메뉴 건너뛰기




Volumn 19, Issue 8, 2013, Pages 1137-1146

Unexpected expansion of tRNA substrate recognition by the yeast m 1G9 methyltransferase Trm10

Author keywords

m1G; Substrate specificity; Trm11; tRNA methyltransferase

Indexed keywords

METHYLTRANSFERASE; TRANSFER RNA; TRM10 PROTEIN; UNCLASSIFIED DRUG;

EID: 84880683872     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.039651.113     Document Type: Article
Times cited : (43)

References (30)
  • 2
    • 0011895723 scopus 로고    scopus 로고
    • Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA
    • Auxilien S, Crain PF, Trewyn RW, Grosjean H. 1996. Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA. J Mol Biol 262: 437-458.
    • (1996) J Mol Biol , vol.262 , pp. 437-458
    • Auxilien, S.1    Crain, P.F.2    Trewyn, R.W.3    Grosjean, H.4
  • 4
    • 0035449350 scopus 로고    scopus 로고
    • Translational misreading: A tRNA modification counteracts a +2 ribosomal frameshift
    • Brégeon D, Colot V, Radman M, Taddei F. 2001. Translational misreading: A tRNA modification counteracts a +2 ribosomal frameshift. Genes Dev 15: 2295-2306.
    • (2001) Genes Dev , vol.15 , pp. 2295-2306
    • Brégeon, D.1    Colot, V.2    Radman, M.3    Taddei, F.4
  • 5
    • 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
  • 7
    • 0022655673 scopus 로고
    • Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2
    • Ericson JU, Björk GR. 1986. Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2. J Bacteriol 166: 1013-1021.
    • (1986) J Bacteriol , vol.166 , pp. 1013-1021
    • Ericson, J.U.1    Björk, G.R.2
  • 9
    • 0033527628 scopus 로고    scopus 로고
    • An adenosine deaminase that generates inosine at the wobble position of tRNAs
    • Gerber AP, KellerW. 1999. An adenosine deaminase that generates inosine at the wobble position of tRNAs. Science 286: 1146-1149.
    • (1999) Science , vol.286 , pp. 1146-1149
    • Gerber, A.P.1    Keller, W.2
  • 11
    • 0028943560 scopus 로고
    • Posttranscriptionally modified nucleosides in transfer RNA: Their locations and frequencies
    • Grosjean H, Sprinzl M, Steinberg S. 1995. Posttranscriptionally modified nucleosides in transfer RNA: Their locations and frequencies. Biochimie 77: 139-141.
    • (1995) Biochimie , vol.77 , pp. 139-141
    • Grosjean, H.1    Sprinzl, M.2    Steinberg, S.3
  • 12
    • 41649102484 scopus 로고    scopus 로고
    • Evidence that tRNA modifying enzymes are important in vivo targets for 5-fluorouracil in yeast
    • Gustavsson M, Ronne H. 2008. Evidence that tRNA modifying enzymes are important in vivo targets for 5-fluorouracil in yeast. RNA 14: 666-674.
    • (2008) RNA , vol.14 , pp. 666-674
    • Gustavsson, M.1    Ronne, H.2
  • 14
    • 0020698678 scopus 로고
    • Purification and characterization of transfer RNA (guanine-1) methyltransferase from Escherichia coli
    • Hjalmarsson KJ, Byström AS, Björk GR. 1983. Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli. J Biol Chem 258: 1343-1351.
    • (1983) J Biol Chem , vol.258 , pp. 1343-1351
    • Hjalmarsson, K.J.1    Byström, A.S.2    Björk, G.R.3
  • 15
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • Holzmann J, Frank P, Loffler E, Bennett KL, Gerner C, Rossmanith W. 2008. RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell 135: 462-474.
    • (2008) Cell , vol.135 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loffler, E.3    Bennett, K.L.4    Gerner, C.5    Rossmanith, W.6
  • 16
    • 84871436566 scopus 로고    scopus 로고
    • Transfer RNA modifications: Nature's combinatorial chemistry playground
