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Volumn 19, Issue 3, 2011, Pages 282-291

Mechanism-based strategies for trapping and crystallizing complexes of RNA-modifying enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DEAMINASE; DOUBLE STRANDED RNA; ENZYME; FLUOROPYRIMIDINE; METHYLTRANSFERASE; MICRORNA; PSEUDOURIDINE; RNA; S ADENOSYLMETHIONINE; TRANSFER RNA;

EID: 79952472839     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.01.005     Document Type: Review
Times cited : (8)

References (58)
  • 1
    • 1242309517 scopus 로고    scopus 로고
    • Decoding the genome: A modified view
    • Agris, P.F. (2004). Decoding the genome: a modified view. Nucleic Acids Res. 32, 223-238.
    • (2004) Nucleic Acids Res , vol.32 , pp. 223-238
    • Agris, P.F.1
  • 2
    • 44349185734 scopus 로고    scopus 로고
    • Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases
    • Alian, A., Lee, T.T., Griner, S.L., Stroud, R.M., and Finer-Moore, J. (2008). Structure of a TrmA-RNA complex: a consensus RNA fold contributes to substrate selectivity and catalysis in m5U methyltransferases. Proc. Natl. Acad. Sci. USA 105, 6876-6881.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6876-6881
    • Alian, A.1    Lee, T.T.2    Griner, S.L.3    Stroud, R.M.4    Finer-Moore, J.5
  • 3
    • 67349200973 scopus 로고    scopus 로고
    • Crystal structure of an RluF-RNA complex: A base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome
    • Alian, A., DeGiovanni, A., Griner, S.L., Finer-Moore, J.S., and Stroud, R.M. (2009). Crystal structure of an RluF-RNA complex: a base-pair rearrangement is the key to selectivity of RluF for U2604 of the ribosome. J. Mol. Biol. 388, 785-800.
    • (2009) J. Mol. Biol. , vol.388 , pp. 785-800
    • Alian, A.1    DeGiovanni, A.2    Griner, S.L.3    Finer-Moore, J.S.4    Stroud, R.M.5
  • 5
    • 0141618449 scopus 로고    scopus 로고
    • Caught in the act of modifying tRNA
    • Correll, C.C. (2003). Caught in the act of modifying tRNA. Nat. Struct. Biol. 10, 772-773.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 772-773
    • Correll, C.C.1
  • 6
    • 0029116609 scopus 로고
    • tRNA-guanine transglycosylase from Escherichia coli. Minimal tRNA structure and sequence requirements for recognition
    • Curnow, A.W., and Garcia, G.A. (1995). tRNA-guanine transglycosylase from Escherichia coli. Minimal tRNA structure and sequence requirements for recognition. J. Biol. Chem. 270, 17264-17267.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17264-17267
    • Curnow, A.W.1    Garcia, G.A.2
  • 7
    • 0027370662 scopus 로고
    • Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: Evidence for stable base modification-dependent conformers
    • Derrick, W.B., and Horowitz, J. (1993). Probing structural differences between native and in vitro transcribed Escherichia coli valine transfer RNA: evidence for stable base modification-dependent conformers. Nucleic Acids Res. 21, 4948-4953. (Pubitemid 23330172)
    • (1993) Nucleic Acids Research , vol.21 , Issue.21 , pp. 4948-4953
    • Derrick, W.B.1    Horowitz, J.2
  • 9
    • 70349813956 scopus 로고    scopus 로고
    • Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation
    • Goto-Ito, S., Ito, T., Kuratani, M., Bessho, Y., and Yokoyama, S. (2009). Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation. Nat. Struct. Mol. Biol. 16, 1109-1115.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1109-1115
    • Goto-Ito, S.1    Ito, T.2    Kuratani, M.3    Bessho, Y.4    Yokoyama, S.5
  • 11
    • 0029966338 scopus 로고    scopus 로고
    • Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture
    • Grosjean, H., Edqvist, J., Straby, K.B., and Giegé, 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    Giegé, R.4
  • 12
    • 0025726470 scopus 로고
    • The T-arm of tRNA is a substrate for tRNA (m5U54)-methyltransferase
    • Gu, X.R., and Santi, D.V. (1991). The T-arm of tRNA is a substrate for tRNA (m5U54)-methyltransferase. Biochemistry 30, 2999-3002.
