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Volumn 18, Issue 10, 2012, Pages 1921-1933

Yeast Trm7 interacts with distinct proteins for critical modifications of the tRNAPhe anticodon loop

Author keywords

RTT10; TRM7; tRNAphe; Wyebustosine; YMR259c

Indexed keywords

1 METHYLGUANOSINE; ARGININE; CYSTEINE; FUNGAL PROTEIN; GUANINE DERIVATIVE; GUANOSINE DERIVATIVE; MICROORGANISM PROTEIN; PHENYLALANINE TRANSFER RNA; RTT10 PROTEIN; TRANSFER RNA; TRM7 PROTEIN; TRM732 PROTEIN; UNCLASSIFIED DRUG; WYEBUTOSINE;

EID: 84866610711     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.035287.112     Document Type: Article
Times cited : (96)

References (76)
  • 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
  • 2
    • 0036795285 scopus 로고    scopus 로고
    • Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA
    • Alexandrov A, Martzen MR, Phizicky EM. 2002. Two proteins that form a complex are required for 7-methylguanosine modification of yeast tRNA. RNA 8: 1253-1266.
    • (2002) RNA , vol.8 , pp. 1253-1266
    • Alexandrov, A.1    Martzen, M.R.2    Phizicky, E.M.3
  • 4
    • 0032428969 scopus 로고    scopus 로고
    • The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA
    • Anderson J, Phan L, Cuesta R, Carlson BA, Pak M, Asano K, Bjork GR, Tamame M, Hinnebusch AG. 1998. The essential Gcd10p-Gcd14p nuclear complex is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA. Genes Dev 12: 3650-3662.
    • (1998) Genes Dev , vol.12 , pp. 3650-3662
    • Anderson, J.1    Phan, L.2    Cuesta, R.3    Carlson, B.A.4    Pak, M.5    Asano, K.6    Bjork, G.R.7    Tamame, M.8    Hinnebusch, A.G.9
  • 5
    • 0033600832 scopus 로고    scopus 로고
    • Singly and bifurcated hydrogen-bonded base-pairs in tRNA anticodon hairpins and ribozymes
    • Auffinger P, Westhof E. 1999. Singly and bifurcated hydrogen-bonded base-pairs in tRNA anticodon hairpins and ribozymes. J Mol Biol 292: 467-483.
    • (1999) J Mol Biol , vol.292 , pp. 467-483
    • Auffinger, P.1    Westhof, E.2
  • 6
    • 11344272208 scopus 로고    scopus 로고
    • An extended signal involved in eukaryotic -1 frameshifting operates through modification of the e site tRNA
    • Bekaert M, Rousset JP. 2005. An extended signal involved in eukaryotic -1 frameshifting operates through modification of the E site tRNA. Mol Cell 17: 61-68.
    • (2005) Mol Cell , vol.17 , pp. 61-68
    • Bekaert, M.1    Rousset, J.P.2
  • 8
    • 34447518814 scopus 로고    scopus 로고
    • A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast
    • Bjork GR, Huang B, Persson OP, Bystrom AS. 2007. A conserved modified wobble nucleoside (mcm5s2U) in lysyl-tRNA is required for viability in yeast. RNA 13: 1245-1255.
    • (2007) RNA , vol.13 , pp. 1245-1255
    • Bjork, G.R.1    Huang, B.2    Persson, O.P.3    Bystrom, A.S.4
  • 9
    • 78650683942 scopus 로고    scopus 로고
    • A quantitative systems approach reveals dynamic control of tRNA modifications during cellular stress
    • doi: 10.1371/journal.pgen.1001247
    • Chan CT, Dyavaiah M, DeMott MS, Taghizadeh K, Dedon PC, Begley TJ. 2010. A quantitative systems approach reveals dynamic control of tRNA modifications during cellular stress. PLoS Genet 6: e1001247. doi: 10.1371/journal.pgen. 1001247.
    • (2010) PLoS Genet , vol.6
    • Chan, C.T.1    Dyavaiah, M.2    DeMott, M.S.3    Taghizadeh, K.4    Dedon, P.C.5    Begley, T.J.6
  • 10
    • 80053461006 scopus 로고    scopus 로고
    • Elongator complex influences telomeric gene silencing and DNA damage response by its role in wobble uridine tRNA modification
    • doi: 10/1371/journal.pgen.1002258
    • Chen C, Huang B, Eliasson M, Ryden P, Bystrom AS. 2011. Elongator complex influences telomeric gene silencing and DNA damage response by its role in wobble uridine tRNA modification. PLoS Genet 7: e1002258. doi: 10/1371/journal.pgen.1002258.
