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Volumn 5, Issue , 2010, Pages

Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; BACTERIA (MICROORGANISMS); EUKARYOTA; FUNGI;

EID: 77955083310     PISSN: None     EISSN: 17456150     Source Type: Journal    
DOI: 10.1186/1745-6150-5-48     Document Type: Article
Times cited : (42)

References (28)
  • 1
    • 71549148346 scopus 로고    scopus 로고
    • TRNA as an active chemical scaffold for diverse chemical transformations
    • 10.1016/j.febslet.2009.11.045, 19925795
    • Francklyn CS, Minajigi A. tRNA as an active chemical scaffold for diverse chemical transformations. FEBS Lett 584(2):366-375. 10.1016/j.febslet.2009.11.045, 19925795.
    • FEBS Lett , vol.584 , Issue.2 , pp. 366-375
    • Francklyn, C.S.1    Minajigi, A.2
  • 2
  • 4
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • 10.1016/j.jmb.2003.08.040, 14568537
    • Leipe DD, Koonin EV, Aravind L. Evolution and classification of P-loop kinases and related proteins. J Mol Biol 2003, 333(4):781-815. 10.1016/j.jmb.2003.08.040, 14568537.
    • (2003) J Mol Biol , vol.333 , Issue.4 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 5
    • 77949274496 scopus 로고    scopus 로고
    • Diversity and evolution of chromatin proteins encoded by DNA viruses
    • de Souza RF, Iyer LM, Aravind L. Diversity and evolution of chromatin proteins encoded by DNA viruses. Biochim Biophys Acta 2009, 1799(3-4):302-318.
    • (2009) Biochim Biophys Acta , vol.1799 , Issue.3-4 , pp. 302-318
    • de Souza, R.F.1    Iyer, L.M.2    Aravind, L.3
  • 6
    • 33744951781 scopus 로고    scopus 로고
    • Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium
    • 10.1074/jbc.M600114200, 16510449
    • Bellais S, Arthur M, Dubost L, Hugonnet JE, Gutmann L, van Heijenoort J, Legrand R, Brouard JP, Rice L, Mainardi JL. Aslfm, the D-aspartate ligase responsible for the addition of D-aspartic acid onto the peptidoglycan precursor of Enterococcus faecium. J Biol Chem 2006, 281(17):11586-11594. 10.1074/jbc.M600114200, 16510449.
    • (2006) J Biol Chem , vol.281 , Issue.17 , 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    Mainardi, J.L.10
  • 7
    • 42449118064 scopus 로고    scopus 로고
    • RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors
    • 10.1073/pnas.0800006105, 2290796, 18305156
    • Roy H, Ibba M. RNA-dependent lipid remodeling by bacterial multiple peptide resistance factors. Proc Natl Acad Sci USA 2008, 105(12):4667-4672. 10.1073/pnas.0800006105, 2290796, 18305156.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.12 , pp. 4667-4672
    • Roy, H.1    Ibba, M.2
  • 8
    • 44349190780 scopus 로고    scopus 로고
    • Investigations of valanimycin biosynthesis: elucidation of the role of seryl-tRNA
    • 10.1073/pnas.0708957105, 2373340, 18451033
    • Garg RP, Qian XL, Alemany LB, Moran S, Parry RJ. Investigations of valanimycin biosynthesis: elucidation of the role of seryl-tRNA. Proc Natl Acad Sci USA 2008, 105(18):6543-6547. 10.1073/pnas.0708957105, 2373340, 18451033.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.18 , pp. 6543-6547
    • Garg, R.P.1    Qian, X.L.2    Alemany, L.B.3    Moran, S.4    Parry, R.J.5
  • 10
    • 0037018946 scopus 로고    scopus 로고
    • 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
    • 10.1021/bi012212u, 12033919
    • Sareen D, Steffek M, Newton GL, Fahey RC. 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 2002, 41(22):6885-6890. 10.1021/bi012212u, 12033919.