    • Jackman JE, Alfonzo JD. 2013. Transfer RNA modifications: Nature's combinatorial chemistry playground. Wiley Interdiscip Rev RNA 4: 35-48.
    • (2013) Wiley Interdiscip Rev RNA , vol.4 , pp. 35-48
    • Jackman, J.E.1    Alfonzo, J.D.2
  • 17
    • 33646870599 scopus 로고    scopus 로고
    • TRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases
    • Jackman JE, Phizicky EM. 2006. tRNAHis guanylyltransferase adds G-1 to the 5' end of tRNAHis by recognition of the anticodon, one of several features unexpectedly shared with tRNA synthetases. RNA 12: 1007-1014.
    • (2006) RNA , vol.12 , pp. 1007-1014
    • Jackman, J.E.1    Phizicky, E.M.2
  • 18
    • 0037407933 scopus 로고    scopus 로고
    • Identification of the yeast gene encoding the tRNA m1G methyltransferase responsible for modification at position 9
    • Jackman JE, Montange RK, Malik HS, Phizicky EM. 2003. Identification of the yeast gene encoding the tRNA m1G methyltransferase responsible for modification at position 9. RNA 9: 574-585.
    • (2003) RNA , vol.9 , pp. 574-585
    • Jackman, J.E.1    Montange, R.K.2    Malik, H.S.3    Phizicky, E.M.4
  • 20
    • 38049091553 scopus 로고    scopus 로고
    • Identification of yeast tRNA Um44 2'-O-methyltransferase (Trm44) and demonstration of a Trm44 role in sustaining levels of specific tRNASer species
    • Kotelawala L, Grayhack EJ, Phizicky EM. 2008. Identification of yeast tRNA Um44 2'-O-methyltransferase (Trm44) and demonstration of a Trm44 role in sustaining levels of specific tRNASer species. RNA 14: 158-169.
    • (2008) RNA , vol.14 , pp. 158-169
    • Kotelawala, L.1    Grayhack, E.J.2    Phizicky, E.M.3
  • 22
    • 77950589659 scopus 로고    scopus 로고
    • Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes
    • Ochi A, Makabe K, Kuwajima K, Hori H. 2010. Flexible recognition of the tRNA G18 methylation target site by TrmH methyltransferase through first binding and induced fit processes. J Biol Chem 285: 9018-9029.
    • (2010) J Biol Chem , vol.285 , pp. 9018-9029
    • Ochi, A.1    Makabe, K.2    Kuwajima, K.3    Hori, H.4
  • 23
    • 79959287938 scopus 로고    scopus 로고
    • Biosynthesis and function of tRNA modifications in Archaea
    • Phillips G, de Crécy-Lagard V. 2011. Biosynthesis and function of tRNA modifications in Archaea. Curr Opin Microbiol 14: 335-341.
    • (2011) Curr Opin Microbiol , vol.14 , pp. 335-341
    • Phillips, G.1    De Crécy-Lagard, V.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 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
  • 27
    • 0017885786 scopus 로고
    • Kinetic studies of Escherichia coli transfer RNA (uracil-5-)- methyltransferase
    • Shugart L. 1978. Kinetic studies of Escherichia coli transfer RNA (uracil-5-)-methyltransferase. Biochemistry 17: 1068-1072.
    • (1978) Biochemistry , vol.17 , pp. 1068-1072
    • Shugart, L.1
  • 28
    • 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, Björk 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    Björk, G.R.5
  • 29
    • 84871194226 scopus 로고    scopus 로고
    • A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase-extensive moonlighting in mitochondrial tRNA biogenesis
    • Vilardo E, Nachbagauer C, Buzet A, Taschner A, Holzmann J, Rossmanith W. 2012. A subcomplex of human mitochondrial RNase P is a bifunctional methyltransferase-extensive moonlighting in mitochondrial tRNA biogenesis. Nucleic Acids Res 40: 11583-11593.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11583-11593
    • Vilardo, E.1    Nachbagauer, C.2    Buzet, A.3    Taschner, A.4    Holzmann, J.5    Rossmanith, W.6
  • 30
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.