    • (2011) PLoS Genet , vol.7
    • Chen, C.1    Huang, B.2    Eliasson, M.3    Ryden, P.4    Bystrom, A.S.5
  • 11
    • 44149119097 scopus 로고    scopus 로고
    • Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5′-3′ exonucleases Rat1 and Xrn1
    • Chernyakov I, Whipple JM, Kotelawala L, Grayhack EJ, Phizicky EM. 2008. Degradation of several hypomodified mature tRNA species in Saccharomyces cerevisiae is mediated by Met22 and the 5′-3′ exonucleases Rat1 and Xrn1. Genes Dev 22: 1369-1380.
    • (2008) Genes Dev , vol.22 , pp. 1369-1380
    • Chernyakov, I.1    Whipple, J.M.2    Kotelawala, L.3    Grayhack, E.J.4    Phizicky, E.M.5
  • 13
    • 0023084849 scopus 로고
    • Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae
    • Published erratum appears in Mol Cell Biol 1987 May;7(5): 2035
    • Dihanich ME, Najarian D, Clark R, Gillman EC, Martin NC, Hopper AK. 1987. Isolation and characterization of MOD5, a gene required for isopentenylation of cytoplasmic and mitochondrial tRNAs of Saccharomyces cerevisiae. Mol Cell Biol 7: 177-184. [Published erratum appears in Mol Cell Biol 1987 May;7(5): 2035.]
    • (1987) Mol Cell Biol , vol.7 , pp. 177-184
    • Dihanich, M.E.1    Najarian, D.2    Clark, R.3    Gillman, E.C.4    Martin, N.C.5    Hopper, A.K.6
  • 14
    • 0016210743 scopus 로고
    • Optical studies of the base-stacking properties of 2′-O-methylated dinucleoside monophosphates
    • Drake AF, Mason SF, Trim AR. 1974. Optical studies of the base-stacking properties of 2′-O-methylated dinucleoside monophosphates. J Mol Biol 86: 727-739.
    • (1974) J Mol Biol , vol.86 , pp. 727-739
    • Drake, A.F.1    Mason, S.F.2    Trim, A.R.3
  • 16
    • 0022996130 scopus 로고
    • 2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae
    • 2-dimethylguanosine modification of both mitochondrial and cytoplasmic tRNA in Saccharomyces cerevisiae. J Biol Chem 261: 9703-9709.
    • (1986) J Biol Chem , vol.261 , pp. 9703-9709
    • Ellis, S.R.1    Morales, M.J.2    Li, J.M.3    Hopper, A.K.4    Martin, N.C.5
  • 17
    • 33749078546 scopus 로고    scopus 로고
    • Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis
    • Esberg A, Huang B, Johansson MJ, Bystrom AS. 2006. Elevated levels of two tRNA species bypass the requirement for elongator complex in transcription and exocytosis. Mol Cell 24: 139-148.
    • (2006) Mol Cell , vol.24 , pp. 139-148
    • Esberg, A.1    Huang, B.2    Johansson, M.J.3    Bystrom, A.S.4
  • 18
    • 0037413674 scopus 로고    scopus 로고
    • Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2′-O-methyltransferases
    • Feder M, Pas J,Wyrwicz LS, Bujnicki JM. 2003. Molecular phylogenetics of the RrmJ/fibrillarin superfamily of ribose 2′-O-methyltransferases. Gene 302: 129-138.
    • (2003) Gene , vol.302 , pp. 129-138
    • Feder, M.1    Pas, J.2    Wyrwicz, L.S.3    Bujnicki, J.M.4
  • 20
    • 34248221547 scopus 로고    scopus 로고
    • Loss of SLC38A5 and FTSJ1 at Xp11.23 in three brothers with nonsyndromic mental retardation due to a microdeletion in an unstable genomic region
    • Froyen G, Bauters M, Boyle J, Van Esch H, Govaerts K, van Bokhoven H, Ropers HH, Moraine C, Chelly J, Fryns JP, et al. 2007. Loss of SLC38A5 and FTSJ1 at Xp11.23 in three brothers with nonsyndromic mental retardation due to a microdeletion in an unstable genomic region. Hum Genet 121: 539-547.
