메뉴 건너뛰기




Volumn 15, Issue 3, 1996, Pages 650-657

Antideterminants present in minihelixSec hinder its recognition by prokaryotic elongation factor Tu

Author keywords

Antideterminant; G U mismatch; Protein RNA recognition; RNA engineering; Selenocysteine

Indexed keywords

ESCHERICHIA COLI; PROKARYOTA; THERMUS THERMOPHILUS;

EID: 0029671252     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb00397.x     Document Type: Article
Times cited : (74)

References (53)
  • 2
    • 0029082529 scopus 로고
    • Structure of the P1 helix from group I self-splicing introns
    • Allain, F.H.T. and Varani, G. (1995) Structure of the P1 helix from group I self-splicing introns. J. Mol. Biol., 250, 333-353.
    • (1995) J. Mol. Biol. , vol.250 , pp. 333-353
    • Allain, F.H.T.1    Varani, G.2
  • 3
    • 0028034499 scopus 로고
    • Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination
    • Aström, S. and Byström, A.S. (1994) Rit1, a tRNA backbone-modifying enzyme that mediates initiator and elongator tRNA discrimination. Cell, 79, 535-546.
    • (1994) Cell , vol.79 , pp. 535-546
    • Aström, S.1    Byström, A.S.2
  • 4
    • 0025889078 scopus 로고
    • Sec of Escherichia coli is the determinant for binding to elongation factors SELB or Tu
    • Sec of Escherichia coli is the determinant for binding to elongation factors SELB or Tu. J. Biol. Chem., 266, 20375-20379.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20375-20379
    • Baron, C.1    Böck, A.2
  • 5
    • 0001314696 scopus 로고
    • The selenocysteine-inserting tRNA species: Structure and function
    • Söll, D. and RajBhandary, U.L. (eds), American Society for Microbiology. Washington, DC
    • Baron, C. and Böck, A. (1995) The selenocysteine-inserting tRNA species: structure and function. In Söll, D. and RajBhandary, U.L. (eds), Transfer RNA; Structure, Biosynthesis and Function. American Society for Microbiology. Washington, DC, pp. 529-544.
    • (1995) Transfer RNA; Structure, Biosynthesis and Function , pp. 529-544
    • Baron, C.1    Böck, A.2
  • 7
    • 0028332817 scopus 로고
    • Cis- and trans-acting ribozymes from a human pathogen, hepatitis delta virus
    • Been, M.D. (1994) Cis- and trans-acting ribozymes from a human pathogen, hepatitis delta virus. Trends Biochem. Sci., 19, 251-256.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 251-256
    • Been, M.D.1
  • 8
    • 0019819931 scopus 로고
    • A study of the interaction of Escherichia coli elongation factor-Tu with aminoacyl-tRNAs by partial digestion with cobra venom ribonuclease
    • Boutorin, A.S., Clark, B.F.C., Ebel, J.-P., Kruse, T.A., Petersen, H.U., Remy, P. and Vassilenko, S. (1981) A study of the interaction of Escherichia coli elongation factor-Tu with aminoacyl-tRNAs by partial digestion with cobra venom ribonuclease. J. Mol. Biol., 152, 593-608.
    • (1981) J. Mol. Biol. , vol.152 , pp. 593-608
    • Boutorin, A.S.1    Clark, B.F.C.2    Ebel, J.-P.3    Kruse, T.A.4    Petersen, H.U.5    Remy, P.6    Vassilenko, S.7
  • 9
    • 0024420343 scopus 로고
    • Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein
    • Forchhammer, K., Leinfelder, W. and Böck, A. (1989) Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. Nature, 342, 453-456.
