메뉴 건너뛰기




Volumn 13, Issue 10, 2007, Pages 1703-1714

Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 1: Minimizing misacylation

Author keywords

Frameshift suppression; Nonsense suppression; Opal suppressor tRNA; tRNA; Unnatural amino acid incorporation

Indexed keywords

AMBER SUPPRESSOR TRANSFER RNA; AMINO ACID TRANSFER RNA LIGASE; GLUTAMINE; OPAL SUPPRESSOR TRANSFER RNA; THG73 PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 34748904276     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.666807     Document Type: Article
Times cited : (24)

References (41)
  • 1
    • 0043028469 scopus 로고    scopus 로고
    • Adaptation of an orthogonal archaeal leucyl-tRNA and synthetase pair for four-base, amber, and opal suppression
    • Anderson, J.C. and Schultz, P.G. 2003. Adaptation of an orthogonal archaeal leucyl-tRNA and synthetase pair for four-base, amber, and opal suppression. Biochemistry 42: 9598-9608.
    • (2003) Biochemistry , vol.42 , pp. 9598-9608
    • Anderson, J.C.1    Schultz, P.G.2
  • 2
    • 0038383546 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis in mapping ion channel function
    • Beene, D.L., Dougherty, D.A., and Lester, H.A. 2003. Unnatural amino acid mutagenesis in mapping ion channel function. Curr. Opin. Neurobiol. 13: 264-270.
    • (2003) Curr. Opin. Neurobiol , vol.13 , pp. 264-270
    • Beene, D.L.1    Dougherty, D.A.2    Lester, H.A.3
  • 3
    • 0035902009 scopus 로고    scopus 로고
    • Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors
    • Brejc, K., van Dijk, W.J., Klaassen, R.V., Schuurmans, M., van Der Oost, J., Smit, A.B., and Sixma, T.K. 2001. Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors. Nature 411: 269-276.
    • (2001) Nature , vol.411 , pp. 269-276
    • Brejc, K.1    van Dijk, W.J.2    Klaassen, R.V.3    Schuurmans, M.4    van Der Oost, J.5    Smit, A.B.6    Sixma, T.K.7
  • 4
    • 0022993694 scopus 로고
    • Introduction of UAG, UAA, and UGA nonsense mutations at a specific site in the Escherichia coli chloramphenicol acetyltransferase gene: Use in measurement of amber, ochre, and opal suppression in mammalian cells
    • Capone, J.P., Sedivy, J.M., Sharp, P.A., and RajBhandary, U.L. 1986. Introduction of UAG, UAA, and UGA nonsense mutations at a specific site in the Escherichia coli chloramphenicol acetyltransferase gene: Use in measurement of amber, ochre, and opal suppression in mammalian cells. Mol. Cell. Biol. 6: 3059-3067.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 3059-3067
    • Capone, J.P.1    Sedivy, J.M.2    Sharp, P.A.3    RajBhandary, U.L.4
  • 5
    • 0030482172 scopus 로고    scopus 로고
    • Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids
    • Cload, S.T., Liu, D.R., Froland, W.A., and Schultz, P.G. 1996. Development of improved tRNAs for in vitro biosynthesis of proteins containing unnatural amino acids. Chem. Biol. 3: 1033-1038.
    • (1996) Chem. Biol , vol.3 , pp. 1033-1038
    • Cload, S.T.1    Liu, D.R.2    Froland, W.A.3    Schultz, P.G.4
  • 6
    • 0033637431 scopus 로고    scopus 로고
    • Unnatural amino acids as probes of protein structure and function
    • Dougherty, D.A. 2000. Unnatural amino acids as probes of protein structure and function. Curr. Opin. Biotechnol. 4: 645-652.
    • (2000) Curr. Opin. Biotechnol , vol.4 , pp. 645-652
    • Dougherty, D.A.1
  • 7
    • 0033607250 scopus 로고    scopus 로고
    • Mapping disulfide connectivity using backbone ester hydrolysis
    • England, P.M., Lester, H.A., and Dougherty, D.A. 1999. Mapping disulfide connectivity using backbone ester hydrolysis. Biochemistry 38: 14409-14415.