    • (2007) Hum Genet , vol.121 , pp. 539-547
    • Froyen, G.1    Bauters, M.2    Boyle, J.3    Van Esch, H.4    Govaerts, K.5    Van Bokhoven, H.6    Ropers, H.H.7    Moraine, C.8    Chelly, J.9    Fryns, J.P.10
  • 22
    • 37249009538 scopus 로고    scopus 로고
    • Kinetics of the interactions between yeast elongation factors 1A and 1Bα, guanine nucleotides, and aminoacyl- TRNA
    • Gromadski KB, Schummer T, Stromgaard A, Knudsen CR, Kinzy TG, Rodnina MV. 2007. Kinetics of the interactions between yeast elongation factors 1A and 1Bα, guanine nucleotides, and aminoacyl- tRNA. J Biol Chem 282: 35629-35637.
    • (2007) J Biol Chem , vol.282 , pp. 35629-35637
    • Gromadski, K.B.1    Schummer, T.2    Stromgaard, A.3    Knudsen, C.R.4    Kinzy, T.G.5    Rodnina, M.V.6
  • 24
    • 0037088811 scopus 로고    scopus 로고
    • A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast
    • doi:10.1093/nar/30.6.e23
    • Gueldener U, Heinisch J, Koehler GJ, Voss D, Hegemann JH. 2002. A second set of loxP marker cassettes for Cre-mediated multiple gene knockouts in budding yeast. Nucleic Acids Res 30: e23. doi:10.1093/nar/30.6.e23.
    • (2002) Nucleic Acids Res , vol.30
    • Gueldener, U.1    Heinisch, J.2    Koehler, G.J.3    Voss, D.4    Hegemann, J.H.5
  • 25
    • 0032867610 scopus 로고    scopus 로고
    • A Watson-Crick base-pair-disrupting methyl group (m1A9) is sufficient for cloverleaf folding of human mitochondrial tRNALys
    • Helm M, Giege R, Florentz C. 1999. A Watson-Crick base-pair-disrupting methyl group (m1A9) is sufficient for cloverleaf folding of human mitochondrial tRNALys. Biochemistry 38: 13338-13346.
    • (1999) Biochemistry , vol.38 , pp. 13338-13346
    • Helm, M.1    Giege, R.2    Florentz, C.3
  • 26
    • 34748832943 scopus 로고    scopus 로고
    • Pho85, a multifunctional cyclin-dependent protein kinase in budding yeast
    • Huang D, Friesen H, Andrews B. 2007. Pho85, a multifunctional cyclin-dependent protein kinase in budding yeast. Mol Microbiol 66: 303-314.
    • (2007) Mol Microbiol , vol.66 , pp. 303-314
    • Huang, D.1    Friesen, H.2    Andrews, B.3
  • 29
    • 43249104840 scopus 로고    scopus 로고
    • Eukaryotic wobble uridine modifications promote a functionally redundant decoding system
    • Johansson MJ, Esberg A, Huang B, Bjork GR, Bystrom AS. 2008. Eukaryotic wobble uridine modifications promote a functionally redundant decoding system. Mol Cell Biol 28: 3301-3312.
    • (2008) Mol Cell Biol , vol.28 , pp. 3301-3312
    • Johansson, M.J.1    Esberg, A.2    Huang, B.3    Bjork, G.R.4    Bystrom, A.S.5
  • 31
    • 2642574393 scopus 로고    scopus 로고
    • Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae
    • Kadaba S, Krueger A, Trice T, Krecic AM, Hinnebusch AG, Anderson J. 2004. Nuclear surveillance and degradation of hypomodified initiator tRNAMet in S. cerevisiae. Genes Dev 18: 1227-1240.
    • (2004) Genes Dev , vol.18 , pp. 1227-1240
    • Kadaba, S.1    Krueger, A.2    Trice, T.3    Krecic, A.M.4    Hinnebusch, A.G.5    Anderson, J.6
  • 32
    • 33344476794 scopus 로고    scopus 로고
    • Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent polyadenylation of nascent hypomethylated tRNA and an aberrant form of 5S rRNA
    • Kadaba S, Wang X, Anderson JT. 2006. Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent polyadenylation of nascent hypomethylated tRNA and an aberrant form of 5S rRNA. RNA 12: 508-521.
