Abstract
Transfer RNAs contain many modified nucleosides, which are derivatives of the four normal nucleosides. At present more than 75 different modified nucleosides are characterised (Edmonds et al., 1991). The synthesis of the majority of the modified nucleosides is carried out on the preformed precursor tRNA except in two cases. Queuine and hypoxanthine are synthesised from guanine and adenine, respectively, and then incorporated into the tRNA through an exchange reaction. The synthesis of these 75 modified nucleosides is catalysed by enzymes, which are highly specific, not only for the nucleoside that they modify but also for the position of the target nucleoside in the tRNA. For example there are different enzymes catalysing the formation of Ψ in the anticodon stem and in the TΨC-loop (Singer et al., 1972). The importance of tRNA modification is reflected by the fact that about 1% of the genetic information in Escherichia coli and Salmonella typhimurium is devoted to the synthesis of tRNA modifying enzymes, which is 4-fold more than that used for the synthesis of their substrate, tRNA (Björk, 1992). This paper will discuss the function of three modified nucleosides present in the anticodon region. Mutants defective in their synthesis have been used to study their role in cell physiology and in the decoding process.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Avis, P.F., Armstrong, D. J., Schäfer, K. P., and Söll, D. (1975). Maturation of ahypermodified nucleoside in transfer RNA. Nucl. Acids Res. 2: 691–698.
W.M. Barnes 1978 region: seven histidine codons in a row. Proc. Natl. Acad. Sci.(USA), 75: 42–81
Björk, G. R. (1984). Transfer RNA modification in different organisms. Chemica Scripta. 26B: 91–95.
Björk G. R. (1992). The role of modified nucleosides in transfer RNA interactions. in: “Transfer RNA in protein synthesis”. Hatfield, D. L., Lee, B. J., and, Pirtle R. M., eds, CRC press, Boca Raton, FL.
Björk, G. R., Wikström, P. M., and Byström, A. S. (1989). Prevention of translational frameshifting by the modified nucleoside 1-Methylguanosine. Science 244: 986–989.
Bossi, L., and Roth, J. R.. (1980). The influence of codon context on genetic code translation. Nature 286:123–127.
Bouadloun, F, Srichaiyo, T., Isaksson L. A., and Björk G. R. (1986). Influence of modification next to the anticodon in tRNA on codon context sensitivity of translational suppression and accuracy. J. Bacteriol. 166: 1022–1027.
Buck M., and Ames B. N. (1984). A modified nucleotide in tRNA as a possible regulator of aerobiosis: Synthesis of cis-2-methyl-thioribosylzeatin in tRNA of Salmonella. Cell 36: 523–531.
Buck, M., McCloskey, J. A., Basile, B., and Ames, B. N. (1982). Cis-2-methylthioribosylzeatin (ms2io6A) is present in transfer RNA of Salmonella typhimurium, but not Escherichia coll. Nucl. Acids Res. 10: 5649–5662.
Byström, A. S., Hjalmarsson, K. J., Wikström, P. M., and Björk, G. R. (1983). The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21-K polypeptide. EMBO J. 2: 899–905.
Carter, P. W., Weiss, D. L., Weith, H. L., and Calvo J. M. (1985). Mutations that convert the four leucine codons of the Salmonella typhimurium leu leader to four threonine codons. J. Bacteriol. 162: 943–949.
Connolly, D. M., and Winkler, M.E. (1991). Structure of Escherichia coli K-12 miaA and characterization of the mutator phenotype caused by miaA insertion mutations. J. Bacteriol. 173: 1711–1721.
Cortese, R., Kammen, H. O., Spengler, S. J., and Ames B. N. (1974).Biosynthesis ofpseudouridine in transfer ribonucleic acid. J. Biol. Chem. 249: 1103–1108.
Craigen, W. J., Cook, R. G., Tate, W. P., and Caskey, C. T. (1985). Proc. Natl. Acad. Sci.USA 82: 3616–3620.
Curran, J. F., and Yarus, M. (1987). Reading frame selection and transfer RNA anticodon loop stacking. Science 238: 1545–1550.
Curran, J. F., and Yarus, M. (1988). Use of tRNA suppressors to probe the regulation of Escherichia coli release factor 2. J. Mol. Biol. 203: 75–83.
Curran, J. F., and Yarus, M. 1989. Rates of aminoacyl-tRNA selection at 29 sense codons in vivo. J. Mol. Biol. 209: 65–77.
Diaz, I., and Ehrenberg, M. (1992). ms2i6A deficiency enhances proofreading in translation. J. Mol. Biol. 222: 1161–1171.
Edmonds, C. G., Crain, P. F., Gupta, R., Hashizume, T., Hocart, C. H., Kowalak, J. A., Pomerantz, S. C.,. Stetter K. O, and McCloskey, J. A..(1991). Posttranscriptional modification of tRNA in thermophilic Archaea (Archaebacteria). J Bacteriol. 173: 3138–3148.
Eisenberg, S. P., Yarus, M., and, Soll, L. 1979. The effect of an Escherichia coil regulatory mutation on transfer RNA structure. J. Mol. Biol. 135: 111–126.
Ericson, J. U., and Björk, G. R. 1986. Pleiotropic effects induced by modification deficiency next to the anticodon of tRNA from Salmonella typhimurium LT2. J. Bacteriol. 166: 1013–1021.
Ericson, J. U., and Björk, G. R. (1991). tRNA anticodons with the modified nucleoside 2methylthio-N6-(4-hydroxyisopentenyl)adenosine distinguish between bases 3’ of the codon. J Mol. Biol. 218: 509–516.
