메뉴 건너뛰기




Volumn 14, Issue 2, 2006, Pages 357-366

Structural basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SUBUNIT; RNA; SULFUR;

EID: 32044441001     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.11.009     Document Type: Article
Times cited : (43)

References (38)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • J.P. Abrahams, and A.G.W. Leslie Methods used in the structure determination of bovine mitochondrial F1 ATPase Acta Crystallogr. D Biol. Crystallogr. 52 1996 30 42
    • (1996) Acta Crystallogr. D Biol. Crystallogr. , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 3
    • 0003695480 scopus 로고    scopus 로고
    • Transfer RNA recognition by aminoacyl-tRNA synthetases
    • P.J. Beuning, and K. Musier-Forsyth Transfer RNA recognition by aminoacyl-tRNA synthetases Biopolymers 52 1999 1 28
    • (1999) Biopolymers , vol.52 , pp. 1-28
    • Beuning, P.J.1    Musier-Forsyth, K.2
  • 4
    • 0002495140 scopus 로고
    • Biosynthesis and function of modified nucleosides
    • D. Söll U.L. RajBhandary ASM Press Washington, DC
    • G.R. Björk Biosynthesis and function of modified nucleosides D. Söll U.L. RajBhandary tRNA: Structure, Biosynthesis, and Function 1995 ASM Press Washington, DC 165 205
    • (1995) TRNA: Structure, Biosynthesis, and Function , pp. 165-205
    • Björk, G.R.1
  • 5
    • 0035449350 scopus 로고    scopus 로고
    • Translational misreading: A tRNA modification counteracts a +2 ribosomal frameshift
    • D. Bregeon, V. Colot, M. Radman, and F. Taddei Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift Genes Dev. 15 2001 2295 2306
    • (2001) Genes Dev. , vol.15 , pp. 2295-2306
    • Bregeon, D.1    Colot, V.2    Radman, M.3    Taddei, F.4
  • 9
    • 14544272337 scopus 로고    scopus 로고
    • Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum
    • C. Dahl, S. Engels, A.S. Pott-Sperling, A. Schulte, J. Sander, Y. Lübbe, O. Deuster, and D.C. Brune Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum J. Bacteriol. 187 2005 1392 1404
    • (2005) J. Bacteriol. , vol.187 , pp. 1392-1404
    • Dahl, C.1    Engels, S.2    Pott-Sperling, A.S.3    Schulte, A.4    Sander, J.5    Lübbe, Y.6    Deuster, O.7    Brune, D.C.8
  • 10
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • E. de La Fortelle, and G. Bricogne Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods Enzymol. 276 1997 472 494
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 11
    • 0021770444 scopus 로고
    • Novel E. coli mutants deficient in biosynthesis of 5-methylaminomethyl-2- thiouridine
    • D. Elseviers, L.A. Petrullo, and P.J. Gallagher Novel E. coli mutants deficient in biosynthesis of 5-methylaminomethyl-2-thiouridine Nucleic Acids Res. 12 1984 3521 3534
    • (1984) Nucleic Acids Res. , vol.12 , pp. 3521-3534
    • Elseviers, D.1    Petrullo, L.A.2    Gallagher, P.J.3
  • 12
    • 0034115404 scopus 로고    scopus 로고
    • Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
    • R.A. Fabianek, H. Hennecke, and L. Thony-Meyer Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli FEMS Microbiol. Rev. 24 2000 303 316
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 303-316
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 14
    • 0023664535 scopus 로고
    • Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities
    • T.G. Hagervall, C.G. Edmonds, J.A. McCloskey, and G.R. Björk Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities J. Biol. Chem. 262 1987 8488 8495
    • (1987) J. Biol. Chem. , vol.262 , pp. 8488-8495
    • Hagervall, T.G.1    Edmonds, C.G.2    McCloskey, J.A.3    Björk, G.R.4
  • 15
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 16
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Y. Ikeuchi, N. Shigi, J. Kato, A. Nishimura, and T. Suzuki Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions Mol. Cell 21 2006 97 108
    • (2006) Mol. Cell , vol.21 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.3    Nishimura, A.4    Suzuki, T.5
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 1991 110 119
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 0034646676 scopus 로고    scopus 로고
    • Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • R. Kambampati, and C.T. Lauhon Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA J. Biol. Chem. 275 2000 10727 10730
    • (2000) J. Biol. Chem. , vol.275 , pp. 10727-10730
    • Kambampati, R.1    Lauhon, C.T.2
  • 19
    • 0037417771 scopus 로고    scopus 로고
    • MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli
    • R. Kambampati, and C.T. Lauhon MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli Biochemistry 42 2003 1109 1117
    • (2003) Biochemistry , vol.42 , pp. 1109-1117
    • Kambampati, R.1    Lauhon, C.T.2
  • 20
    • 0034711380 scopus 로고    scopus 로고
    • High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division
    • E. Katoh, T. Hatta, H. Shindo, Y. Ishii, H. Yamada, T. Mizuno, and T. Yamazaki High precision NMR structure of YhhP, a novel Escherichia coli protein implicated in cell division J. Mol. Biol. 304 2000 219 229
    • (2000) J. Mol. Biol. , vol.304 , pp. 219-229
    • Katoh, E.1    Hatta, T.2    Shindo, H.3    Ishii, Y.4    Yamada, H.5    Mizuno, T.6    Yamazaki, T.7
  • 21
    • 0030839446 scopus 로고    scopus 로고