    • (2006) RNA , vol.12 , pp. 508-521
    • Kadaba, S.1    Wang, X.2    Anderson, J.T.3
  • 33
    • 0026524798 scopus 로고
    • Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group
    • Kawai G, Yamamoto Y, Kamimura T, Masegi T, Sekine M, Hata T, Iimori T, Watanabe T, Miyazawa T, Yokoyama S. 1992. Conformational rigidity of specific pyrimidine residues in tRNA arises from posttranscriptional modifications that enhance steric interaction between the base and the 2′-hydroxyl group. Biochemistry 31: 1040-1046.
    • (1992) Biochemistry , vol.31 , pp. 1040-1046
    • Kawai, G.1    Yamamoto, Y.2    Kamimura, T.3    Masegi, T.4    Sekine, M.5    Hata, T.6    Iimori, T.7    Watanabe, T.8    Miyazawa, T.9    Yokoyama, S.10
  • 38
    • 0018179979 scopus 로고
    • Isopentenyladenosine deficient tRNA from an antisuppressor mutant of Saccharomyces cerevisiae
    • Laten H, Gorman J, Bock RM. 1978. Isopentenyladenosine deficient tRNA from an antisuppressor mutant of Saccharomyces cerevisiae. Nucleic Acids Res 5: 4329-4342.
    • (1978) Nucleic Acids Res , vol.5 , pp. 4329-4342
    • Laten, H.1    Gorman, J.2    Bock, R.M.3
  • 39
    • 0037163022 scopus 로고    scopus 로고
    • Lack of pseudouridine 38/39 in the anticodon arm of yeast cytoplasmic tRNA decreases in vivo recoding efficiency
    • Lecointe F, Namy O, Hatin I, Simos G, Rousset JP, Grosjean H. 2002. Lack of pseudouridine 38/39 in the anticodon arm of yeast cytoplasmic tRNA decreases in vivo recoding efficiency. J Biol Chem 277: 30445-30453.
    • (2002) J Biol Chem , vol.277 , pp. 30445-30453
    • Lecointe, F.1    Namy, O.2    Hatin, I.3    Simos, G.4    Rousset, J.P.5    Grosjean, H.6
  • 43
    • 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. 1988. 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
  • 44
    • 16544374004 scopus 로고    scopus 로고
    • Structure of a purine-purine wobble base pair in the decoding center of the ribosome
    • Murphy FV 4th, Ramakrishnan V. 2004. Structure of a purine-purine wobble base pair in the decoding center of the ribosome. Nat Struct Mol Biol 11: 1251-1252.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1251-1252
    • Murphy IV, F.V.1    Ramakrishnan, V.2
  • 47
    • 33646778150 scopus 로고    scopus 로고
    • Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA
    • Noma A, Kirino Y, Ikeuchi Y, Suzuki T. 2006. Biosynthesis of wybutosine, a hyper-modified nucleoside in eukaryotic phenylalanine tRNA. EMBO J 25: 2142-2154.
    • (2006) EMBO J , vol.25 , pp. 2142-2154
    • Noma, A.1    Kirino, Y.2    Ikeuchi, Y.3    Suzuki, T.4
  • 48
    • 40849098073 scopus 로고    scopus 로고
    • Chromatin-associated genes protect the yeast genome from Ty1 insertional mutagenesis
    • Nyswaner KM, Checkley MA, Yi M, Stephens RM, Garfinkel DJ. 2008. Chromatin-associated genes protect the yeast genome from Ty1 insertional mutagenesis. Genetics 178: 197-214.
    • (2008) Genetics , vol.178 , pp. 197-214
    • Nyswaner, K.M.1    Checkley, M.A.2    Yi, M.3    Stephens, R.M.4    Garfinkel, D.J.5
  • 50
    • 79960582843 scopus 로고    scopus 로고
    • Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast
    • Ohira T, Suzuki T. 2011. Retrograde nuclear import of tRNA precursors is required for modified base biogenesis in yeast. Proc Natl Acad Sci 108: 10502-10507.