    • (1991) Biochemistry , vol.30 , pp. 2999-3002
    • Gu, X.R.1    Santi, D.V.2
  • 13
    • 0033435203 scopus 로고    scopus 로고
    • The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA
    • Gu, X., Liu, Y., and Santi, D.V. (1999). The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA. Proc. Natl. Acad. Sci. USA 96, 14270-14275.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14270-14275
    • Gu, X.1    Liu, Y.2    Santi, D.V.3
  • 14
    • 0024309855 scopus 로고
    • Structure of an unmodified tRNA molecule
    • Hall, K.B., Sampson, J.R., Uhlenbeck, O.C., and Redfield, A.G. (1989). Structure of an unmodified tRNA molecule. Biochemistry 28, 5794-5801. (Pubitemid 19183715)
    • (1989) Biochemistry , vol.28 , Issue.14 , pp. 5794-5801
    • Hall, K.B.1    Sampson, J.R.2    Uhlenbeck, O.C.3    Redfield, A.G.4
  • 15
    • 33749357492 scopus 로고    scopus 로고
    • Mechanistic investigations of the pseudouridine synthase RluA using RNA containing 5-fluorouridine
    • DOI 10.1021/bi061293x
    • Hamilton, C.S., Greco, T.M., Vizthum, C.A., Ginter, J.M., Johnston, M.V., and Mueller, E.G. (2006). Mechanistic investigations of the pseudouridine synthase RluA using RNA containing 5-fluorouridine. Biochemistry 45, 12029-12038. (Pubitemid 44497828)
    • (2006) Biochemistry , vol.45 , Issue.39 , pp. 12029-12038
    • Hamilton, C.S.1    Greco, T.M.2    Vizthum, C.A.3    Ginter, J.M.4    Johnston, M.V.5    Mueller, E.G.6
  • 16
  • 17
    • 74049154427 scopus 로고    scopus 로고
    • The box H/ACA ribonucleoprotein complex: Interplay of RNA and protein structures in post-transcriptional RNA modification
    • Hamma, T., and Ferré-D'Amaré, A.R. (2010). The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification. J. Biol. Chem. 285, 805-809.
    • (2010) J. Biol. Chem. , vol.285 , pp. 805-809
    • Hamma, T.1    Ferré-D'Amaré, A.R.2
  • 18
    • 0035966271 scopus 로고    scopus 로고
    • Cocrystal structure of a tRNA Psi55 pseudouridine synthase: Nucleotide flipping by an RNA-modifying enzyme
    • DOI 10.1016/S0092-8674(01)00618-3
    • Hoang, C., and Ferré-D'Amaré, A.R. (2001). Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme. Cell 107, 929-939. (Pubitemid 34084983)
    • (2001) Cell , vol.107 , Issue.7 , pp. 929-939
    • Hoang, C.1    Ferre-D'Amare, A.R.2
  • 19
    • 23644435149 scopus 로고    scopus 로고
    • Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain
    • DOI 10.1110/ps.051493605
    • Hoang, C., Hamilton, C.S., Mueller, E.G., and Ferré- D'Amaré, A.R. (2005). Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domain. Protein Sci. 14, 2201-2206. (Pubitemid 41132385)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2201-2206
    • Hoang, C.1    Hamilton, C.S.2    Mueller, E.G.3    Ferre-D'Amare, A.R.4
  • 20
    • 33751013845 scopus 로고    scopus 로고
    • Crystal structure of pseudouridine synthase RluA: Indirect sequence readout through protein-induced RNA structure
    • DOI 10.1016/j.molcel.2006.09.017
    • Hoang, C., Chen, J., Vizthum, C.A., Kandel, J.M., Hamilton, C.S., Mueller, E.G., and Ferré-D'Amaré, A.R. (2006). Crystal structure of pseudouridine synthase RluA: indirect sequence readout through protein-induced RNA structure. Mol. Cell 24, 535-545. (Pubitemid 350284223)
    • (2006) Molecular Cell , vol.24 , Issue.4 , pp. 535-545
    • Hoang, C.1    Chen, J.2    Vizthum, C.A.3    Kandel, J.M.4    Hamilton, C.S.5    Mueller, E.G.6    Ferre-D'Amare, A.R.7
  • 21
    • 0031431078 scopus 로고    scopus 로고
    • RNA crystallography
    • Holbrook, S.R., and Kim, S.H. (1997). RNA crystallography. Biopolymers 44, 3-21.
