메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

An Appended Domain Results in an Unusual Architecture for Malaria Parasite Tryptophanyl-tRNA Synthetase

Author keywords

[No Author keywords available]

Indexed keywords

TRYPTOPHAN TRANSFER RNA LIGASE;

EID: 84878950023     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066224     Document Type: Article
Times cited : (24)

References (35)
  • 1
    • 84856408211 scopus 로고    scopus 로고
    • WHO, Geneva, Switzerland
    • WHO (2011) World Malaria Report. Geneva, Switzerland.
    • (2011) World Malaria Report
  • 3
    • 75449119681 scopus 로고    scopus 로고
    • A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite Plasmodium falciparum
    • Bhatt TK, Kapil C, Khan S, Jairajpuri MA, Sharma V, et al. (2009) A genomic glimpse of aminoacyl-tRNA synthetases in malaria parasite Plasmodium falciparum. BMC Genomics 10: 644.
    • (2009) BMC Genomics , vol.10 , pp. 644
    • Bhatt, T.K.1    Kapil, C.2    Khan, S.3    Jairajpuri, M.A.4    Sharma, V.5
  • 4
    • 82555196544 scopus 로고    scopus 로고
    • Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses
    • Bhatt TK, Khan S, Dwivedi VP, Banday MM, Sharma A, et al. (2011) Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses. Nature Communications 2: 530.
    • (2011) Nature Communications , vol.2 , pp. 530
    • Bhatt, T.K.1    Khan, S.2    Dwivedi, V.P.3    Banday, M.M.4    Sharma, A.5
  • 6
    • 84862286628 scopus 로고    scopus 로고
    • Selective and Specific Inhibition of the Plasmodium falciparum Lysyl-tRNA Synthetase by the Fungal Secondary Metabolite Cladosporin
    • Hoepfner D, McNamara CW, Lim CS, Studer C, Riedl R, et al. (2012) Selective and Specific Inhibition of the Plasmodium falciparum Lysyl-tRNA Synthetase by the Fungal Secondary Metabolite Cladosporin. Cell Host & Microbe 11: 654-663.
    • (2012) Cell Host & Microbe , vol.11 , pp. 654-663
    • Hoepfner, D.1    McNamara, C.W.2    Lim, C.S.3    Studer, C.4    Riedl, R.5
  • 7
    • 0033782994 scopus 로고    scopus 로고
    • Aminoacyl-tRNA Synthesis
    • Ibba M, Soll D, (2000) Aminoacyl-tRNA Synthesis. Annu Rev Biochem 69: 617-50.
    • (2000) Annu Rev Biochem , vol.69 , pp. 617-650
    • Ibba, M.1    Soll, D.2
  • 8
    • 0346848759 scopus 로고    scopus 로고
    • On the Evolution of Structure in Aminoacyl-tRNA Synthetases
    • O'Donoghue P, Luthey-Schulten Z, (2003) On the Evolution of Structure in Aminoacyl-tRNA Synthetases. Microbiol & Mol Biol Rev 67: 550-573.
    • (2003) Microbiol & Mol Biol Rev , vol.67 , pp. 550-573
    • O'Donoghue, P.1    Luthey-Schulten, Z.2
  • 9
    • 0029099218 scopus 로고
    • Eleven down and nine to go
    • Cusack S, (1995) Eleven down and nine to go. Nat Struct Mol Biol 2: 824-831.
    • (1995) Nat Struct Mol Biol , vol.2 , pp. 824-831
    • Cusack, S.1
  • 10
    • 0037255536 scopus 로고    scopus 로고
    • Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations
    • Retailleau P, Huang X, Yin Y, Hu M, Weinreb V, et al. (2003) Interconversion of ATP binding and conformational free energies by tryptophanyl-tRNA synthetase: structures of ATP bound to open and closed, pre-transition-state conformations. J Mol Biol 325: 39-63.
    • (2003) J Mol Biol , vol.325 , pp. 39-63
    • Retailleau, P.1    Huang, X.2    Yin, Y.3    Hu, M.4    Weinreb, V.5
  • 11
    • 1542349274 scopus 로고    scopus 로고
    • Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment-insights into substrate recognition, tRNA binding, and angiogenesis activity
    • Yu Y, Liu Y, Shen N, Xu X, Xu F, et al. (2004) Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment-insights into substrate recognition, tRNA binding, and angiogenesis activity. J Biol Chem 279: 8378-88.
    • (2004) J Biol Chem , vol.279 , pp. 8378-8388
    • Yu, Y.1    Liu, Y.2    Shen, N.3    Xu, X.4    Xu, F.5
  • 12
  • 14
    • 0027818737 scopus 로고
    • Mammalian tryptophanyl-tRNA synthetases
    • Kisselev LL, (1993) Mammalian tryptophanyl-tRNA synthetases. Biochimie 75: 1027-1039.
    • (1993) Biochimie , vol.75 , pp. 1027-1039
    • Kisselev, L.L.1
  • 15
    • 0742270603 scopus 로고    scopus 로고
    • A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase
    • Kise Y, Lee SW, Park SG, Fukai S, Sengoku T, et al. (2004) A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase. Nat Struct Mol Biol 11: 149-56.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 149-156
    • Kise, Y.1    Lee, S.W.2    Park, S.G.3    Fukai, S.4    Sengoku, T.5
  • 16
    • 0027159055 scopus 로고
    • Interferon inducibility of mammalian tryptophanyl-tRNA synthetase: new perspectives
    • Kisselev L, Frolova L, Haenni AL, (1993) Interferon inducibility of mammalian tryptophanyl-tRNA synthetase: new perspectives. Trends Biochem Sci 18: 263-267.
    • (1993) Trends Biochem Sci , vol.18 , pp. 263-267
    • Kisselev, L.1    Frolova, L.2    Haenni, A.L.3
  • 17
    • 0028951169 scopus 로고