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 10502-10507
    • Ohira, T.1    Suzuki, T.2
  • 53
    • 71549130107 scopus 로고    scopus 로고
    • Do all modifications benefit all tRNAs?
    • Phizicky EM, Alfonzo JD. 2010. Do all modifications benefit all tRNAs? FEBS Lett 584: 265-271.
    • (2010) FEBS Lett , vol.584 , pp. 265-271
    • Phizicky, E.M.1    Alfonzo, J.D.2
  • 54
    • 77956276464 scopus 로고    scopus 로고
    • TRNA biology charges to the front
    • Phizicky EM, Hopper AK. 2010. tRNA biology charges to the front. Genes Dev 24: 1832-1860.
    • (2010) Genes Dev , vol.24 , pp. 1832-1860
    • Phizicky, E.M.1    Hopper, A.K.2
  • 55
    • 0037007220 scopus 로고    scopus 로고
    • Trm7p catalyses the formation of two 2′-O-methylriboses in yeast tRNA anticodon loop
    • Pintard L, Lecointe F, Bujnicki JM, Bonnerot C, Grosjean H, Lapeyre B. 2002. Trm7p catalyses the formation of two 2′-O-methylriboses in yeast tRNA anticodon loop. EMBO J 21: 1811-1820.
    • (2002) EMBO J , vol.21 , pp. 1811-1820
    • Pintard, L.1    Lecointe, F.2    Bujnicki, J.M.3    Bonnerot, C.4    Grosjean, H.5    Lapeyre, B.6
  • 56
    • 18944364447 scopus 로고    scopus 로고
    • Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA
    • Purushothaman SK, Bujnicki JM, Grosjean H, Lapeyre B. 2005. Trm11p and Trm112p are both required for the formation of 2-methylguanosine at position 10 in yeast tRNA. Mol Cell Biol 25: 4359-4370.
    • (2005) Mol Cell Biol , vol.25 , pp. 4359-4370
    • Purushothaman, S.K.1    Bujnicki, J.M.2    Grosjean, H.3    Lapeyre, B.4
  • 57
    • 0028508568 scopus 로고
    • A single methyl group prevents the mischarging of a tRNA
    • Putz J, Florentz C, Benseler F, Giege R. 1994. A single methyl group prevents the mischarging of a tRNA. Nat Struct Biol 1: 580-582.
    • (1994) Nat Struct Biol , vol.1 , pp. 580-582
    • Putz, J.1    Florentz, C.2    Benseler, F.3    Giege, R.4
  • 59
    • 4444382164 scopus 로고    scopus 로고
    • A splice site mutation in the methyltransferase gene FTSJ1 in Xp11.23 is associated with non-syndromic mental retardation in a large Belgian family (MRX9)
    • Ramser J, Winnepenninckx B, Lenski C, Errijgers V, Platzer M, Schwartz CE, Meindl A, Kooy RF. 2004. A splice site mutation in the methyltransferase gene FTSJ1 in Xp11.23 is associated with non-syndromic mental retardation in a large Belgian family (MRX9). J Med Genet 41: 679-683.
    • (2004) J Med Genet , vol.41 , pp. 679-683
    • Ramser, J.1    Winnepenninckx, B.2    Lenski, C.3    Errijgers, V.4    Platzer, M.5    Schwartz, C.E.6    Meindl, A.7    Kooy, R.F.8
  • 60
    • 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 85: 1033-1037.
    • (1988) Proc Natl Acad Sci , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 62
    • 34447300418 scopus 로고    scopus 로고
    • The exosome subunit Rrp44 plays a direct role in RNA substrate recognition
    • Schneider C, Anderson JT, Tollervey D. 2007. The exosome subunit Rrp44 plays a direct role in RNA substrate recognition. Mol Cell 27: 324-331.
    • (2007) Mol Cell , vol.27 , pp. 324-331
    • Schneider, C.1    Anderson, J.T.2    Tollervey, D.3
  • 64
    • 0033862354 scopus 로고    scopus 로고
    • The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: A classic structure revisited
    • Shi H, Moore PB. 2000. The crystal structure of yeast phenylalanine tRNA at 1.93 A resolution: A classic structure revisited. RNA 6: 1091-1105.