Gaber R. F. and, Culbertson M. R. (1984). Codon recognition during frameshift suppression in Saccharomyces cerevisiae. Mol.Cell.Biol 4: 2052–2061.
Griffiths, E., and, Humphreys, J. 1978. Alterations in tRNAs containing 2-methylthio-N6-A 2-isopentenyl)-adenosine during growth of enteropathogenic Escherichia coli in the presence of iron-binding proteins. Eur. J. Biochem. 82: 503–513.
Grosjean, H., K. Nicoghosian, K., Haumont, E., Söll, D. and, Cedergren, R. 1985. Nucleotide sequences of two serine tRNAs with a GGA anticodon: The structure-function relationships in the serine family of E. coli tRNAs. Nucl. Acid Res. 13: 5697–5706.
Hagervall, T. G., Tuohy, T. M. F., Atkins J. F. and, Björk, G. R. (1992). Deficiency of 1methylguanosine in tRNA from Salmonella typhimurium induces frameshifting by quadruplet translocation. J. Mol Biol. Submitted.
Hagervall, T. G., Ericson, J. U., Esberg, K. B., Ji-nong, L. and, Björk, G. R. 1990. Role tRNA modification in translation fidelity. Biochem. Biophys. Acta 1050: 263–266.
Hall, R. H. The modified nucleosides in nucleic acids. Columbia University Press. 1971. Johnston, H. M., Barnes, W. M., Chumley, F. G., Bossi, L., and Roth, J. R. Model for regulation of the histidine operon of Salmonella. Proc. Natl. Acad. Sci. (USA). 77: 508, 1980.
Komine Y., Adachi T., Inokuchi H., Ozeki H. (1990). Genomic organization and physical mapping of the transfer RNA genes in Escherichia coli K12. J. Mol. Biol. 212: 579–598.
Newmark R. A. & Cantor C. R. (1968). Nuclear magnetic resonance study of the interactions of guanosine and cytidine in dimethyl sulfoxide. J. Am. Chem. Soc. 90: 5010–5017.
Palmer, D. T., P. H. Blum, and S. W. Artz,1983. Effects of the hisT mutation of Salmonella typhimurium on translation elongation rate. J. Bacteriol. 153: 357–363.
Parker, J. 1982. Specific mistranslation in hisT mutants of Escherichia coli Mol Gen. Genet. 187: 405–409.
Pieczenik G. (1980). Predicting coding function from nucleotide sequence or survival of “fitness” of tRNA. Proc. Natl. Acad. Sci. USA. 77: 3539–3543.
Rosenberg, A. H., and M. L. Gefter. 1969. An iron-dependent modification of several transfer RNA species in Escherichia coll. J. Mol. Biol. 46: 581–584.
Roth, J. R, D. N. Anton, and P. E. Hartman. 1966. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties.J. Mol. Biol. 22: 305–323.
Singer, C., Smith G. R., Cortese C., and Ames B. N. (1972). Mutant tRNA ineffective in repression and lacking two pseudouridine modifications. Nature (London) New Biol. 238: 72.
Sprinzl M., Dank N., Nock S., Schön A. (1991). Compilation of tRNA sequences and sequences of tRNA genes. Nucleic Acids Res. 19: supplement, 2127–2171.
Sroga G. E., Nemoto F., Kuchino Y. and, Björk G. R. (1992). Insertion in the anticodon loop or base substitution (sufC) in the anticodon stem of tRNA PZ from Salmonella typhimurium induces suppression of frameshift mutations. Nucl. Acids. Res. 20:3463–3469.
Turnbough Jr., C. L., Neill, R. J., Landsberg, R. and, Ames, B. N. (1979). Pseudouridylation of tRNAs and its role in regulation in Salmonella typhimurium. J. Biol. Chem. 254: 5111–5119.
Weiss R. B:, Dunn D. M., Atkins J. F., Gesteland R. F. (1987). Slippery runs, shifty stops, backward steps and forward hops: -2, -1, +1, +2, +5, and +6 ribosomal frameshifting. Cold Spring Harbor Symp. Quant. Biol. 52: 687–693.
Weiss, R. B., D. M. Dunn, J. E. Dahlberg, J. F. Atkins, and R. F. Gesteland. 1988. EMBO J. 7:1503–1507.
Weiss R. B., Dunn D. M., Atkins J. F., Gesteland R. F. (1990). Ribosomal frameshifting from -2 to +50 nucleotides. Prog Nucl Acid Mol Biol 39: 159–183.
Wettstein, F. O., and G. S. Stent. 1968. Physiologically induced changes in the property of phenylalanine tRNA in Escherichia coli. J. Mol. Biol. 38: 25–40.
Woese, C. R. 1967. in: “The genetic code. The molecular basis for genetic expression”. Harper and Row, p. 134.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media New York
About this chapter
Cite this chapter
Hagervall, T.G. et al. (1993). Functional Aspects of Three Modified Nucleosides, Ψ, ms2io6A, and m1G, Present in the Anticodon Loop of tRNA. In: Nierhaus, K.H., Franceschi, F., Subramanian, A.R., Erdmann, V.A., Wittmann-Liebold, B. (eds) The Translational Apparatus. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2407-6_7
Download citation
DOI: https://doi.org/10.1007/978-1-4615-2407-6_7
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6021-6
Online ISBN: 978-1-4615-2407-6
eBook Packages: Springer Book Archive