    • (1989) Nature , vol.342 , pp. 453-456
    • Forchhammer, K.1    Leinfelder, W.2    Böck, A.3
  • 10
    • 0025103403 scopus 로고
    • Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E. coli
    • Förster, C., Ott, G., Forchhammer, K. and Sprinzl, M. (1990) Interaction of a selenocysteine-incorporating tRNA with elongation factor Tu from E. coli. Nucleic Acids Res., 18, 487-491.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 487-491
    • Förster, C.1    Ott, G.2    Forchhammer, K.3    Sprinzl, M.4
  • 11
    • 0027745663 scopus 로고
    • Discrimination between initiation and elongation of protein biosynthesis in yeast: Identity assured by a nucleotide modification in the initiator tRNA
    • Förster, C., Chakraburtty, K. and Sprinzl, M. (1993) Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA. Nucleic Acids Res., 21, 5679-5683.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5679-5683
    • Förster, C.1    Chakraburtty, K.2    Sprinzl, M.3
  • 12
    • 0028213965 scopus 로고
    • Efficient aminoacylation of resected RNA helices by class II aspartyl-tRNA synthetase dependent on a single nucleotide
    • Frugier, M., Florentz, C. and Giegé, R. (1994) Efficient aminoacylation of resected RNA helices by class II aspartyl-tRNA synthetase dependent on a single nucleotide. EMBO J., 13, 2218-2226.
    • (1994) EMBO J. , vol.13 , pp. 2218-2226
    • Frugier, M.1    Florentz, C.2    Giegé, R.3
  • 14
    • 0025835642 scopus 로고
    • Synthesis of RNA containing inosine: Analysis of the sequence requirements for the 5′ splice site of the Tetrahymena group I intron
    • Green, R., Szostak, J.W., Benner, S.A., Rich, A. and Usman, N. (1991) Synthesis of RNA containing inosine: analysis of the sequence requirements for the 5′ splice site of the Tetrahymena group I intron. Nucleic Acids Res., 19, 4161-4166.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4161-4166
    • Green, R.1    Szostak, J.W.2    Benner, S.A.3    Rich, A.4    Usman, N.5
  • 16
    • 0026000848 scopus 로고
    • Crystal structure of an RNA double helix incorporating a track of non-Watson-Crick base pairs
    • Holbrook, S.R., Cheong, C., Tinoco, I., Jr and Kim, S.-H. (1991) Crystal structure of an RNA double helix incorporating a track of non-Watson-Crick base pairs. Nature, 353, 579-581.
    • (1991) Nature , vol.353 , pp. 579-581
    • Holbrook, S.R.1    Cheong, C.2    Tinoco Jr., I.3    Kim, S.-H.4
  • 17
    • 0024284965 scopus 로고
    • A simple structural feature is a major determinant of the identity of a transfer RNA
    • Hou, Y.-M. and Schimmel, P. (1988) A simple structural feature is a major determinant of the identity of a transfer RNA. Nature, 333, 140-145.
    • (1988) Nature , vol.333 , pp. 140-145
    • Hou, Y.-M.1    Schimmel, P.2
  • 18
    • 0025280236 scopus 로고
    • Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu-GTP: Evidence for a new functional role for elongation factor Tu in protein biosynthesis
    • Januak, F., Dell, V.A., Abrahamson, J.K., Watson, B.S., Miller, D.L. and Johnson, A.E. (1990) Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu-GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis. Biochemistry, 29, 4268-4277.
    • (1990) Biochemistry , vol.29 , pp. 4268-4277
    • Januak, F.1    Dell, V.A.2    Abrahamson, J.K.3    Watson, B.S.4    Miller, D.L.5    Johnson, A.E.6
  • 19
    • 0347302203 scopus 로고
    • Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
    • Joshi, R.L., Faulhammer, H., Chapeville, F., Sprinzl, M. and Haenni, A.L. (1984) Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu. Nucleic Acids Res., 12, 7467-7478.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7467-7478
    • Joshi, R.L.1    Faulhammer, H.2    Chapeville, F.3    Sprinzl, M.4    Haenni, A.L.5
  • 22
    • 0026512522 scopus 로고
    • Bar to normal UGA translation by the selenocysteine transfer RNA
    • Li, W. and Yarus, M. (1992) Bar to normal UGA translation by the selenocysteine transfer RNA. J. Mol. Biol., 223, 9-15.
    • (1992) J. Mol. Biol. , vol.223 , pp. 9-15
    • Li, W.1    Yarus, M.2
  • 23
    • 0026509493 scopus 로고
    • Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR
    • Limmer, S., Reiser, C.O.A., Schirmer, N.K., Grillenbeck, N.W. and Sprinzl, M. (1992) Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR. Biochemistry, 31, 2970-2977.