    • Differential regulation of the human, interferon inducible tryptophanyl-tRNA synthetase by various cytokines in cell lines
    • Fleckner J, Martensen PM, Tolstrup AB, Kjeldgaard NO, Justesen J, (1995) Differential regulation of the human, interferon inducible tryptophanyl-tRNA synthetase by various cytokines in cell lines. Cytokine 7: 70-77.
    • (1995) Cytokine , vol.7 , pp. 70-77
    • Fleckner, J.1    Martensen, P.M.2    Tolstrup, A.B.3    Kjeldgaard, N.O.4    Justesen, J.5
  • 19
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • Schimmel P, Ribas De Pouplana L, (2000) Footprints of aminoacyl-tRNA synthetases are everywhere. Trends Biochem Sci 25: 207-209.
    • (2000) Trends Biochem Sci , vol.25 , pp. 207-209
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 20
    • 33947302386 scopus 로고    scopus 로고
    • Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii
    • Fukunaga R, Yokoyama S, (2007) Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii. Acta Crystallogr D Biol Crystallogr. 63: 390-400.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 390-400
    • Fukunaga, R.1    Yokoyama, S.2
  • 22
    • 84859739785 scopus 로고    scopus 로고
    • Uneven spread of cis- and trans-editing aminoacyl-tRNA synthetase domains within translational compartments of P. falciparum
    • Khan S, Sharma A, Jamwal A, Sharma V, Pole AK, et al. (2011) Uneven spread of cis- and trans-editing aminoacyl-tRNA synthetase domains within translational compartments of P. falciparum. Sci Rep 1: 188.
    • (2011) Sci Rep , vol.1 , pp. 188
    • Khan, S.1    Sharma, A.2    Jamwal, A.3    Sharma, V.4    Pole, A.K.5
  • 24
    • 0037246674 scopus 로고    scopus 로고
    • PlasmoDB: the Plasmodium genome resource. A database integrating experimental and computational data
    • Bahl A, Brunk B, Crabtree J, Fraunholz MJ, Gajria B, et al. (2003) PlasmoDB: the Plasmodium genome resource. A database integrating experimental and computational data. Nucleic Acids Res 31: 212-5.
    • (2003) Nucleic Acids Res , vol.31 , pp. 212-215
    • Bahl, A.1    Brunk, B.2    Crabtree, J.3    Fraunholz, M.J.4    Gajria, B.5
  • 25
    • 3343010591 scopus 로고    scopus 로고
    • Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method
    • Tonkin CJ, van Dooren GG, Spurck TP, Struck NS, Good RT, et al. (2004) Localization of organellar proteins in Plasmodium falciparum using a novel set of transfection vectors and a new immunofluorescence fixation method. Mol Biochem Parasitol 137: 13-21.
    • (2004) Mol Biochem Parasitol , vol.137 , pp. 13-21
    • Tonkin, C.J.1    van Dooren, G.G.2    Spurck, T.P.3    Struck, N.S.4    Good, R.T.5
  • 26
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson JR, Uhlenbeck OC, (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
  • 27
    • 0021030608 scopus 로고
    • Anticodon loop size and sequence requirements for recognition of formylmethionine tRNA by methionyl-tRNA synthetase
    • Schulman LH, Pelka H, (1983) Anticodon loop size and sequence requirements for recognition of formylmethionine tRNA by methionyl-tRNA synthetase. Proc Natl Acad Sci USA 80: 6755-6759.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 6755-6759
    • Schulman, L.H.1    Pelka, H.2
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 276: 307-326.
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 30
  • 32
    • 68449088258 scopus 로고    scopus 로고
    • The C-Ala domain brings together editing and aminoacylation functions on one tRNA
    • Guo M, Chong YE, Beebe K, Shapiro R, Yang XL, et al. (2009) The C-Ala domain brings together editing and aminoacylation functions on one tRNA. Science 325: 744-747.
    • (2009) Science , vol.325 , pp. 744-747
    • Guo, M.1    Chong, Y.E.2    Beebe, K.3    Shapiro, R.4    Yang, X.L.5
  • 33
    • 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, (1999) Evolution of aminoacyl-tRNA synthetases analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res 9: 689-710.
    • (1999) Genome Res , vol.9 , pp. 689-710
    • Wolf, Y.I.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 34
    • 0034141480 scopus 로고    scopus 로고
    • A recurrent RNA binding domain is appended to eukaryotic aminoacyl-tRNA synthetases
    • Cahuzac B, Berthonneau E, Birlirakis N, Guittet E, Mirande M, (2000) A recurrent RNA binding domain is appended to eukaryotic aminoacyl-tRNA synthetases. EMBO J 19: 445-52.
    • (2000) EMBO J , vol.19 , pp. 445-452
    • Cahuzac, B.1    Berthonneau, E.2    Birlirakis, N.3    Guittet, E.4    Mirande, M.5
  • 35
    • 66649089722 scopus 로고    scopus 로고
    • Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization
    • Naganumaa M, Sekinea S-i, Fukunagaa R, Yokoyamaa S, (2009) Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization. Proc Natl Acad Sci USA 106: 8489-8494.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8489-8494
    • Naganumaa, M.1    Sekinea, S.-i.2    Fukunagaa, R.3    Yokoyamaa, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.