    • (1999) Biochemistry , vol.38 , pp. 14409-14415
    • England, P.M.1    Lester, H.A.2    Dougherty, D.A.3
  • 8
    • 0029123899 scopus 로고
    • The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating
    • Filatov, G.N. and White, M.M. 1995. The role of conserved leucines in the M2 domain of the acetylcholine receptor in channel gating. Mol. Pharmacol. 48: 379-384.
    • (1995) Mol. Pharmacol , vol.48 , pp. 379-384
    • Filatov, G.N.1    White, M.M.2
  • 10
    • 33745365951 scopus 로고    scopus 로고
    • A base pair at the bottom of the anticodon stem is reciprocally preferred for discrimination of cognate tRNAs by Escherichia coli lysyl- and glutaminyl-tRNA synthetases
    • doi: 10.1093/nar/gkl414
    • Fukunaga, J., Ohno, S., Nishikawa, K., and Yokogawa, T. 2006. A base pair at the bottom of the anticodon stem is reciprocally preferred for discrimination of cognate tRNAs by Escherichia coli lysyl- and glutaminyl-tRNA synthetases. Nucleic Acids Res. 34: 3181-3188. doi: 10.1093/nar/gkl414.
    • (2006) Nucleic Acids Res , vol.34 , pp. 3181-3188
    • Fukunaga, J.1    Ohno, S.2    Nishikawa, K.3    Yokogawa, T.4
  • 11
    • 0031260274 scopus 로고    scopus 로고
    • Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins
    • Gallivan, J.P., Lester, H.A., and Dougherty, D.A. 1997. Site-specific incorporation of biotinylated amino acids to identify surface-exposed residues in integral membrane proteins. Chem. Biol. 4: 739-749.
    • (1997) Chem. Biol , vol.4 , pp. 739-749
    • Gallivan, J.P.1    Lester, H.A.2    Dougherty, D.A.3
  • 13
    • 0029902187 scopus 로고    scopus 로고
    • Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme
    • Ibba, M., Hong, K.W., Sherman, J.M., Sever, S., and Soll, D. 1996. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. Proc. Natl. Acad. Sci. 93: 6953-6958.
    • (1996) Proc. Natl. Acad. Sci , vol.93 , pp. 6953-6958
    • Ibba, M.1    Hong, K.W.2    Sherman, J.M.3    Sever, S.4    Soll, D.5
  • 14
    • 0025887667 scopus 로고
    • Gln are major recognition elements for E. coli glutaminyl-tRNA synthetase
    • Gln are major recognition elements for E. coli glutaminyl-tRNA synthetase. Nature 352: 258-260.
    • (1991) Nature , vol.352 , pp. 258-260
    • Jahn, M.1    Rogers, M.J.2    Soll, D.3
  • 15
    • 0030480913 scopus 로고    scopus 로고
    • Determinants of nicotinic receptor gating in natural and unnatural side chain structures at the M2 9′ position
    • Kearney, P.C., Zhang, H., Zhong, W., Dougherty, D.A., and Lester, H.A. 1996. Determinants of nicotinic receptor gating in natural and unnatural side chain structures at the M2 9′ position. Neuron 17: 1221-1229.
    • (1996) Neuron , vol.17 , pp. 1221-1229
    • Kearney, P.C.1    Zhang, H.2    Zhong, W.3    Dougherty, D.A.4    Lester, H.A.5
  • 16
    • 0025331936 scopus 로고
    • Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency
    • Kleina, L.G., Masson, J.M., Normanly, J., Abelson, J., and Miller, J.H. 1990. Construction of Escherichia coli amber suppressor tRNA genes. II. Synthesis of additional tRNA genes and improvement of suppressor efficiency. J. Mol. Biol. 213: 705-717.