    • (2002) Biochemistry , vol.41 , Issue.22 , pp. 6885-6890
    • Sareen, D.1    Steffek, M.2    Newton, G.L.3    Fahey, R.C.4
  • 11
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • 10.1093/nar/25.17.3389, 146917, 9254694
    • Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997, 25(17):3389-3402. 10.1093/nar/25.17.3389, 146917, 9254694.
    • (1997) Nucleic Acids Res , vol.25 , Issue.17 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3    Zhang, J.4    Zhang, Z.5    Miller, W.6    Lipman, D.J.7
  • 12
    • 0032420333 scopus 로고    scopus 로고
    • JPred: a consensus secondary structure prediction server
    • 10.1093/bioinformatics/14.10.892, 9927721
    • Cuff JA, Clamp ME, Siddiqui AS, Finlay M, Barton GJ. JPred: a consensus secondary structure prediction server. Bioinformatics (Oxford, England) 1998, 14(10):892-893. 10.1093/bioinformatics/14.10.892, 9927721.
    • (1998) Bioinformatics (Oxford, England) , vol.14 , Issue.10 , pp. 892-893
    • Cuff, J.A.1    Clamp, M.E.2    Siddiqui, A.S.3    Finlay, M.4    Barton, G.J.5
  • 13
    • 0036643477 scopus 로고    scopus 로고
    • Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA
    • 10.1002/prot.10064, 12012333
    • Aravind L, Anantharaman V, Koonin EV. Monophyly of class I aminoacyl tRNA synthetase, USPA, ETFP, photolyase, and PP-ATPase nucleotide-binding domains: implications for protein evolution in the RNA. Proteins 2002, 48(1):1-14. 10.1002/prot.10064, 12012333.
    • (2002) Proteins , vol.48 , Issue.1 , pp. 1-14
    • Aravind, L.1    Anantharaman, V.2    Koonin, E.V.3
  • 14
    • 23144452044 scopus 로고    scopus 로고
    • The HHpred interactive server for protein homology detection and structure prediction
    • Web Server, 10.1093/nar/gki408, 1160169, 15980461
    • Soding J, Biegert A, Lupas AN. The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 2005, (33 Web Server):W244-248. 10.1093/nar/gki408, 1160169, 15980461.
    • (2005) Nucleic Acids Res , Issue.33
    • Soding, J.1    Biegert, A.2    Lupas, A.N.3
  • 15
    • 0032830481 scopus 로고    scopus 로고
    • Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events
    • Wolf YI, Aravind L, Grishin NV, Koonin EV. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res 1999, 9(8):689-710.
    • (1999) Genome Res , vol.9 , Issue.8 , pp. 689-710
    • Wolf, Y.I.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 17
    • 77955983722 scopus 로고    scopus 로고
    • Origin and evolution of peptide-modifying dioxygenases and identification of the wybutosine hydroxylase/hydroperoxidase
    • Iyer LM, Abhiman S, de Souza RF, Aravind L. Origin and evolution of peptide-modifying dioxygenases and identification of the wybutosine hydroxylase/hydroperoxidase. Nucleic Acids Res 2010,
    • (2010) Nucleic Acids Res
    • Iyer, L.M.1    Abhiman, S.2    de Souza, R.F.3    Aravind, L.4
  • 18
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • 10.1016/S0969-2126(96)00033-0, 8805533
    • Conti E, Franks NP, Brick P. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 1996, 4(3):287-298. 10.1016/S0969-2126(96)00033-0, 8805533.
    • (1996) Structure , vol.4 , Issue.3 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 19
    • 0035156443 scopus 로고    scopus 로고
    • Exploring the domain structure of modular nonribosomal peptide synthetases
    • 10.1016/S0969-2126(00)00560-8, 11342140
    • Weber T, Marahiel MA. Exploring the domain structure of modular nonribosomal peptide synthetases. Structure 2001, 9(1):R3-9. 10.1016/S0969-2126(00)00560-8, 11342140.
    • (2001) Structure , vol.9 , Issue.1
    • Weber, T.1    Marahiel, M.A.2
  • 20
    • 0028830908 scopus 로고
    • Bioactive cyclic dipeptides
    • 10.1016/0196-9781(94)00017-Z, 7716068
    • Prasad C. Bioactive cyclic dipeptides. Peptides 1995, 16(1):151-164. 10.1016/0196-9781(94)00017-Z, 7716068.