    • (2000) RNA , vol.6 , pp. 1091-1105
    • Shi, H.1    Moore, P.B.2
  • 65
    • 80655144724 scopus 로고    scopus 로고
    • Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway
    • Shi Y, Stefan CJ, Rue SM, Teis D, Emr SD. 2011. Two novel WD40 domain-containing proteins, Ere1 and Ere2, function in the retromer-mediated endosomal recycling pathway. Mol Biol Cell 22: 4093-4107.
    • (2011) Mol Biol Cell , vol.22 , pp. 4093-4107
    • Shi, Y.1    Stefan, C.J.2    Rue, S.M.3    Teis, D.4    Emr, S.D.5
  • 68
    • 45149103870 scopus 로고    scopus 로고
    • A loss-of-function mutation in the FTSJ1 gene causes nonsyndromic X-linked mental retardation in a Japanese family
    • Takano K, Nakagawa E, Inoue K, Kamada F, Kure S, Goto Y. 2008. A loss-of-function mutation in the FTSJ1 gene causes nonsyndromic X-linked mental retardation in a Japanese family. Am J Med Genet B Neuropsychiatr Genet 147B: 479-484.
    • (2008) Am J Med Genet B Neuropsychiatr Genet , vol.147 B , pp. 479-484
    • Takano, K.1    Nakagawa, E.2    Inoue, K.3    Kamada, F.4    Kure, S.5    Goto, Y.6
  • 69
    • 77955335145 scopus 로고    scopus 로고
    • Armadillo-repeat protein functions: Questions for little creatures
    • Tewari R, Bailes E, Bunting KA, Coates JC. 2010. Armadillo-repeat protein functions: Questions for little creatures. Trends Cell Biol 20: 470-481.
    • (2010) Trends Cell Biol , vol.20 , pp. 470-481
    • Tewari, R.1    Bailes, E.2    Bunting, K.A.3    Coates, J.C.4
  • 70
    • 77950345305 scopus 로고    scopus 로고
    • 46) in tRNA from Thermus thermophilus is required for cell viability at high temperatures through a tRNA modification network
    • 46) in tRNA from Thermus thermophilus is required for cell viability at high temperatures through a tRNA modification network. Nucleic Acids Res 38: 942-957.
    • (2010) Nucleic Acids Res , vol.38 , pp. 942-957
    • Tomikawa, C.1    Yokogawa, T.2    Kanai, T.3    Hori, H.4
  • 71
    • 0035801515 scopus 로고    scopus 로고
    • Improvement of reading frame maintenance is a common function for several tRNA modifications
    • Urbonavicius J, Qian Q, Durand JM, Hagervall TG, Bjork GR. 2001. Improvement of reading frame maintenance is a common function for several tRNA modifications. EMBO J 20: 4863-4873.
    • (2001) EMBO J , vol.20 , pp. 4863-4873
    • Urbonavicius, J.1    Qian, Q.2    Durand, J.M.3    Hagervall, T.G.4    Bjork, G.R.5
  • 73
    • 34548816729 scopus 로고    scopus 로고
    • Role of a tRNA base modification and its precursors in frameshifting in eukaryotes
    • Waas WF, Druzina Z, Hanan M, Schimmel P. 2007. Role of a tRNA base modification and its precursors in frameshifting in eukaryotes. J Biol Chem 282: 26026-26034.
    • (2007) J Biol Chem , vol.282 , pp. 26026-26034
    • Waas, W.F.1    Druzina, Z.2    Hanan, M.3    Schimmel, P.4
  • 74
    • 79958053947 scopus 로고    scopus 로고
    • The yeast rapid tRNA decay pathway primarily monitors the structural integrity of the acceptor and T-stems of mature tRNA
    • Whipple JM, Lane EA, Chernyakov I, D'Silva S, Phizicky EM. 2011. The yeast rapid tRNA decay pathway primarily monitors the structural integrity of the acceptor and T-stems of mature tRNA. Genes Dev 25: 1173-1184.
    • (2011) Genes Dev , vol.25 , pp. 1173-1184
    • Whipple, J.M.1    Lane, E.A.2    Chernyakov, I.3    D'Silva, S.4    Phizicky, E.M.5
  • 76
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: Lessons from protein synthesis
    • Zaher HS, Green R. 2009. Fidelity at the molecular level: Lessons from protein synthesis. Cell 136: 746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2


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