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Volumn 28, Issue 9, 2009, Pages 1362-1373

RNA helicase module in an acetyltransferase that modifies a specific tRNA anticodon

Author keywords

N4 acetylcytidine (ac4C); RNA acetyltransferase; TmcA; TRNA; Wobble modification

Indexed keywords

ACYLTRANSFERASE; ADENOSINE TRIPHOSPHATASE; CYTIDINE DERIVATIVE; DEAD BOX PROTEIN; N4 ACETYLCYTIDINE; RNA ACETYLTRANSFERASE; RNA HELICASE; TRANSFER RNA; UNCLASSIFIED DRUG; ACETYL COENZYME A; ADENOSINE DIPHOSPHATE;

EID: 65649134700     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2009.69     Document Type: Article
Times cited : (48)

References (40)
  • 1
    • 33846269602 scopus 로고    scopus 로고
    • tRNA's wobble decoding of the genome: 40 years of modification
    • Agris PF, Vendeix FA, Graham WD (2007) tRNA's wobble decoding of the genome: 40 years of modification. J Mol Biol 366: 1-13
    • (2007) J Mol Biol , vol.366 , pp. 1-13
    • Agris, P.F.1    Vendeix, F.A.2    Graham, W.D.3
  • 3
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA
    • Bono F, Ebert J, Lorentzen E, Conti E (2006) The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 126: 713-725
    • (2006) Cell , vol.126 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 4
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers JM, Johnson ER, McKay DB (2000) Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc Natl Acad Sci USA 97: 13080-13085
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 6
    • 33846186825 scopus 로고    scopus 로고
    • Structural and functional insights into the human Upf1 helicase core
    • Cheng Z, Muhlrad D, Lim MK, Parker R, Song H (2007) Structural and functional insights into the human Upf1 helicase core. EMBO J 26: 253-264
    • (2007) EMBO J , vol.26 , pp. 253-264
    • Cheng, Z.1    Muhlrad, D.2    Lim, M.K.3    Parker, R.4    Song, H.5
  • 7
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin O, Banroques J, Tanner NK, Linder P (2006) The DEAD-box protein family of RNA helicases. Gene 367: 17-37
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 8
    • 0029966338 scopus 로고    scopus 로고
    • Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture
    • Grosjean H, Edqvist J, Straby KB, Giege R (1996) Enzymatic formation of modified nucleosides in tRNA: dependence on tRNA architecture. J Mol Biol 255: 67-85
    • (1996) J Mol Biol , vol.255 , pp. 67-85
    • Grosjean, H.1    Edqvist, J.2    Straby, K.B.3    Giege, R.4
  • 9
    • 0035966271 scopus 로고    scopus 로고
    • Cocrystal structure of a tRNA Psi55 pseudouridine synthase: Nucleotide flipping by an RNA-modifying enzyme
    • Hoang C, Ferre-D'Amare AR (2001) Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme. Cell 107: 929-939
    • (2001) Cell , vol.107 , pp. 929-939
    • Hoang, C.1    Ferre-D'Amare, A.R.2
  • 10
    • 49949086040 scopus 로고    scopus 로고
    • The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon
    • Ikeuchi Y, Kitahara K, Suzuki T (2008) The RNA acetyltransferase driven by ATP hydrolysis synthesizes N4-acetylcytidine of tRNA anticodon. EMBO J 27: 2194-2203
    • (2008) EMBO J , vol.27 , pp. 2194-2203
    • Ikeuchi, Y.1    Kitahara, K.2    Suzuki, T.3
  • 11
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • Ikeuchi Y, Shigi N, Kato J, Nishimura A, Suzuki T (2006) Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol Cell 21: 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
  • 12
    • 22544480568 scopus 로고    scopus 로고
    • Molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition
    • Ikeuchi Y, Soma A, Ote T, Kato J, Sekine Y, Suzuki T (2005) Molecular mechanism of lysidine synthesis that determines tRNA identity and codon recognition. Mol Cell 19: 235-246
    • (2005) Mol Cell , vol.19 , pp. 235-246
    • Ikeuchi, Y.1    Soma, A.2    Ote, T.3    Kato, J.4    Sekine, Y.5    Suzuki, T.6
  • 15
