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Volumn 8, Issue 7, 2013, Pages

Structural Studies of a Bacterial tRNAHIS Guanylyltransferase (Thg1)-Like Protein, with Nucleotide in the Activation and Nucleotidyl Transfer Sites

Author keywords

[No Author keywords available]

Indexed keywords

5' MONOPHOSPHORYLATED TRNA; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; BACTERIAL PROTEIN; BACTERIAL RNA; GUANOSINE TRIPHOSPHATE; HISTIDINE; NUCLEOTIDE; THG1 LIKE PROTEIN; TRANSFER RNA; TRNA GUANYLYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 84879771547     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0067465     Document Type: Article
Times cited : (15)

References (32)
  • 1
    • 84860004845 scopus 로고    scopus 로고
    • Doing it in reverse: 3′-to-5′ polymerization by the Thg1 superfamily
    • Jackman JE, Gott JM, Gray MW, (2012) Doing it in reverse: 3′-to-5′ polymerization by the Thg1 superfamily. RNA 18: 886-899.
    • (2012) RNA , vol.18 , pp. 886-899
    • Jackman, J.E.1    Gott, J.M.2    Gray, M.W.3
  • 2
    • 0348014687 scopus 로고    scopus 로고
    • tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5′ end of tRNAHis
    • Gu W, Jackman JE, Lohan AJ, Gray MW, Phizicky EM, (2003) tRNAHis maturation: an essential yeast protein catalyzes addition of a guanine nucleotide to the 5′ end of tRNAHis. Genes Dev 17: 2889-2901.
    • (2003) Genes Dev , vol.17 , pp. 2889-2901
    • Gu, W.1    Jackman, J.E.2    Lohan, A.J.3    Gray, M.W.4    Phizicky, E.M.5
  • 3
    • 84863393590 scopus 로고    scopus 로고
    • Kinetic analysis of 3′-5′ nucleotide addition catalyzed by eukaryotic tRNA(His) guanylyltransferase
    • Smith BA, Jackman JE, (2012) Kinetic analysis of 3′-5′ nucleotide addition catalyzed by eukaryotic tRNA(His) guanylyltransferase. Biochemistry 51: 453-465.
    • (2012) Biochemistry , vol.51 , pp. 453-465
    • Smith, B.A.1    Jackman, J.E.2
  • 4
    • 0026317972 scopus 로고
    • Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism
    • Jahn D, Pande S, (1991) Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism. J Biol Chem 266: 22832-22836.
    • (1991) J Biol Chem , vol.266 , pp. 22832-22836
    • Jahn, D.1    Pande, S.2
  • 5
    • 24344499742 scopus 로고    scopus 로고
    • Depletion of Saccharomyces cerevisiae tRNA(His) guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m(5)C
    • Gu W, Hurto RL, Hopper AK, Grayhack EJ, Phizicky EM, (2005) Depletion of Saccharomyces cerevisiae tRNA(His) guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m(5)C. Mol Cell Biol 25: 8191-8201.
    • (2005) Mol Cell Biol , vol.25 , pp. 8191-8201
    • Gu, W.1    Hurto, R.L.2    Hopper, A.K.3    Grayhack, E.J.4    Phizicky, E.M.5
  • 6
    • 77951171100 scopus 로고    scopus 로고
    • The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase
    • Preston MA, Phizicky EM, (2010) The requirement for the highly conserved G-1 residue of Saccharomyces cerevisiae tRNAHis can be circumvented by overexpression of tRNAHis and its synthetase. RNA 16: 1068-1077.
    • (2010) RNA , vol.16 , pp. 1068-1077
    • Preston, M.A.1    Phizicky, E.M.2
  • 7
    • 0343470264 scopus 로고
    • Post-transcriptional nucleotide addition is responsible for the formation of the 5′ terminus of histidine tRNA
    • Cooley L, Appel B, Söll D, (1982) Post-transcriptional nucleotide addition is responsible for the formation of the 5′ terminus of histidine tRNA. Proc Natl Acad Sci U S A 79: 6475-6479.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 6475-6479
    • Cooley, L.1    Appel, B.2    Söll, D.3
  • 9
    • 0022652241 scopus 로고
    • The additional guanylate at the 5′ terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P
    • Orellana O, Cooley L, Söll D, (1986) The additional guanylate at the 5′ terminus of Escherichia coli tRNAHis is the result of unusual processing by RNase P. Mol Cell Biol. 6: 525-529.
    • (1986) Mol Cell Biol , vol.6 , pp. 525-529
    • Orellana, O.1    Cooley, L.2    Söll, D.3
  • 10
    • 76249089296 scopus 로고    scopus 로고
    • Template-dependent 3′-5′ nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of life
    • Abad MG, Rao BS, Jackman JE, (2010) Template-dependent 3′-5′ nucleotide addition is a shared feature of tRNAHis guanylyltransferase enzymes from multiple domains of life. Proc Natl Acad Sci U S A 107: 674-679.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 674-679
    • Abad, M.G.1    Rao, B.S.2    Jackman, J.E.3
  • 11
    • 33745041683 scopus 로고    scopus 로고
    • tRNAHis guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G-1 addition
