메뉴 건너뛰기




Volumn 289, Issue 1, 1999, Pages 1-7

Amino acid acceptor identity switch of Escherichia coli tmRNA from alanine to histidine in vitro

Author keywords

Alanyl tRNA synthetase; Histidyl tRNA synthetase; tmRNA; Trans translation; tRNA identity

Indexed keywords

ALANINE; HISTIDINE; MESSENGER RNA; POLYPEPTIDE; POLYURIDYLIC ACID; TRANSFER RNA;

EID: 0033612218     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2754     Document Type: Article
Times cited : (36)

References (42)
  • 3
    • 0030026177 scopus 로고    scopus 로고
    • A case for trans translation
    • Atkins J. F., Gesteland R. F. A case for trans translation. Nature. 379:1996;769-771.
    • (1996) Nature , vol.379 , pp. 769-771
    • Atkins, J.F.1    Gesteland, R.F.2
  • 5
    • 0024850365 scopus 로고
    • Primer extension analysis of RNA
    • Boorstein W. R., Craig E. A. Primer extension analysis of RNA. Methods Enzymol. 180:1989;347-369.
    • (1989) Methods Enzymol. , vol.180 , pp. 347-369
    • Boorstein, W.R.1    Craig, E.A.2
  • 8
    • 0032101712 scopus 로고    scopus 로고
    • Presence and location of modified nucleotides in Escherichia coli tmRNA: Structural mimicry with tRNA acceptor branches
    • Felden B., Hanawa K., Atkins J. F., Himeno H., Muto A., Gesteland R. F., McCloskey J. A., Crain P. F. Presence and location of modified nucleotides in Escherichia coli tmRNA: structural mimicry with tRNA acceptor branches. EMBO J. 17:1998;3188-3196.
    • (1998) EMBO J. , vol.17 , pp. 3188-3196
    • Felden, B.1    Hanawa, K.2    Atkins, J.F.3    Himeno, H.4    Muto, A.5    Gesteland, R.F.6    McCloskey, J.A.7    Crain, P.F.8
  • 9
    • 0025114689 scopus 로고
    • Enzymatic aminoacylation of an eight-base-pair microhelix with histidine
    • Francklyn C., Schimmel P. Enzymatic aminoacylation of an eight-base-pair microhelix with histidine. Proc. Natl Acad. Sci. USA. 87:1990;8655-8659.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8655-8659
    • Francklyn, C.1    Schimmel, P.2
  • 11
    • 0032511223 scopus 로고    scopus 로고
    • A nickel complex cleaves uridines in folded RNA structures: Application to E. coli tmRNA and related engineered molecules
    • Hickerson R., Watkins-Sims C. D., Burrows C. J., Atkins J. F., Gesteland R. F., Felden B. A nickel complex cleaves uridines in folded RNA structures: Application to E. coli tmRNA and related engineered molecules. J. Mol. Biol. 279:1998;577-587.
    • (1998) J. Mol. Biol. , vol.279 , pp. 577-587
    • Hickerson, R.1    Watkins-Sims, C.D.2    Burrows, C.J.3    Atkins, J.F.4    Gesteland, R.F.5    Felden, B.6
  • 15
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou Y.-M., Schimmel P. A simple structural feature is a major determinant of the identity of a transfer RNA. Nature. 333:1988;140-145.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.-M.1    Schimmel, P.2
  • 16
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of protein synthesized from messenger RNA
    • Keiler K. C., Waller P. R. H., Sauer R. T. Role of a peptide tagging system in degradation of protein synthesized from messenger RNA. Science. 271:1996;990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.H.2    Sauer, R.T.3
  • 18
    • 0032539857 scopus 로고    scopus 로고
    • 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli
    • Li Z., Pandit S., Deutscher M. P. 3′ exoribonucleolytic trimming is a common feature of the maturation of small, stable RNAs in Escherichia coli. Proc. Natl Acad. Sci. USA. 95:1998;2856-2861.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2856-2861
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 19
    • 0024279871 scopus 로고
    • Changing the identity of a tRNA by introducing a G-U wobble pair near the 3′ acceptor end
    • McClain W. H., Foss K. Changing the identity of a tRNA by introducing a G-U wobble pair near the 3′ acceptor end. Science. 240:1988;793-796.
    • (1988) Science , vol.240 , pp. 793-796
    • McClain, W.H.1    Foss, K.2
  • 20
    • 0020645043 scopus 로고
    • New M13 vectors for cloning
    • Messing J. New M13 vectors for cloning. Methods Enzymol. 101:1983;20-78.
    • (1983) Methods Enzymol. , vol.101 , pp. 20-78
    • Messing, J.1
  • 21
    • 0023651444 scopus 로고
    • Oligoribonucleotide synthesis using T7 polymerase and synthetic DNA templates
    • Milligan J. F., Groebe D. R., Witherell G. W., Uhlenbeck O. C. Oligoribonucleotide synthesis using T7 polymerase and synthetic DNA templates. Nucl. Acids Res. 15:1987;8783-8798.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 8783-8798
    • Milligan, J.F.1    Groebe, D.R.2    Witherell, G.W.3    Uhlenbeck, O.C.4
  • 22
    • 0030432334 scopus 로고    scopus 로고
    • Structure and function of bacterial 10Sa RNA: Trans -translation system
    • Muto A., Sato M., Tadaki T., Fukushima M., Ushida C., Himeno H. Structure and function of bacterial 10Sa RNA: trans -translation system. Biochimie. 78:1996;985-991.