    • (1992) Biochemistry , vol.31 , pp. 2970-2977
    • Limmer, S.1    Reiser, C.O.A.2    Schirmer, N.K.3    Grillenbeck, N.W.4    Sprinzl, M.5
  • 24
    • 0027287954 scopus 로고
    • The 3′-terminal end (NCCA) of tRNA determines the structure and stability of the aminoacyl acceptor stem
    • Limmer, S., Hofman, H.P., Ott, G. and Sprinzl, M. (1993) The 3′-terminal end (NCCA) of tRNA determines the structure and stability of the aminoacyl acceptor stem. Proc. Natl Acad. Sci. USA, 90, 6199-6202.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6199-6202
    • Limmer, S.1    Hofman, H.P.2    Ott, G.3    Sprinzl, M.4
  • 26
    • 0027369542 scopus 로고
    • Rules that govern tRNA identity in protein synthesis
    • McClain, W.H. (1993) Rules that govern tRNA identity in protein synthesis. J. Mol. Biol., 234, 257-280.
    • (1993) J. Mol. Biol. , vol.234 , pp. 257-280
    • McClain, W.H.1
  • 27
    • 0024279871 scopus 로고
    • Changing the identity of a tRNA by introducing a G-U wobble pair near the 3′ acceptor end
    • McClain, W.H. and Foss, K. (1988) Changing the identity of a tRNA by introducing a G-U wobble pair near the 3′ acceptor end. Science, 240, 793-796.
    • (1988) Science , vol.240 , pp. 793-796
    • McClain, W.H.1    Foss, K.2
  • 28
    • 0024295537 scopus 로고
    • Association of transfer RNA acceptor identity with a helical irregularity
    • McClain, W.H., Chen, Y.M., Foss, K. and Schneider, J. (1988) Association of transfer RNA acceptor identity with a helical irregularity. Science, 242, 1681-1684.
    • (1988) Science , vol.242 , pp. 1681-1684
    • McClain, W.H.1    Chen, Y.M.2    Foss, K.3    Schneider, J.4
  • 29
    • 0023734317 scopus 로고
    • Codon and amino-acid specificities of a transfer RNA are both converted by a single posttranscriptional modification
    • Muramatsu, T., Nishikawa, K., Nemoto, F., Kuchino, Y., Nishimura, S., Miyazawa, T. and Yokoyama, S. (1988) Codon and amino-acid specificities of a transfer RNA are both converted by a single posttranscriptional 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
  • 30
    • 0025850420 scopus 로고
    • Specificity for aminoacylation of an RNA helix: An unpaired exocyclic amino group in the minor groove
    • Musier-Forsyth, K., Usman, N., Scaringe, S., Doudna, J., Green, R. and Schimmel, P. (1991) Specificity for aminoacylation of an RNA helix: an unpaired exocyclic amino group in the minor groove. Science, 253, 784-786.
    • (1991) Science , vol.253 , pp. 784-786
    • Musier-Forsyth, K.1    Usman, N.2    Scaringe, S.3    Doudna, J.4    Green, R.5    Schimmel, P.6
  • 31
    • 0028180696 scopus 로고
    • Phe are not essential for ternary complex formation and peptide elongation
    • Phe are not essential for ternary complex formation and peptide elongation. EMBO J., 13, 2464-2471.
    • (1994) EMBO J. , vol.13 , pp. 2464-2471
    • Nazarenko, I.A.1    Harrington, K.M.2    Uhlenbeck, O.C.3
  • 32
    • 0024971344 scopus 로고
    • Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3′ terminus
    • Ott, G., Faulhammer, H. and Sprinzl, M. (1989) Interaction of elongation factor Tu from Escherichia coli with aminoacyl-tRNA carrying a fluorescent reporter group on the 3′ terminus. Eur. J. Biochem., 184, 345-352.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 345-352
    • Ott, G.1    Faulhammer, H.2    Sprinzl, M.3
  • 34
    • 0025612150 scopus 로고
    • Interaction of the isolated domain II/III of Thermus thermophilus factor Tu with the nucleotide exchange factor EF-Ts
    • Peter, M.E., Reiser, C.O.A., Schirmer, N.K., Kiefhaber, T., Ott, G., Grillenbeck, N.W. and Sprinzl, M. (1990) Interaction of the isolated domain II/III of Thermus thermophilus factor Tu with the nucleotide exchange factor EF-Ts. Nucleic Acids Res., 18, 6889-6893.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6889-6893
    • Peter, M.E.1    Reiser, C.O.A.2    Schirmer, N.K.3    Kiefhaber, T.4    Ott, G.5    Grillenbeck, N.W.6    Sprinzl, M.7
  • 35
    • 0018945995 scopus 로고
    • Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu
    • Pingould, A., and Urbanke, C. (1980) Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu. Biochemistry, 19, 2108-2112.