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim JL, Morgenstern KA, Griffith JP, Dwyer MD, Thomson JA, Murcko MA, Lin C, Caron PR (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6: 89-100
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 16
    • 0034698144 scopus 로고    scopus 로고
    • p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism
    • Lau OD, Courtney AD, Vassilev A, Marzilli LA, Cotter RJ, Nakatani Y, Cole PA (2000) p300/CBP-associated factor histone acetyltransferase processing of a peptide substrate. Kinetic analysis of the catalytic mechanism. J Biol Chem 275: 21953-21959
    • (2000) J Biol Chem , vol.275 , pp. 21953-21959
    • Lau, O.D.1    Courtney, A.D.2    Vassilev, A.3    Marzilli, L.A.4    Cotter, R.J.5    Nakatani, Y.6    Cole, P.A.7
  • 17
    • 32244445417 scopus 로고    scopus 로고
    • Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA
    • Losey HC, Ruthenburg AJ, Verdine GL (2006) Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA. Nat Struct Mol Biol 13: 153-159
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 153-159
    • Losey, H.C.1    Ruthenburg, A.J.2    Verdine, G.L.3
  • 18
    • 0031832046 scopus 로고    scopus 로고
    • The RNA modification database - 1998
    • McCloskey JA, Crain PF (1998) The RNA modification database - 1998. Nucleic Acids Res 26: 196-197
    • (1998) Nucleic Acids Res , vol.26 , pp. 196-197
    • McCloskey, J.A.1    Crain, P.F.2
  • 19
    • 0023734317 scopus 로고
    • Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification
    • Muramatsu T, Nishikawa K, Nemoto F, Kuchino Y, Nishimura S, Miyazawa T, Yokoyama S (1988a) Codon and amino-acid specificities of a transfer RNA are both converted by a single post-transcriptional modification. Nature 336: 179-181
    • (1988) Nature , vol.336 , pp. 179-181
    • Muramatsu, T.1    Nishikawa, K.2    Nemoto, F.3    Kuchino, Y.4    Nishimura, S.5    Miyazawa, T.6    Yokoyama, S.7
  • 21
    • 33745596803 scopus 로고    scopus 로고
    • Ammonia channel couples glutaminase with transamidase reactions in GatCAB
    • Nakamura A, Yao M, Chimnaronk S, Sakai N, Tanaka I (2006) Ammonia channel couples glutaminase with transamidase reactions in GatCAB. Science 312: 1954-1958
    • (2006) Science , vol.312 , pp. 1954-1958
    • Nakamura, A.1    Yao, M.2    Chimnaronk, S.3    Sakai, N.4    Tanaka, I.5
  • 22
    • 33747125139 scopus 로고    scopus 로고
    • Snapshots of tRNA sulphuration via an adenylated intermediate
    • Numata T, Ikeuchi Y, Fukai S, Suzuki T, Nureki O (2006) Snapshots of tRNA sulphuration via an adenylated intermediate. Nature 442: 419-424
    • (2006) Nature , vol.442 , pp. 419-424
    • Numata, T.1    Ikeuchi, Y.2    Fukai, S.3    Suzuki, T.4    Nureki, O.5
  • 23
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause A, Sonenberg N (1992) Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J 11: 2643-2654
    • (1992) EMBO J , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 24
    • 0035918241 scopus 로고    scopus 로고
    • Further characterization of the helicase activity of eIF4A. Substrate specificity
    • Rogers Jr GW, Lima WF, Merrick WC (2001) Further characterization of the helicase activity of eIF4A. Substrate specificity. J Biol Chem 276: 12598-12608
    • (2001) J Biol Chem , vol.276 , pp. 12598-12608
    • Rogers Jr, G.W.1    Lima, W.F.2    Merrick, W.C.3
  • 27
    • 0030816674 scopus 로고    scopus 로고
    • The modified wobble base inosine in yeast tRNAIle is a positive determinant for aminoacylation by isoleucyl-tRNA synthetase
    • Senger B, Auxilien S, Englisch U, Cramer F, Fasiolo F (1997) The modified wobble base inosine in yeast tRNAIle is a positive determinant for aminoacylation by isoleucyl-tRNA synthetase. Biochemistry 36: 8269-8275
    • (1997) Biochemistry , vol.36 , pp. 8269-8275
    • Senger, B.1    Auxilien, S.2    Englisch, U.3    Cramer, F.4    Fasiolo, F.5