    • (1997) Biopolymers , vol.44 , pp. 3-21
    • Holbrook, S.R.1    Kim, S.H.2
  • 22
    • 0032488657 scopus 로고    scopus 로고
    • A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst
    • DOI 10.1021/bi971874+
    • Huang, L., Pookanjanatavip, M., Gu, X., and Santi, D.V. (1998). A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst. Biochemistry 37, 344-351. (Pubitemid 28049138)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 344-351
    • Huang, L.1    Pookanjanatavip, M.2    Gu, X.3    Santi, D.V.4
  • 23
    • 34247199024 scopus 로고    scopus 로고
    • How U38, 39, and 40 of Many tRNAs Become the Targets for Pseudouridylation by TruA
    • DOI 10.1016/j.molcel.2007.02.027, PII S1097276507001451
    • Hur, S., and Stroud, R.M. (2007). How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Mol. Cell 26, 189-203. (Pubitemid 46617334)
    • (2007) Molecular Cell , vol.26 , Issue.2 , pp. 189-203
    • Hur, S.1    Stroud, R.M.2
  • 24
    • 0038613099 scopus 로고    scopus 로고
    • Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme
    • DOI 10.1016/S0092-8674(03)00280-0
    • Ishitani, R., Nureki, O., Nameki, N., Okada, N., Nishimura, S., and Yokoyama, S. (2003). Alternative tertiary structure of tRNA for recognition by a posttranscriptional modification enzyme. Cell 113, 383-394. (Pubitemid 36556119)
    • (2003) Cell , vol.113 , Issue.3 , pp. 383-394
    • Ishitani, R.1    Nureki, O.2    Nameki, N.3    Okada, N.4    Nishimura, S.5    Yokoyama, S.6
  • 25
    • 44949173836 scopus 로고    scopus 로고
    • Structure, dynamics, and function of RNA modification enzymes
    • Ishitani, R., Yokoyama, S., and Nureki, O. (2008). Structure, dynamics, and function of RNA modification enzymes. Curr. Opin. Struct. Biol. 18, 330-339.
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 330-339
    • Ishitani, R.1    Yokoyama, S.2    Nureki, O.3
  • 26
    • 43049099252 scopus 로고    scopus 로고
    • An embarrassment of riches: The enzymology of RNA modification
    • Iwata-Reuyl, D. (2008). An embarrassment of riches: the enzymology of RNA modification. Curr. Opin. Chem. Biol. 12, 126-133.
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 126-133
    • Iwata-Reuyl, D.1
  • 27
    • 77951974177 scopus 로고    scopus 로고
    • Structural aspects of messenger RNA reading frame maintenance by the ribosome
    • Jenner, L.B., Demeshkina, N., Yusupova, G., and Yusupov, M. (2010). Structural aspects of messenger RNA reading frame maintenance by the ribosome. Nat. Struct. Mol. Biol. 17, 555-560.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 555-560
    • Jenner, L.B.1    Demeshkina, N.2    Yusupova, G.3    Yusupov, M.4
  • 28
    • 0038475918 scopus 로고    scopus 로고
    • A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya
    • DOI 10.1261/rna.5230603
    • Kaya, Y., and Ofengand, J. (2003). A novel unanticipated type of pseudouridine synthase with homologs in bacteria, archaea, and eukarya. RNA 9, 711-721. (Pubitemid 36618199)
    • (2003) RNA , vol.9 , Issue.6 , pp. 711-721
    • Kaya, Y.1    Ofengand, J.2
  • 29
    • 0028650333 scopus 로고
    • Enzymatic mechanism of tRNA (m5U54)methyltransferase
    • Kealey, J.T., Gu, X., and Santi, D.V. (1994). Enzymatic mechanism of tRNA (m5U54)methyltransferase. Biochimie 76, 1133-1142.
    • (1994) Biochimie , vol.76 , pp. 1133-1142
    • Kealey, J.T.1    Gu, X.2    Santi, D.V.3
  • 30
    • 77749329940 scopus 로고    scopus 로고
    • Box H/ACA small ribonucleoproteins
    • Kiss, T., Fayet-Lebaron, E., and Jady, B.E. (2010). Box H/ACA small ribonucleoproteins. Mol. Cell 37, 597-606.