    • Synthesis and studies on the effect of 2-thiouridine and 4-thiouridine on sugar conformation and RNA duplex stability
    • R.K. Kumar, and D.R. Davis Synthesis and studies on the effect of 2-thiouridine and 4-thiouridine on sugar conformation and RNA duplex stability Nucleic Acids Res. 25 1997 1272 1280
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1272-1280
    • Kumar, R.K.1    Davis, D.R.2
  • 23
    • 0036952614 scopus 로고    scopus 로고
    • Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli
    • C.T. Lauhon Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli J. Bacteriol. 184 2002 6820 6829
    • (2002) J. Bacteriol. , vol.184 , pp. 6820-6829
    • Lauhon, C.T.1
  • 24
    • 0035823572 scopus 로고    scopus 로고
    • The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA
    • E.G. Mueller, P.M. Palenchar, and C.J. Buck The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA J. Biol. Chem. 276 2001 33588 33595
    • (2001) J. Biol. Chem. , vol.276 , pp. 33588-33595
    • Mueller, E.G.1    Palenchar, P.M.2    Buck, C.J.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • A. Perrakis, R. Morris, and V.S. Lamzin Automated protein model building combined with iterative structure refinement Nat. Struct. Biol. 6 1999 458 463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 27
    • 0031855745 scopus 로고    scopus 로고
    • Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur
    • A.S. Pott, and C. Dahl Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur Microbiol. 144 1998 1881 1894
    • (1998) Microbiol. , vol.144 , pp. 1881-1894
    • Pott, A.S.1    Dahl, C.2
  • 29
    • 0036292374 scopus 로고    scopus 로고
    • Crystal structure of a conserved hypothetical protein from Escherichia coli
    • D.H. Shin, H. Yokota, R. Kim, and S.-H. Kim Crystal structure of a conserved hypothetical protein from Escherichia coli J. Struct. Funct. Genomics 2 2002 53 66
    • (2002) J. Struct. Funct. Genomics , vol.2 , pp. 53-66
    • Shin, D.H.1    Yokota, H.2    Kim, R.3    Kim, S.-H.4
  • 30
    • 0021941805 scopus 로고
    • Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2-thiouridine
    • M.A. Sullivan, J.F. Cannon, F.H. Webb, and R.M. Bock Antisuppressor mutation in Escherichia coli defective in biosynthesis of 5-methylaminomethyl-2- thiouridine J. Bacteriol. 161 1985 368 376
    • (1985) J. Bacteriol. , vol.161 , pp. 368-376
    • Sullivan, M.A.1    Cannon, J.F.2    Webb, F.H.3    Bock, R.M.4
  • 31
    • 0037011177 scopus 로고    scopus 로고
    • Taurine as a constituent of mitochondrial tRNAs: New insights into the functions of taurine and human mitochondrial diseases
    • T. Suzuki, T. Suzuki, T. Wada, K. Saigo, and K. Watanabe Taurine as a constituent of mitochondrial tRNAs: new insights into the functions of taurine and human mitochondrial diseases EMBO J. 21 2002 6581 6589
    • (2002) EMBO J. , vol.21 , pp. 6581-6589
    • Suzuki, T.1    Suzuki, T.2    Wada, T.3    Saigo, K.4    Watanabe, K.5
  • 32
    • 0027273985 scopus 로고
    • A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase
    • L.A. Sylvers, K.C. Rogers, M. Shimizu, E. Ohtsuka, and D. Söll A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase Biochemistry 32 1993 3836 3841
    • (1993) Biochemistry , vol.32 , pp. 3836-3841
    • Sylvers, L.A.1    Rogers, K.C.2    Shimizu, M.3    Ohtsuka, E.4    Söll, D.5
  • 33
    • 0015927336 scopus 로고
    • Biosynthesis of 5-methylaminomethyl-2-thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-methylaminomethyl-2-thiouridylate
    • Y. Taya, and S. Nishimura Biosynthesis of 5-methylaminomethyl-2- thiouridylate. I. Isolation of a new tRNA-methylase specific for 5-methylaminomethyl-2-thiouridylate Biochem. Biophys. Res. Commun. 51 1973 1062 1068
    • (1973) Biochem. Biophys. Res. Commun. , vol.51 , pp. 1062-1068
    • Taya, Y.1    Nishimura, S.2
  • 34
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • J. Urbonavicius, Q. Qian, J.M. Durand, T.G. Hagervall, and G.R. Björk Improvement of reading frame maintenance is a common function for several tRNA modifications EMBO J. 20 2001 4863 4873
    • (2001) EMBO J. , vol.20 , pp. 4863-4873
    • Urbonavicius, J.1    Qian, Q.2    Durand, J.M.3    Hagervall, T.G.4    Björk, G.R.5
  • 35
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • C.M. Weeks, and R. Miller The design and implementation of SnB v2.0 J. Appl. Crystallogr. 32 1999 120 124
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 36
    • 0002365884 scopus 로고
    • Modified nucleosides and codon recognition
    • D. Söll U.L. RajBhandary ASM Press Washington, DC
    • S. Yokoyama, and S. Nishimura Modified nucleosides and codon recognition D. Söll U.L. RajBhandary tRNA: Structure, Biosynthesis, and Function 1995 ASM Press Washington, DC 207 224
    • (1995) TRNA: Structure, Biosynthesis, and Function , pp. 207-224
    • Yokoyama, S.1    Nishimura, S.2
  • 37
    • 0018788007 scopus 로고
    • 1H NMR studies on the conformational characteristics of 2-thiopyrimidine nucleotides found in transfer RNAs
    • 1H NMR studies on the conformational characteristics of 2-thiopyrimidine nucleotides found in transfer RNAs Nucleic Acids Res. 6 1979 2611 2626
    • (1979) Nucleic Acids Res. , vol.6 , pp. 2611-2626
    • Yokoyama, S.1    Yamaizumi, Z.2    Nishimura, S.3    Miyazawa, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.