    • (1990) J. Mol. Biol , vol.213 , pp. 705-717
    • Kleina, L.G.1    Masson, J.M.2    Normanly, J.3    Abelson, J.4    Miller, J.H.5
  • 17
    • 13444266438 scopus 로고    scopus 로고
    • Complete set of orthogonal 21st aminoacyl-tRNA synthetase-amber, ochre, and opal suppressor tRNA pairs: Concomitant suppression of three different termination codons in an mRNA in mammalian cells
    • doi: 10.1093/nar/gkh959
    • Kohrer, C., Sullivan, E.L., and RajBhandary, U.L. 2004. Complete set of orthogonal 21st aminoacyl-tRNA synthetase-amber, ochre, and opal suppressor tRNA pairs: Concomitant suppression of three different termination codons in an mRNA in mammalian cells. Nucleic Acids Res. 32: 6200-6211. doi: 10.1093/nar/gkh959.
    • (2004) Nucleic Acids Res , vol.32 , pp. 6200-6211
    • Kohrer, C.1    Sullivan, E.L.2    RajBhandary, U.L.3
  • 18
    • 0034176414 scopus 로고    scopus 로고
    • Acetylcholine receptor gating is influenced by the polarity of amino acids at position 9′ in the M2 domain
    • Kosolapov, A.V., Filatov, G.N., and White, M.M. 2000. Acetylcholine receptor gating is influenced by the polarity of amino acids at position 9′ in the M2 domain. J. Membr. Biol. 174: 191-197.
    • (2000) J. Membr. Biol , vol.174 , pp. 191-197
    • Kosolapov, A.V.1    Filatov, G.N.2    White, M.M.3
  • 20
    • 0031906815 scopus 로고    scopus 로고
    • The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation
    • McClain, W.H., Schneider, J., Bhattacharya, S., and Gabriel, K. 1998. The importance of tRNA backbone-mediated interactions with synthetase for aminoacylation. Proc. Natl. Acad. Sci. 95: 460-465.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 460-465
    • McClain, W.H.1    Schneider, J.2    Bhattacharya, S.3    Gabriel, K.4
  • 21
    • 0345531144 scopus 로고    scopus 로고
    • Using a solid-phase ribozyme aminoacylation system to reprogram the genetic code
    • Murakami, H., Kourouklis, D., and Suga, H. 2003. Using a solid-phase ribozyme aminoacylation system to reprogram the genetic code. Chem. Biol. 10: 1077-1084.
    • (2003) Chem. Biol , vol.10 , pp. 1077-1084
    • Murakami, H.1    Kourouklis, D.2    Suga, H.3
  • 22
    • 33646044708 scopus 로고    scopus 로고
    • A highly flexible tRNA acylation method for nonnatural polypeptide synthesis
    • Murakami, H., Ohta, A., Ashigai, H., and Suga, H. 2006. A highly flexible tRNA acylation method for nonnatural polypeptide synthesis. Nat. Methods 3: 357-359.
    • (2006) Nat. Methods , vol.3 , pp. 357-359
    • Murakami, H.1    Ohta, A.2    Ashigai, H.3    Suga, H.4
  • 23
    • 29244487058 scopus 로고    scopus 로고
    • Binding efficiency of elongation factor Tu to tRNAs charged with nonnatural fluorescent amino acids
    • Nakata, H., Ohtsuki, T., Abe, R., Hohsaka, T., and Sisido, M. 2006. Binding efficiency of elongation factor Tu to tRNAs charged with nonnatural fluorescent amino acids. Anal. Biochem. 348: 321-323.
    • (2006) Anal. Biochem , vol.348 , pp. 321-323
    • Nakata, H.1    Ohtsuki, T.2    Abe, R.3    Hohsaka, T.4    Sisido, M.5
  • 24
    • 0025337664 scopus 로고
    • Construction of Escherichia coli amber suppressor tRNA genes. III. Determination of tRNA specificity
    • Normanly, J., Kleina, L.G., Masson, J.M., Abelson, J., and Miller, J.H. 1990. Construction of Escherichia coli amber suppressor tRNA genes. III. Determination of tRNA specificity. J. Mol. Biol. 213: 719-726.