    • Jackman JE, Phizicky EM, (2006) tRNAHis guanylyltransferase catalyzes a 3′-5′ polymerization reaction that is distinct from G-1 addition. Proc Natl Acad Sci U S A 103: 8640-8645.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8640-8645
    • Jackman, J.E.1    Phizicky, E.M.2
  • 12
    • 79953016145 scopus 로고    scopus 로고
    • tRNA 5′-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from Bacteria and Archaea
    • Rao BS, Maris EL, Jackman JE, (2011) tRNA 5′-end repair activities of tRNAHis guanylyltransferase (Thg1)-like proteins from Bacteria and Archaea. Nucleic Acids Res 39: 1833-1842.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1833-1842
    • Rao, B.S.1    Maris, E.L.2    Jackman, J.E.3
  • 13
    • 79952998913 scopus 로고    scopus 로고
    • A role for tRNA(His) guanylyltransferase (Thg1)-like proteins from Dictyostelium discoideum in mitochondrial 5′-tRNA editing
    • Abad MG, Long Y, Willcox A, Gott JM, Gray MW, et al. (2011) A role for tRNA(His) guanylyltransferase (Thg1)-like proteins from Dictyostelium discoideum in mitochondrial 5′-tRNA editing. RNA 17: 613-623.
    • (2011) RNA , vol.17 , pp. 613-623
    • Abad, M.G.1    Long, Y.2    Willcox, A.3    Gott, J.M.4    Gray, M.W.5
  • 14
    • 0027500536 scopus 로고
    • Editing of transfer RNAs in Acanthamoeba castellanii mitochondria
    • Lonergan KM, Gray MW, (1993) Editing of transfer RNAs in Acanthamoeba castellanii mitochondria. Science 259: 812-816.
    • (1993) Science , vol.259 , pp. 812-816
    • Lonergan, K.M.1    Gray, M.W.2
  • 15
    • 0027220487 scopus 로고
    • Predicted editing of additional transfer RNAs in Acanthamoeba castellanii mitochondria
    • Lonergan KM, Gray MW, (1993) Predicted editing of additional transfer RNAs in Acanthamoeba castellanii mitochondria. Nucleic Acids Res 21: 4402.
    • (1993) Nucleic Acids Res , vol.21 , pp. 4402
    • Lonergan, K.M.1    Gray, M.W.2
  • 16
    • 78650524780 scopus 로고    scopus 로고
    • tRNA(His) guanylyltransferase (THG1), a unique 3′-5′ nucleotidyl transferase, shares unexpected structural homology with canonical 5′-3′ DNA polymerases
    • Hyde SJ, Eckenroth BE, Smith BA, Eberley WA, Heintz NH, et al. (2010) tRNA(His) guanylyltransferase (THG1), a unique 3′-5′ nucleotidyl transferase, shares unexpected structural homology with canonical 5′-3′ DNA polymerases. Proc Natl Acad Sci U S A 107: 20305-20310.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 20305-20310
    • Hyde, S.J.1    Eckenroth, B.E.2    Smith, B.A.3    Eberley, W.A.4    Heintz, N.H.5
  • 19
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: structural diversity and common mechanisms
    • Steitz TA, (1999) DNA polymerases: structural diversity and common mechanisms. J Biol Chem 274: 17395-17398.
    • (1999) J Biol Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 20
    • 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. Macromolecular Crystallography, Pt A 276: 307-326.
    • (1997) Macromolecular Crystallography, Pt A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT, (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2: 2728-2733.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 27
    • 0037779022 scopus 로고    scopus 로고
    • A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning
    • Padilla JE, Yeates TO, (2003) A statistic for local intensity differences: robustness to anisotropy and pseudo-centering and utility for detecting twinning. Acta Crystallogr D Biol Crystallogr 59: 1124-1130.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 1124-1130
    • Padilla, J.E.1    Yeates, T.O.2
  • 28
    • 36549053563 scopus 로고    scopus 로고
    • Characterizing a crystal from an initial native dataset
    • Sawaya MR, (2007) Characterizing a crystal from an initial native dataset. Methods Mol Biol 364: 95-120.
    • (2007) Methods Mol Biol , vol.364 , pp. 95-120
    • Sawaya, M.R.1
  • 29
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, 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.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 30
    • 42349104471 scopus 로고    scopus 로고
    • Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase
    • Jackman JE, Phizicky EM, (2008) Identification of critical residues for G-1 addition and substrate recognition by tRNA(His) guanylyltransferase. Biochemistry 47: 4817-4825.
    • (2008) Biochemistry , vol.47 , pp. 4817-4825
    • Jackman, J.E.1    Phizicky, E.M.2
  • 32
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • Doublié S, Tabor S, Long AM, Richardson CC, Ellenberger T, (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391: 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.