  • 28
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku T, Nureki O, Nakamura A, Kobayashi S, Yokoyama S (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125: 287-300
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 30
    • 11144222543 scopus 로고    scopus 로고
    • Crystal structure of the human ATP-dependent splicing and export factor UAP56
    • Shi H, Cordin O, Minder CM, Linder P, Xu RM (2004) Crystal structure of the human ATP-dependent splicing and export factor UAP56. Proc Natl Acad Sci USA 101: 17628-17633
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17628-17633
    • Shi, H.1    Cordin, O.2    Minder, C.M.3    Linder, P.4    Xu, R.M.5
  • 32
    • 0018082458 scopus 로고
    • The role of the minor base N4-acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA
    • Stern L, Schulman LH (1978) The role of the minor base N4-acetylcytidine in the function of the Escherichia coli noninitiator methionine transfer RNA. J Biol Chem 253: 6132-6139
    • (1978) J Biol Chem , vol.253 , pp. 6132-6139
    • Stern, L.1    Schulman, L.H.2
  • 33
    • 0035852638 scopus 로고    scopus 로고
    • Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii
    • Story RM, Li H, Abelson JN (2001) Crystal structure of a DEAD box protein from the hyperthermophile Methanococcus jannaschii. Proc Natl Acad Sci USA 98: 1465-1470
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1465-1470
    • Story, R.M.1    Li, H.2    Abelson, J.N.3
  • 34
    • 19444374782 scopus 로고    scopus 로고
    • Biosynthesis and function of tRNA wobble modifications
    • Grosjean H ed, New York: Springer-Verlag
    • Suzuki T (2005) Biosynthesis and function of tRNA wobble modifications. In Fine-Tuning of RNA Functions by Modification and Editing, Grosjean H (ed), Vol. 12, pp 24-69. New York: Springer-Verlag
    • (2005) Fine-Tuning of RNA Functions by Modification and Editing , vol.12 , pp. 24-69
    • Suzuki, T.1
  • 35
    • 0027273985 scopus 로고
    • A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase
    • Sylvers LA, Rogers KC, Shimizu M, Ohtsuka E, Soll D (1993) A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase. Biochemistry 32: 3836-3841
    • (1993) Biochemistry , vol.32 , pp. 3836-3841
    • Sylvers, L.A.1    Rogers, K.C.2    Shimizu, M.3    Ohtsuka, E.4    Soll, D.5
  • 36
    • 33646862141 scopus 로고    scopus 로고
    • Mutations in PRP43 that uncouple RNA-dependent NTPase activity and pre-mRNA splicing function
    • Tanaka N, Schwer B (2006) Mutations in PRP43 that uncouple RNA-dependent NTPase activity and pre-mRNA splicing function. Biochemistry 45: 6510-6521
    • (2006) Biochemistry , vol.45 , pp. 6510-6521
    • Tanaka, N.1    Schwer, B.2
  • 37
    • 0034698085 scopus 로고    scopus 로고
    • Kinetic mechanism of the histone acetyltransferase GCN5 from yeast
    • Tanner KG, Langer MR, Kim Y, Denu JM (2000) Kinetic mechanism of the histone acetyltransferase GCN5 from yeast. J Biol Chem 275: 22048-22055
    • (2000) J Biol Chem , vol.275 , pp. 22048-22055
    • Tanner, K.G.1    Langer, M.R.2    Kim, Y.3    Denu, J.M.4
  • 38
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: From generic motors to specific dissociation functions
    • Tanner NK, Linder P (2001) DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol Cell 8: 251-262
    • (2001) Mol Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 40
    • 33644872571 scopus 로고    scopus 로고
    • LAFIRE: Software for automating the refinement process of protein-structure analysis
    • Yao M, Zhou Y, Tanaka I (2006) LAFIRE: software for automating the refinement process of protein-structure analysis. Acta Crystallogr D Biol Crystallogr 62 (Part 2): 189-196
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , Issue.PART 2 , pp. 189-196
    • Yao, M.1    Zhou, Y.2    Tanaka, I.3


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