    • (1995) Peptides , vol.16 , Issue.1 , pp. 151-164
    • Prasad, C.1
  • 21
    • 34547664918 scopus 로고    scopus 로고
    • Analysis of the immune-related transcriptome of a lophotrochozoan model, the marine annelid Platynereis dumerilii
    • 10.1186/1742-9994-4-18, 1939704, 17617895
    • Altincicek B, Vilcinskas A. Analysis of the immune-related transcriptome of a lophotrochozoan model, the marine annelid Platynereis dumerilii. Front Zool 2007, 4:18. 10.1186/1742-9994-4-18, 1939704, 17617895.
    • (2007) Front Zool , vol.4 , pp. 18
    • Altincicek, B.1    Vilcinskas, A.2
  • 22
    • 0033055062 scopus 로고    scopus 로고
    • The use of gene clusters to infer functional coupling
    • 10.1073/pnas.96.6.2896, 15866, 10077608
    • Overbeek R, Fonstein M, D'Souza M, Pusch GD, Maltsev N. The use of gene clusters to infer functional coupling. Proc Natl Acad Sci USA 1999, 96(6):2896-2901. 10.1073/pnas.96.6.2896, 15866, 10077608.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.6 , pp. 2896-2901
    • Overbeek, R.1    Fonstein, M.2    D'Souza, M.3    Pusch, G.D.4    Maltsev, N.5
  • 23
    • 70350643410 scopus 로고    scopus 로고
    • The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis
    • 10.1039/b913092f, 19865642
    • Oves-Costales D, Kadi N, Challis GL. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem Commun (Camb) 2009, (43):6530-6541. 10.1039/b913092f, 19865642.
    • (2009) Chem Commun (Camb) , Issue.43 , pp. 6530-6541
    • Oves-Costales, D.1    Kadi, N.2    Challis, G.L.3
  • 24
    • 34247198471 scopus 로고    scopus 로고
    • Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain
    • 10.1016/j.chembiol.2007.02.005, 17462573
    • Llewellyn NM, Li Y, Spencer JB. Biosynthesis of butirosin: transfer and deprotection of the unique amino acid side chain. Chem Biol 2007, 14(4):379-386. 10.1016/j.chembiol.2007.02.005, 17462573.
    • (2007) Chem Biol , vol.14 , Issue.4 , pp. 379-386
    • Llewellyn, N.M.1    Li, Y.2    Spencer, J.B.3
  • 25
    • 10844269673 scopus 로고    scopus 로고
    • Portability of oxidase domains in nonribosomal peptide synthetase modules
    • 10.1021/bi0481139, 15595851
    • Schneider TL, Walsh CT. Portability of oxidase domains in nonribosomal peptide synthetase modules. Biochemistry 2004, 43(50):15946-15955. 10.1021/bi0481139, 15595851.
    • (2004) Biochemistry , vol.43 , Issue.50 , pp. 15946-15955
    • Schneider, T.L.1    Walsh, C.T.2
  • 26
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: the most functionally diverse protein superfamily?
    • 10.1016/j.phytochem.2003.08.016, 14697267
    • Dunwell JM, Purvis A, Khuri S. Cupins: the most functionally diverse protein superfamily?. Phytochemistry 2004, 65(1):7-17. 10.1016/j.phytochem.2003.08.016, 14697267.
    • (2004) Phytochemistry , vol.65 , Issue.1 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 27
    • 75749112037 scopus 로고    scopus 로고
    • Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism
    • 10.1021/bi901985b, 20052967
    • Grocholski T, Koskiniemi H, Lindqvist Y, Mantsala P, Niemi J, Schneider G. Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism. Biochemistry 49(5):934-944. 10.1021/bi901985b, 20052967.
    • Biochemistry , vol.49 , Issue.5 , pp. 934-944
    • Grocholski, T.1    Koskiniemi, H.2    Lindqvist, Y.3    Mantsala, P.4    Niemi, J.5    Schneider, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.