    • (1990) J. Mol. Biol , vol.213 , pp. 719-726
    • Normanly, J.1    Kleina, L.G.2    Masson, J.M.3    Abelson, J.4    Miller, J.H.5
  • 25
    • 0032311418 scopus 로고    scopus 로고
    • In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system
    • Nowak, M.W., Gallivan, J.P., Silverman, S.K., Labarca, C.G., Dougherty, D.A., and Lester, H.A. 1998. In vivo incorporation of unnatural amino acids into ion channels in Xenopus oocyte expression system. Methods Enzymol. 293: 504-529.
    • (1998) Methods Enzymol , vol.293 , pp. 504-529
    • Nowak, M.W.1    Gallivan, J.P.2    Silverman, S.K.3    Labarca, C.G.4    Dougherty, D.A.5    Lester, H.A.6
  • 26
    • 0024391111 scopus 로고
    • Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes
    • Perona, J.J., Swanson, R.N., Rould, M.A., Steitz, T.A., and Soll, D. 1989. Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes. Science 246: 1152-1154.
    • (1989) Science , vol.246 , pp. 1152-1154
    • Perona, J.J.1    Swanson, R.N.2    Rould, M.A.3    Steitz, T.A.4    Soll, D.5
  • 27
    • 0036233248 scopus 로고    scopus 로고
    • MALDI-TOF mass spectrometry methods for evaluation of in vitro aminoacyl tRNA production
    • Petersson, E.J., Shahgholi, M., Lester, H.A., and Dougherty, D.A. 2002. MALDI-TOF mass spectrometry methods for evaluation of in vitro aminoacyl tRNA production. RNA 8: 542-547.
    • (2002) RNA , vol.8 , pp. 542-547
    • Petersson, E.J.1    Shahgholi, M.2    Lester, H.A.3    Dougherty, D.A.4
  • 28
    • 85013539887 scopus 로고
    • Methods for expression of excitability proteins in Xenopus oocytes
    • ed. T. Narahashi, pp, Academic Press, San Diego, CA
    • Quick, M.W. and Lester, H.A. 1994. Methods for expression of excitability proteins in Xenopus oocytes. In Ion channels of excitable cells (ed. T. Narahashi), pp. 261-279. Academic Press, San Diego, CA.
    • (1994) Ion channels of excitable cells , pp. 261-279
    • Quick, M.W.1    Lester, H.A.2
  • 29
    • 0024822218 scopus 로고
    • The use of 59-phospho-2 deoxyribocytidylylriboadenosine as a facile route to chemical aminoacylation of tRNA
    • doi: 10.1093/nar/17.23.9649
    • Robertson, S.A., Noren, C.J., Anthony-Cahill, S.J., Griffith, M.C., and Schultz, P.G. 1989. The use of 59-phospho-2 deoxyribocytidylylriboadenosine as a facile route to chemical aminoacylation of tRNA. Nucleic Acids Res. 17: 9649-9660. doi: 10.1093/nar/17.23.9649.
    • (1989) Nucleic Acids Res , vol.17 , pp. 9649-9660
    • Robertson, S.A.1    Noren, C.J.2    Anthony-Cahill, S.J.3    Griffith, M.C.4    Schultz, P.G.5
  • 30
    • 33745015242 scopus 로고    scopus 로고
    • In vivo incorporation of multiple unnatural amino acids through nonsense and frameshift suppression
    • Rodriguez, E.A., Lester, H.A., and Dougherty, D.A. 2006. In vivo incorporation of multiple unnatural amino acids through nonsense and frameshift suppression. Proc. Natl. Acad. Sci. 103: 8650-8655.
    • (2006) Proc. Natl. Acad. Sci , vol.103 , pp. 8650-8655
    • Rodriguez, E.A.1    Lester, H.A.2    Dougherty, D.A.3
  • 31
    • 34748850236 scopus 로고    scopus 로고
    • Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 2: Evaluating suppression efficiency
    • this issue, doi: 10.1261/rna.667607
    • Rodriguez, E.A., Lester, H.A., and Dougherty, D.A. 2007. Improved amber and opal suppressor tRNAs for incorporation of unnatural amino acids in vivo. Part 2: Evaluating suppression efficiency. RNA (this issue). doi: 10.1261/rna.667607.