    • (2010) Mol. Cell , vol.37 , pp. 597-606
    • Kiss, T.1    Fayet-Lebaron, E.2    Jady, B.E.3
  • 31
    • 0029945504 scopus 로고    scopus 로고
    • Pseudouridine synthases: Four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases
    • Koonin, E.V. (1996). Pseudouridine synthases: four families of enzymes containing a putative uridine-binding motif also conserved in dUTPases and dCTP deaminases. Nucleic Acids Res. 24, 2411-2415.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2411-2415
    • Koonin, E.V.1
  • 32
    • 0033529290 scopus 로고    scopus 로고
    • A distinctive RNA fold: The solution structure of an analogue of the yeast tRNAPhe T Psi C domain
    • Koshlap, K.M., Guenther, R., Sochacka, E., Malkiewicz, A., and Agris, P.F. (1999). A distinctive RNA fold: the solution structure of an analogue of the yeast tRNAPhe T Psi C domain. Biochemistry 38, 8647-8656.
    • (1999) Biochemistry , vol.38 , pp. 8647-8656
    • Koshlap, K.M.1    Guenther, R.2    Sochacka, E.3    Malkiewicz, A.4    Agris, P.F.5
  • 34
    • 14844293080 scopus 로고    scopus 로고
    • A unique RNA fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function
    • DOI 10.1016/j.cell.2004.12.037
    • Lee, T.T., Agarwalla, S., and Stroud, R.M. (2005). A unique RNA Fold in the RumA-RNA-cofactor ternary complex contributes to substrate selectivity and enzymatic function. Cell 120, 599-611. (Pubitemid 40343073)
    • (2005) Cell , vol.120 , Issue.5 , pp. 599-611
    • Lee, T.T.1    Agarwalla, S.2    Stroud, R.M.3
  • 35
    • 34347402424 scopus 로고    scopus 로고
    • Complexes of tRNA and maturation enzymes: Shaping up for translation
    • Li, H. (2007). Complexes of tRNA and maturation enzymes: shaping up for translation. Curr. Opin. Struct. Biol. 17, 293-301.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 293-301
    • Li, H.1
  • 36
    • 67650340746 scopus 로고    scopus 로고
    • Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA
    • Liang, B., Zhou, J., Kahen, E., Terns, R.M., Terns, M.P., and Li, H. (2009). Structure of a functional ribonucleoprotein pseudouridine synthase bound to a substrate RNA. Nat. Struct. Mol. Biol. 16, 740-746.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 740-746
    • Liang, B.1    Zhou, J.2    Kahen, E.3    Terns, R.M.4    Terns, M.P.5    Li, H.6
  • 37
    • 0034682446 scopus 로고    scopus 로고
    • m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts
    • Liu, Y., and Santi, D.V. (2000). m5C RNA and m5C DNA methyl transferases use different cysteine residues as catalysts. Proc. Natl. Acad. Sci. USA 97, 8263-8265.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8263-8265
    • Liu, Y.1    Santi, D.V.2
  • 38
    • 32244445417 scopus 로고    scopus 로고
    • Crystal structure of Staphylococcus aureus tRNA adenosine deaminase TadA in complex with RNA
    • Losey, H.C., Ruthenburg, A.J., and Verdine, G.L. (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
  • 39
    • 35148886286 scopus 로고    scopus 로고
    • Crystal structure of human Pus10, a novel pseudouridine synthase
    • McCleverty, C.J., Hornsby, M., Spraggon, G., and Kreusch, A. (2007). Crystal structure of human Pus10, a novel pseudouridine synthase. J. Mol. Biol. 373, 1243-1254.
    • (2007) J. Mol. Biol. , vol.373 , pp. 1243-1254
    • McCleverty, C.J.1    Hornsby, M.2    Spraggon, G.3    Kreusch, A.4
  • 40
    • 78751557887 scopus 로고    scopus 로고
    • The handling of the mechanistic probe 5-fluorouridine by the pseudouridine synthase TruA and its consistency with the handling of the same probe by the pseudouridine synthases TruB and RluA
    • McDonald, M.K., Miracco, E.J., Chen, J., Xie, Y., and Mueller, E.G. (2011). The handling of the mechanistic probe 5-fluorouridine by the pseudouridine synthase TruA and its consistency with the handling of the same probe by the pseudouridine synthases TruB and RluA. Biochemistry 50, 426-436.