    • (1996) Biochimie , vol.78 , pp. 985-991
    • Muto, A.1    Sato, M.2    Tadaki, T.3    Fukushima, M.4    Ushida, C.5    Himeno, H.6
  • 23
    • 0031939779 scopus 로고    scopus 로고
    • A bacterial RNA that functions as both a tRNA and an mRNA
    • Muto A., Ushida C., Himeno H. A bacterial RNA that functions as both a tRNA and an mRNA. Trends Biochem. Sci. 23:1998;25-29.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 25-29
    • Muto, A.1    Ushida, C.2    Himeno, H.3
  • 25
    • 0033605218 scopus 로고    scopus 로고
    • Functional and structural analysis of a pseudoknot upstream of the tag-encoded sequence in E. coli tmRNA
    • Nameki N., Felden B., Atkins J. F., Gesteland R. F., Himeno H., Muto A. Functional and structural analysis of a pseudoknot upstream of the tag-encoded sequence in E. coli tmRNA. J. Mol. Biol. 286:1999;733-744.
    • (1999) J. Mol. Biol. , vol.286 , pp. 733-744
    • Nameki, N.1    Felden, B.2    Atkins, J.F.3    Gesteland, R.F.4    Himeno, H.5    Muto, A.6
  • 27
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren C. J., Anthony-Cahill S. J., Griffith M. C., Schultz P. G. A general method for site-specific incorporation of unnatural amino acids into proteins. Science. 244:1989;182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 28
    • 0026013476 scopus 로고
    • CGG, an unassigned or nonsense codon in Mycoplasma capricolum
    • Oba T., Andachi Y., Muto A., Osawa S. CGG, an unassigned or nonsense codon in Mycoplasma capricolum. Proc. Natl Acad. Sci. USA. 88:1991;921-925.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 921-925
    • Oba, T.1    Andachi, Y.2    Muto, A.3    Osawa, S.4
  • 30
    • 0023953676 scopus 로고
    • Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro
    • Sampson J. R., Uhlenbeck O. C. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl Acad. Sci. USA. 85:1988;1033-1037.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 1033-1037
    • Sampson, J.R.1    Uhlenbeck, O.C.2
  • 31
    • 0025906386 scopus 로고
    • Aminoacylation of alanine minihelices. "discriminator" base modulates transition state of single turnover reaction
    • Shi J.-P., Schimmel P. Aminoacylation of alanine minihelices. "Discriminator" base modulates transition state of single turnover reaction. J. Biol. Chem. 266:1991;2705-2708.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2705-2708
    • Shi, J.-P.1    Schimmel, P.2
  • 32
    • 0026495236 scopus 로고
    • The role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases
    • Shimizu M., Asahara H., Tamura K., Hasegawa T., Himeno H. The role of anticodon bases and the discriminator nucleotide in the recognition of some E. coli tRNAs by their aminoacyl-tRNA synthetases. J. Mol. Evol. 35:1992;436-443.
    • (1992) J. Mol. Evol. , vol.35 , pp. 436-443
    • Shimizu, M.1    Asahara, H.2    Tamura, K.3    Hasegawa, T.4    Himeno, H.5
  • 33
    • 0032190210 scopus 로고    scopus 로고
    • Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae
    • Soma A., Himeno H. Cross-species aminoacylation of tRNA with a long variable arm between Escherichia coli and Saccharomyces cerevisiae. Nucl. Acids Res. 26:1998;4374-4381.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 4374-4381
    • Soma, A.1    Himeno, H.2
  • 35
  • 37
    • 0028906813 scopus 로고
    • C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide
    • Tu G.-F., Reid G. E., Zhang J.-G., Moritz R. L., Simpson R. J. C-terminal extension of truncated recombinant proteins in Escherichia coli with a 10Sa RNA decapeptide. J. Biol. Chem. 270:1995;9322-9326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9322-9326
    • Tu, G.-F.1    Reid, G.E.2    Zhang, J.-G.3    Moritz, R.L.4    Simpson, R.J.5
  • 38
    • 0028170454 scopus 로고
    • TRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis
    • Ushida C., Himeno H., Watanabe T., Muto A. tRNA-like structures in 10Sa RNAs of Mycoplasma capricolum and Bacillus subtilis. Nucl. Acids Res. 22:1994;3392-3396.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 3392-3396
    • Ushida, C.1    Himeno, H.2    Watanabe, T.3    Muto, A.4
  • 39
    • 0029907105 scopus 로고    scopus 로고
    • Phylogenetic analysis of tmRNA secondary structures
    • Williams K. P., Bartel D. P. Phylogenetic analysis of tmRNA secondary structures. RNA. 2:1996;1306-1310.
    • (1996) RNA , vol.2 , pp. 1306-1310
    • Williams, K.P.1    Bartel, D.P.2
  • 41
    • 0028237043 scopus 로고
    • Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA in Escherichia coli
    • Yan W., Francklyn C. Cytosine 73 is a discriminator nucleotide in vivo for histidyl-tRNA in Escherichia coli. J. Biol. Chem. 269:1994;10022-10027.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10022-10027
    • Yan, W.1    Francklyn, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.