    • (2007) RNA
    • Rodriguez, E.A.1    Lester, H.A.2    Dougherty, D.A.3
  • 34
    • 0026698949 scopus 로고
    • Regulation mechanisms of intracellular pH of Xenopus laevis oocyte
    • Sasaki, S., Ishibashi, K., Nagai, T., and Marumo, F. 1992. Regulation mechanisms of intracellular pH of Xenopus laevis oocyte. Biochim. Biophys. Acta 1137: 45-51.
    • (1992) Biochim. Biophys. Acta , vol.1137 , pp. 45-51
    • Sasaki, S.1    Ishibashi, K.2    Nagai, T.3    Marumo, F.4
  • 35
    • 3142581910 scopus 로고    scopus 로고
    • Site-specific insertion of spin-labeled L-amino acids in Xenopus oocytes
    • Shafer, A.M., Kalai, T., Bin Liu, S.Q., Hideg, K., and Voss, J.C. 2004. Site-specific insertion of spin-labeled L-amino acids in Xenopus oocytes. Biochemistry 43: 8470-8482.
    • (2004) Biochemistry , vol.43 , pp. 8470-8482
    • Shafer, A.M.1    Kalai, T.2    Bin Liu, S.Q.3    Hideg, K.4    Voss, J.C.5
  • 36
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • Unwin, N. 2005. Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution. J. Mol. Biol. 346: 967-989.
    • (2005) J. Mol. Biol , vol.346 , pp. 967-989
    • Unwin, N.1
  • 37
    • 33744939245 scopus 로고    scopus 로고
    • Tandemly activated tRNAs as participants in protein synthesis
    • Wang, B., Zhou, J., Lodder, M., Anderson III, R.D., and Hecht, S.M. 2006. Tandemly activated tRNAs as participants in protein synthesis. J. Biol. Chem. 281: 13865-13868.
    • (2006) J. Biol. Chem , vol.281 , pp. 13865-13868
    • Wang, B.1    Zhou, J.2    Lodder, M.3    Anderson III, R.D.4    Hecht, S.M.5
  • 38
    • 0019825777 scopus 로고
    • Direct measurement of intracellular pH changes in Xenopus eggs at fertilization and cleavage
    • Webb, D.J. and Nuccitelli, R. 1981. Direct measurement of intracellular pH changes in Xenopus eggs at fertilization and cleavage. J. Cell Biol. 91: 562-567.
    • (1981) J. Cell Biol , vol.91 , pp. 562-567
    • Webb, D.J.1    Nuccitelli, R.2
  • 39
    • 0028173160 scopus 로고
    • Nonsense-mediated mRNA decay in Xenopus oocytes and embryos
    • Whitfield, T.T., Sharpe, C.R., and Wylie, C.C. 1994. Nonsense-mediated mRNA decay in Xenopus oocytes and embryos. Dev. Biol. 165: 731-734.
    • (1994) Dev. Biol , vol.165 , pp. 731-734
    • Whitfield, T.T.1    Sharpe, C.R.2    Wylie, C.C.3
  • 41
    • 0032514762 scopus 로고    scopus 로고
    • From ab initio quantum mechanics to molecular neurobiology: A cation-π binding site in the nicotinic receptor
    • Zhong, W., Gallivan, J.P., Zhang, Y., Li, L., Lester, H.A., and Dougherty, D.A. 1998. From ab initio quantum mechanics to molecular neurobiology: A cation-π binding site in the nicotinic receptor. Proc. Natl. Acad. Sci. 95: 12088-12093.
    • (1998) Proc. Natl. Acad. Sci , vol.95 , pp. 12088-12093
    • Zhong, W.1    Gallivan, J.P.2    Zhang, Y.3    Li, L.4    Lester, H.A.5    Dougherty, D.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.