdf373
    • Yaremchuk, A., Kriklivyi, I., Tukalo, M. and Cusack, S. (2002) Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition. EMBO J., 21, 3829-3840. (Pubitemid 34787055)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3829-3840
    • Yaremchuk, A.1    Kriklivyi, I.2    Tukalo, M.3    Cusack, S.4
  • 46
    • 33745529250 scopus 로고    scopus 로고
    • Two conformations of a crystalline human tRNA synthetase-tRNA complex: Implications for protein synthesis
    • DOI 10.1038/sj.emboj.7601154, PII 7601154
    • Yang, X.L., Otero, F.J., Ewalt, K.L., Liu, J., Swairjo, M.A., Köhrer, C., RajBhandary, U.L., Skene, R.J., McRee, D.E. and Schimmel, P. (2006) Two conformations of a crystalline human tRNA synthetase-tRNA complex: implications for protein synthesis. EMBO J., 25, 2919-2929. (Pubitemid 43980398)
    • (2006) EMBO Journal , vol.25 , Issue.12 , pp. 2919-2929
    • Yang, X.-L.1    Otero, F.J.2    Ewalt, K.L.3    Liu, J.4    Swairjo, M.A.5    Kohrer, C.6    Rajbhandary, U.L.7    Skene, R.J.8    McRee, D.E.9    Schimmel, P.10
  • 47
    • 33845706511 scopus 로고    scopus 로고
    • Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
    • DOI 10.1038/sj.emboj.7601433, PII 7601433
    • 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. (Pubitemid 44967775)
    • (2006) EMBO Journal , vol.25 , Issue.24 , pp. 5942-5950
    • Suto, K.1    Shimizu, Y.2    Watanabe, K.3    Ueda, T.4    Fukai, S.5    Nureki, O.6    Tomita, K.7
  • 48
    • 34247589630 scopus 로고    scopus 로고
    • The Ribosomal Peptidyl Transferase
    • DOI 10.1016/j.molcel.2007.03.015, PII S1097276507001852
    • Beringer, M. and Rodnina, M.V. (2007) The ribosomal peptidyl transferase. Mol. Cell, 26, 311-321. (Pubitemid 46687094)
    • (2007) Molecular Cell , vol.26 , Issue.3 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 50
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • DOI 10.1016/S0968-0004(00)01553-X, PII S096800040001553X
    • Schimmel, P. and Ribas De Pouplana, L. (2000) Footprints of aminoacyl-tRNA synthetases are everywhere. Trends Biochem. Sci., 25, 207-209. (Pubitemid 30236212)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.5 , pp. 207-209
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 51
    • 0036849261 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases: Versatile players in the changing theater of translation
    • DOI 10.1017/S1355838202021180
    • Francklyn, C., Perona, J.J., Puetz, J. and Hou, Y.M. (2002) Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation. RNA, 8, 1363-1372. (Pubitemid 35332960)
    • (2002) RNA , vol.8 , Issue.11 , pp. 1363-1372
    • Francklyn, C.1    Perona, J.J.2    Puetz, J.3    Hou, Y.-M.4
  • 52
    • 0037018946 scopus 로고    scopus 로고
    • ATP-dependent L-cysteine: 1D-myo-inosityl 2-amino-2-deoxy-α-D- glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases
    • DOI 10.1021/bi012212u
    • Sareen, D., Steffek, M., Newton, G.L. and Fahey, R.C. (2002) ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases. Biochemistry, 41, 6885-6890. (Pubitemid 34575658)
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 6885-6890
    • Sareen, D.1    Steffek, M.2    Newton, G.L.3    Fahey, R.C.4
  • 53
    • 77955083310 scopus 로고    scopus 로고
    • Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis
    • Aravind, L., de Souza, R.F. and Iyer, L.M. (2010) Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis. Biol. Direct, 5, 48.
    • (2010) Biol. Direct , vol.5 , pp. 48
    • Aravind, L.1    De Souza, R.F.2    Iyer, L.M.3
  • 56
    • 48749101156 scopus 로고    scopus 로고
    • Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: Structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon
    • Blaise, M., Olieric, V., Sauter, C., Lorber, B., Roy, B., Karmakar, S., Banerjee, R., Becker, H.D. and Kern, D. (2008) Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon. J. Mol. Biol., 381, 1224-1237.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1224-1237
    • Blaise, M.1    Olieric, V.2    Sauter, C.3    Lorber, B.4    Roy, B.5    Karmakar, S.6    Banerjee, R.7    Becker, H.D.8    Kern, D.9
  • 57
    • 77957079227 scopus 로고    scopus 로고
    • Homologs of aminoacyl-tRNA synthetases acylate carrier proteins and provide a link between ribosomal and nonribosomal peptide synthesis
    • Mocibob, M., Ivic, N., Bilokapic, S., Maier, T., Luic, M., Ban, N. and Weygand-Durasevic, I. (2010) Homologs of aminoacyl-tRNA synthetases acylate carrier proteins and provide a link between ribosomal and nonribosomal peptide synthesis. Proc. Natl Acad. Sci. USA, 107, 14585-14590.
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 14585-14590
    • Mocibob, M.1    Ivic, N.2    Bilokapic, S.3    Maier, T.4    Luic, M.5    Ban, N.6    Weygand-Durasevic, I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.