The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

tRNA-Trp  -  tRNA

Kazachstania servazzii

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of tRNA-Trp


High impact information on tRNA-Trp

  • A gene for Saccharomyces cerevisiae tRNATrp has been sequenced which contains an intervening sequence of 34 bp (H. S. Kang and J. Abelson, unpublished results) [3].
  • A nuclear extract from Xenopus oocytes is capable of supporting transcription of the tRNATrp gene contained on plasmid pBR313 [3].
  • DNA sequence analysis of this gene revealed that the mitochondrial tRNATrp anticodon is 5'UCA3'. Because there is a U in the wobble position, this tRNA can recognize and insert tryptophan into a growing polypeptide chain in response to the nonsense codon UGA [4].
  • This RNA was transcribed from a cluster of repetitive sequences: both intact and truncated delta and sigma elements adjacent to a tRNATrp gene [5].
  • Transcripts from this hybrid gene were found to be processed by endonuclease and ligase at the tRNATrp exon-intron boundaries [6].

Biological context of tRNA-Trp

  • The rate of aminoacylation of the procaryotic tRNATrp by the enzyme is three orders of magnitude lower [7].
  • The sequence of wheat germ tRNATrp as determined by [32P] post-labelling techniques is: [sequence in text] The interesting features are: (i) Presence of a C11:G24 base pair in contrast to the U11:G24 in E. coli Su- tRNATrp [8].
  • Oxidized tRNATrp (but not tRNATrp without the 3'-A) accelerates tryptophan-dependent hydrolysis of ATP catalyzed by the enzyme [9].
  • The pattern of phosphate alkylation of tRNATrp is very similar to that found with other tRNAs studied before using the same approach with protected phosphates mainly located in the D and T psi arms [10].
  • The Saccharomyces cerevisiae haploid genome includes six copies of the gene encoding tRNATrp which are scattered on five chromosomes [11].

Anatomical context of tRNA-Trp


Associations of tRNA-Trp with chemical compounds

  • Once tRNATrp is added to the synthetase.adenylate complex, the protective effect of the adenylate disappears [9].
  • The same effects are found also in the presence of tRNATrp oxidized with NaI04 and tRNATrp lacking the 3'-terminal adenosine [9].
  • Alkylation in beef tRNATrp of phosphodiester bonds by ethylnitrosourea and of N-7 in guanosines and N-3 in cytidines by dimethyl sulfate and carbethoxylation of N-7 in adenosines by diethyl pyrocarbonate were investigated under various conditions [10].
  • The method has been applied for mapping exposed cytosine bases in tRNATrp (yeast) which have been found in the anti-codon loop and at the 3'-end of the molecule [13].
  • Analysis of the base compositions showed that isoacceptor B differed from isoacceptor A in one respect only: 2'-O-methylguanosine, a modified guanosine base occurring at position 17 of the major isoacceptor A tRNATrp, was not detectable in hydrolysates of purified isoacceptor B [14].

Analytical, diagnostic and therapeutic context of tRNA-Trp

  • We have used site-directed mutagenesis to convert the anticodon of a cloned tRNATrp gene from CCA to CTA with the expectation that this gene would produce tRNA molecules capable of interacting with the UAG terminator codon [15].
  • Northern blot analyses of the steady state levels of tRNATrp in cells containing the high copy-number clones reveal 20-100% increases in the abundance of tRNATrp [16].


  1. Position of aminoacylation of individual Escherichia coli and yeast tRNAs. Hecht, S.M., Chinualt, A.C. Proc. Natl. Acad. Sci. U.S.A. (1976) [Pubmed]
  2. Specific binding of tryptophan transfer RNA to avian myeloblastosis virus RNA-dependent DNA polymerase (reverse transcriptase). Panet, A., Haseltine, W.A., Baltimore, D., Peters, G., Harada, F., Dahlberg, J.E. Proc. Natl. Acad. Sci. U.S.A. (1975) [Pubmed]
  3. In vitro transcription and processing of a yeast tRNA gene containing an intervening sequence. Ogden, R.C., Beckman, J.S., Abelson, J., Kang, H.S., Söll, D., Schmidt, O. Cell (1979) [Pubmed]
  4. Yeast mitochondrial tRNATrp can recognize the nonsense codon UGA. Martin, N.C., Pham, H.D., Underbrink-Lyon, K., Miller, D., Donelson, J.E. Nature (1980) [Pubmed]
  5. The yeast repeated element sigma contains a hormone-inducible promoter. Van Arsdell, S.W., Stetler, G.L., Thorner, J. Mol. Cell. Biol. (1987) [Pubmed]
  6. Splicing of intron-containing tRNATrp by the archaeon Haloferax volcanii occurs independent of mature tRNA structure. Armbruster, D.W., Daniels, C.J. J. Biol. Chem. (1997) [Pubmed]
  7. Aminoacylation of tRNA Trp from beef liver, yeast and E. coli by beef pancrease tryptophan-tRNA ligase. Stoichiometry of tRNATrp binding. Dorizzi, M., Merault, G., Fournier, M., Labouesse, J., Keith, G., Dirheimer, G., Buckingham, R.H. Nucleic Acids Res. (1977) [Pubmed]
  8. Structure and function of tryptophan tRNA from wheat germ. Ghosh, K., Ghosh, H.P. Nucleic Acids Res. (1984) [Pubmed]
  9. The effect of tRNA and tryptophanyl adenylate on limited proteolysis of beef pancreas tryptophanyl-tRNA synthetase. Scheinker, V.S., Beresten, S.F., Degtyarev, S.K., Kisselev, L.L. Nucleic Acids Res. (1979) [Pubmed]
  10. Tertiary structure of animal tRNATrp in solution and interaction of tRNATrp with tryptophanyl-tRNA synthetase. Garret, M., Labouesse, B., Litvak, S., Romby, P., Ebel, J.P., Giegé, R. Eur. J. Biochem. (1984) [Pubmed]
  11. Functional differences among the six Saccharomyces cerevisiae tRNATrp genes. Ong, W.C., Ibrahim, M., Town, M., Johnson, J.D. Yeast (1997) [Pubmed]
  12. Sequence and codon recognition of bean mitochondria and chloroplast tRNAsTrp: evidence for a high degree of homology. Maréchal, L., Guillemaut, P., Grienenberger, J.M., Jeannin, G., Weil, J.H. Nucleic Acids Res. (1985) [Pubmed]
  13. A rapid method for mapping exposed cytosines in polyribonucleotides. Application to tRNATrp (yeast, beef liver). Mashkova, T.D., Mazo, A.M., Scheinker, V.S., Beresten, S.F., Bogdanova, S.L., Avdonina, T.A., Kisselev, L.L. Mol. Biol. Rep. (1980) [Pubmed]
  14. Accumulation of 2'-O-methylguanosine deficient tRNATrp in tryptophan limited Saccharomyces cerevisiae. Stäheli, P., Agris, P.F., Niederberger, P., Gehrke, C.W., Hütter, R. J. Gen. Microbiol. (1982) [Pubmed]
  15. Construction, expression, and function of a new yeast amber suppressor, tRNATrpA. Kim, D., Johnson, J. J. Biol. Chem. (1988) [Pubmed]
  16. Yeast tRNATrp genes with anticodons corresponding to UAA and UGA nonsense codons. Kim, D., Raymond, G.J., Clark, S.D., Vranka, J.A., Johnson, J.D. Nucleic Acids Res. (1990) [Pubmed]
WikiGenes - Universities