    • (1980) Biochemistry , vol.19 , pp. 2108-2112
    • Pingould, A.1    Urbanke, C.2
  • 36
    • 0027165593 scopus 로고
    • Additive, cooperative and anti-cooperative effects between identity nucleotides of a tRNA
    • Pütz, J., Puglisi, J.D., Florentz, C. and Giegé, R. (1993) Additive, cooperative and anti-cooperative effects between identity nucleotides of a tRNA. EMBO J., 12, 2949-2957.
    • (1993) EMBO J. , vol.12 , pp. 2949-2957
    • Pütz, J.1    Puglisi, J.D.2    Florentz, C.3    Giegé, R.4
  • 37
    • 0002084108 scopus 로고
    • Initiator tRNAs and initiation of protein synthesis
    • Söll, D., and RajBhandary, U.L. (eds), American Society for Microbiology, Washington, DC
    • RajBhandary, U.L. and Chow, C.M. (1995) Initiator tRNAs and initiation of protein synthesis. In Söll, D., and RajBhandary, U.L. (eds), Transfer RNA: Structure, Biosynthesis and Function. American Society for Microbiology, Washington, DC, pp. 511-528.
    • (1995) Transfer RNA: Structure, Biosynthesis and Function , pp. 511-528
    • RajBhandary, U.L.1    Chow, C.M.2
  • 38
    • 0017648934 scopus 로고
    • Initial stages of the thermal unfolding of yeast phenylalanine transfer RNA as studied by chemical modification: The effect of magnesium
    • Rhodes, D. (1977) Initial stages of the thermal unfolding of yeast phenylalanine transfer RNA as studied by chemical modification: the effect of magnesium. Eur. J. Biochem., 81, 91-101.
    • (1977) Eur. J. Biochem. , vol.81 , pp. 91-101
    • Rhodes, D.1
  • 40
    • 0028241947 scopus 로고
    • Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu
    • Rudinger, J., Blechschmidt, B., Ribeiro, S. and Sprinzl, M. (1994) Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu. Biochemistry, 33, 5682-5688.
    • (1994) Biochemistry , vol.33 , pp. 5682-5688
    • Rudinger, J.1    Blechschmidt, B.2    Ribeiro, S.3    Sprinzl, M.4
  • 41
    • 0024451607 scopus 로고
    • The selenocysteine-inserting opal suppressor serine tRNA from E. coli is highly unusual in structure and modification
    • Schön, A., Böck, A., Ott, G., Sprinzl, M. and Söll, D. (1989) The selenocysteine-inserting opal suppressor serine tRNA from E. coli is highly unusual in structure and modification. Nucleic Acids Res., 17, 7159-7165.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7159-7165
    • Schön, A.1    Böck, A.2    Ott, G.3    Sprinzl, M.4    Söll, D.5
  • 42
    • 0023502772 scopus 로고
    • Mutants of Escherichia coli formylmethionine tRNA: A single base change enables initiator tRNA to act as an elongator in vitro
    • Seong, B.L. and RajBhandary, U.L. (1987) Mutants of Escherichia coli formylmethionine tRNA: a single base change enables initiator tRNA to act as an elongator in vitro. Proc. Natl Acad. Sci. USA, 84, 8859-8863.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 8859-8863
    • Seong, B.L.1    RajBhandary, U.L.2
  • 43
    • 0024508879 scopus 로고
    • Suppression of amber codons in vivo as evidence that mutants derived from Escherichia coli initiator tRNA can act as the step of elongation in protein synthesis
    • Seong, B.L., Lee, C.P. and RajBhandary, U.L. (1989) Suppression of amber codons in vivo as evidence that mutants derived from Escherichia coli initiator tRNA can act as the step of elongation in protein synthesis. J. Biol. Chem., 246, 6504-6508.