    • (2011) Biochemistry , vol.50 , pp. 426-436
    • McDonald, M.K.1    Miracco, E.J.2    Chen, J.3    Xie, Y.4    Mueller, E.G.5
  • 41
    • 0022036496 scopus 로고
    • Queuosine modification of the wobble base in tRNAHis influences in vivo decoding properties
    • Meier, F., Suter, B., Grosjean, H., Keith, G., and Kubli, E. (1985). Queuosine modification of the wobble base in tRNAHis influences 'in vivo' decoding properties. EMBO J. 4, 823-827.
    • (1985) EMBO J. , vol.4 , pp. 823-827
    • Meier, F.1    Suter, B.2    Grosjean, H.3    Keith, G.4    Kubli, E.5
  • 42
    • 77953656943 scopus 로고    scopus 로고
    • Motorin, Y., and Helm, M. (2010). tRNA stabilization by modified nucleotides. Biochemistry 49, 4934-4944.
    • (2010) Biochemistry , vol.49 , pp. 4934-4944
    • Motorin, Y.1    Helm, M.2
  • 44
    • 26044435441 scopus 로고    scopus 로고
    • Recent progress of structural biology of tRNA processing and modification
    • Nakanishi, K., and Nureki, O. (2005). Recent progress of structural biology of tRNA processing and modification. Mol. Cells 19, 157-166.
    • (2005) Mol. Cells , vol.19 , pp. 157-166
    • Nakanishi, K.1    Nureki, O.2
  • 45
    • 70350500192 scopus 로고    scopus 로고
    • Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase
    • Nakanishi, K., Bonnefond, L., Kimura, S., Suzuki, T., Ishitani, R., and Nureki, O. (2009). Structural basis for translational fidelity ensured by transfer RNA lysidine synthetase. Nature 461, 1144-1148.
    • (2009) Nature , vol.461 , pp. 1144-1148
    • Nakanishi, K.1    Bonnefond, L.2    Kimura, S.3    Suzuki, T.4    Ishitani, R.5    Nureki, O.6
  • 46
    • 33747125139 scopus 로고    scopus 로고
    • Snapshots of tRNA sulphuration via an adenylated intermediate
    • DOI 10.1038/nature04896, PII NATURE04896
    • Numata, T., Ikeuchi, Y., Fukai, S., Suzuki, T., and Nureki, O. (2006). Snapshots of tRNA sulphuration via an adenylated intermediate. Nature 442, 419-424. (Pubitemid 44264786)
    • (2006) Nature , vol.442 , Issue.7101 , pp. 419-424
    • Numata, T.1    Ikeuchi, Y.2    Fukai, S.3    Suzuki, T.4    Nureki, O.5
  • 47
    • 0242331664 scopus 로고    scopus 로고
    • Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
    • Pan, H., Agarwalla, S., Moustakas, D.T., Finer-Moore, J., and Stroud, R.M. (2003). Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit. Proc. Natl. Acad. Sci. USA 100, 12648-12653.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12648-12653
    • Pan, H.1    Agarwalla, S.2    Moustakas, D.T.3    Finer-Moore, J.4    Stroud, R.M.5
  • 48
    • 2542578632 scopus 로고    scopus 로고
    • Conformational change of pseudouridine 55 synthase upon its association with RNA substrate
    • DOI 10.1093/nar/gkh287
    • Phannachet, K., and Huang, R.H. (2004). Conformational change of pseudouridine 55 synthase upon its association with RNA substrate. Nucleic Acids Res. 32, 1422-1429. (Pubitemid 38854743)
    • (2004) Nucleic Acids Research , vol.32 , Issue.4 , pp. 1422-1429
    • Phannachet, K.1    Huang, R.H.2
  • 49
    • 0029991713 scopus 로고    scopus 로고
    • Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange
    • Romier, C., Reuter, K., Suck, D., and Ficner, R. (1996). Crystal structure of tRNA-guanine transglycosylase: RNA modification by base exchange. EMBO J. 15, 2850-2857. (Pubitemid 26176263)
    • (1996) EMBO Journal , vol.15 , Issue.11 , pp. 2850-2857
    • Romier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 50
    • 65449143614 scopus 로고    scopus 로고
    • RNA-protein mutually induced fit: Structure of Escherichia coli isopentenyl-tRNA transferase in complex with tRNA(Phe)