    • (1989) J. Biol. Chem. , vol.246 , pp. 6504-6508
    • Seong, B.L.1    Lee, C.P.2    RajBhandary, U.L.3
  • 44
    • 0027244036 scopus 로고
    • Compilation of tRNA sequences and sequences of tRNA genes
    • Steinberg, S., Misch, A. and Sprinzl, M. (1993) Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res., 21, 3011-3015.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3011-3015
    • Steinberg, S.1    Misch, A.2    Sprinzl, M.3
  • 45
    • 0028955347 scopus 로고
    • Minor groove recognition of the conserved G-U pair at the Tetrahymena ribozyme reaction site
    • Strobel, S.A. and Cech, T.R. (1995) Minor groove recognition of the conserved G-U pair at the Tetrahymena ribozyme reaction site. Science, 267, 675-679.
    • (1995) Science , vol.267 , pp. 675-679
    • Strobel, S.A.1    Cech, T.R.2
  • 47
    • 0028348649 scopus 로고
    • Genes coding for the selenocysteine-inserting tRNA species from Desulfomicrobium baculatum and Clostridium thermoaceticum: Structural and evolutionary implications
    • Tormay, P., Wilting, R., Heider, J. and Böck, A. (1994) Genes coding for the selenocysteine-inserting tRNA species from Desulfomicrobium baculatum and Clostridium thermoaceticum: structural and evolutionary implications. J. Bacteriol., 176, 1268-1274.
    • (1994) J. Bacteriol. , vol.176 , pp. 1268-1274
    • Tormay, P.1    Wilting, R.2    Heider, J.3    Böck, A.4
  • 48
    • 0021879256 scopus 로고
    • Crystallographic refinement of yeast aspartic acid transfer RNA
    • Westhof, E., Dumas, P. and Moras, D. (1985) Crystallographic refinement of yeast aspartic acid transfer RNA. J. Mol. Biol., 184, 119-145.
    • (1985) J. Mol. Biol. , vol.184 , pp. 119-145
    • Westhof, E.1    Dumas, P.2    Moras, D.3
  • 49
    • 0026587746 scopus 로고
    • NMR analysis of helix I from the 5S RNA of Escherichia coli
    • White, S.A., Nilges, M., Huang, A., Brünger, A.T. and Moore, P.B. (1992) NMR analysis of helix I from the 5S RNA of Escherichia coli. Biochemistry, 31, 1610-1621.
    • (1992) Biochemistry , vol.31 , pp. 1610-1621
    • White, S.A.1    Nilges, M.2    Huang, A.3    Brünger, A.T.4    Moore, P.B.5
  • 50
    • 0020338428 scopus 로고
    • The site of interaction of aminoacyl-tRNA with elongation factor Tu
    • Wikman, F.P., Siboska, G.E., Petersen, H.U. and Clark, B.F.C. (1982) The site of interaction of aminoacyl-tRNA with elongation factor Tu. EMBO J., 1, 1095-1100.
    • (1982) EMBO J. , vol.1 , pp. 1095-1100
    • Wikman, F.P.1    Siboska, G.E.2    Petersen, H.U.3    Clark, B.F.C.4
  • 52
    • 0027979223 scopus 로고
    • Ser function as major identity elements for serylation in an orientation-dependent, but not sequence-specific manner
    • Ser function as major identity elements for serylation in an orientation-dependent, but not sequence-specific manner. EMBO J., 13, 241-248.
    • (1994) EMBO J. , vol.13 , pp. 241-248
    • Wu, X.-Q.1    Gross, H.J.2
  • 53
    • 0025748046 scopus 로고
    • Synthesis and purification of large amounts of RNA oligonucleotides
    • Wyatt, J.R., Chastain, M. and Puglisi, J.D. (1991) Synthesis and purification of large amounts of RNA oligonucleotides. BioTechniques, 11, 764-769.
    • (1991) BioTechniques , vol.11 , pp. 764-769
    • Wyatt, J.R.1    Chastain, M.2    Puglisi, J.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.