    • Seif, E., and Hallberg, B.M. (2009). RNA-protein mutually induced fit: structure of Escherichia coli isopentenyl-tRNA transferase in complex with tRNA(Phe). J. Biol. Chem. 284, 6600-6604.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6600-6604
    • Seif, E.1    Hallberg, B.M.2
  • 51
    • 1642580816 scopus 로고    scopus 로고
    • Not all pseudouridine synthases are potently inhibited by RNA containing 5-fluorouridine
    • DOI 10.1261/rna.5100104
    • Spedaliere, C.J., and Mueller, E.G. (2004). Not all pseudouridine synthases are potently inhibited by RNA containing 5-fluorouridine. RNA 10, 192-199. (Pubitemid 38129824)
    • (2004) RNA , vol.10 , Issue.2 , pp. 192-199
    • Spedaliere, C.J.1    Mueller, E.G.2
  • 52
    • 5644289361 scopus 로고    scopus 로고
    • The pseudouridine synthases: Revisiting a mechanism that seemed settled
    • Spedaliere, C.J., Ginter, J.M., Johnston, M.V., and Mueller, E.G. (2004). The pseudouridine synthases: revisiting a mechanism that seemed settled. J. Am. Chem. Soc. 126, 12758-12759.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12758-12759
    • Spedaliere, C.J.1    Ginter, J.M.2    Johnston, M.V.3    Mueller, E.G.4
  • 53
    • 61449176110 scopus 로고    scopus 로고
    • Structural basis for binding of RNA and cofactor by a KsgA methyltransferase
    • Tu, C., Tropea, J.E., Austin, B.P., Court, D.L., Waugh, D.S., and Ji, X. (2009). Structural basis for binding of RNA and cofactor by a KsgA methyltransferase. Structure 17, 374-385.
    • (2009) Structure , vol.17 , pp. 374-385
    • Tu, C.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 54
    • 34250876436 scopus 로고    scopus 로고
    • 5C methyltransferase
    • DOI 10.1261/rna.515707
    • Walbott, H., Husson, C., Auxilien, S., and Golinelli-Pimpaneau, B. (2007). Cysteine of sequence motif VI is essential for nucleophilic catalysis by yeast m5C methyltransferase. RNA 13, 967-973. (Pubitemid 46984888)
    • (2007) RNA , vol.13 , Issue.7 , pp. 967-973
    • Walbott, H.1    Husson, C.2    Auxilien, S.3    Golinelli-Pimpaneau, B.4
  • 55
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson, J.R. (2000). Induced fit in RNA-protein recognition. Nat. Struct. Biol. 7, 834-837.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 56
    • 0037099742 scopus 로고    scopus 로고
    • TadA, an essential tRNA-specific adenosine deaminase from Escherichia coli
    • DOI 10.1093/emboj/cdf362
    • Wolf, J., Gerber, A.P., and Keller, W. (2002). tadA, an essential tRNA-specific adenosine deaminase from Escherichia coli. EMBO J. 21, 3841-3851. (Pubitemid 34787056)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3841-3851
    • Wolf, J.1    Gerber, A.P.2    Keller, W.3
  • 57
    • 0141596159 scopus 로고    scopus 로고
    • Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
    • Xie, W., Liu, X., and Huang, R.H. (2003). Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate. Nat. Struct. Biol. 10, 781-788.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 781-788
    • Xie, W.1    Liu, X.2    Huang, R.H.3
  • 58
    • 55849083574 scopus 로고    scopus 로고
    • Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: Insight into tRNA recognition and reaction mechanism
    • Zhou, C., and Huang, R.H. (2008). Crystallographic snapshots of eukaryotic dimethylallyltransferase acting on tRNA: insight into tRNA recognition and reaction mechanism. Proc. Natl. Acad. Sci. USA 105, 16142-16147.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 16142-16147
    • Zhou, C.1    Huang, R.H.2


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