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Gene Review

argU  -  tRNA

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0529, JWR0010, dnaY, fimU, pin
 
 
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Disease relevance of argU

  • The large putative Rep protein encoded by pME2001 was overexpressed in Escherichia coli as an N-terminal His-tagged version using pET28a and a compatible helper plasmid that coexpresses minor tRNAs, argU and ileX to compensate for codon usage difference [1].
  • Additional homologies to lambdoid phages were found in the 25 kb clockwise of argU [2].
  • Characterization of the cryptic lambdoid prophage DLP12 of Escherichia coli and overlap of the DLP12 integrase gene with the tRNA gene argU [2].
  • The 77-bp DNA sequence of fimU from S. enteritidis was identical to that of fimU encoding tRNA(Arg) (UCU) from Salmonella typhimurium and 96% identical to that of the Escherichia coli argU homolog [3].
  • The gene coding for the 3C protease from human rhinovirus strain 1B was efficiently expressed in an Escherichia coli strain which also overexpressed the rare argU tRNA [4].
 

High impact information on argU

  • In addition, the production of a number of proteins resolved by two-dimensional gel electrophoresis was enhanced significantly during the stationary phase in the cells harboring a plasmid containing argU [5].
  • Overproduction of the complex was further enhanced when the Escherichia coli argU gene encoding the rare arginine tRNA was also overproduced [6].
  • To investigate the affects of fimU on FimY production, a FimY fusion with the E. coli maltose-binding protein was constructed and expressed in an E. coli argU background [7].
  • At 43 degrees C, the cellular level of the argU10(Ts) tRNA is further reduced to a trace amount, while neither the cellular abundance nor the aminoacylation level of the wild-type argU tRNA changes [8].
  • The Escherichia coli argU10(Ts) phenotype is caused by a reduction in the cellular level of the argU tRNA for the rare codons AGA and AGG [8].
 

Chemical compound and disease context of argU

 

Biological context of argU

  • Expression proved successful by transforming pET28_Af_Exo in Origami B(DE3) containing a tRNA plasmid with extra copies of argU, ileY and leuW tRNA genes as a host strain [11].
  • Unlike other tRNA operons, however, argU expression is severely inhibited by sequences downstream of the transcription start point [12].
  • Coexpression of E. coli argU dramatically enhanced both cell growth and expression of KAM [13].
  • The argU (dnaY) gene of Escherichia coli is located, in clockwise orientation, at 577.5 kilobases (kb) on the chromosome physical map [2].
  • The argU and DLP12 int genes overlapped at their 3' ends, and argU contained sequence homologous to a portion of the phage P22 attP site [2].
 

Associations of argU with chemical compounds

  • The effect of the pin3 mutation is abolished by the wild-type allele of argU, an arginine tRNA that reads the rare Arg codons AGA and AGG, which are used for eight of the 14 Arg codons in the old gene [14].
  • Co-expression of the dnaY gene completely blocks mistranslation of arginine to lysine during a1 overexpression in minimal media, and homogeneous protein is produced [15].
 

Other interactions of argU

  • Hence, by using modified BL21(DE3) E. coli cells, namely BL21-CodonPlus(DE3)-RIL cells (Stratagene) with extra copies of E. coli argU, ileY, and leuW tRNA genes, it was possible to attain high-level expression of the proteins affected by rare codon usage [16].
 

Analytical, diagnostic and therapeutic context of argU

  • Western blots of extracts from the argU mutant and parental strain indicated that production of FimY was significantly reduced in the absence of a functional tRNAArg(UCU) [7].
  • In the present study, argU tRNA was purified from E. coli A19 strain and nucleoside N* was characterized by the TLC and HPLC analyses [9].

References

  1. Comparative sequence analysis of plasmids pME2001 and pME2200 of methanothermobacter marburgensis strains Marburg and ZH3. Luo, Y., Leisinger, T., Wasserfallen, A. Plasmid (2001) [Pubmed]
  2. Characterization of the cryptic lambdoid prophage DLP12 of Escherichia coli and overlap of the DLP12 integrase gene with the tRNA gene argU. Lindsey, D.F., Mullin, D.A., Walker, J.R. J. Bacteriol. (1989) [Pubmed]
  3. tRNA(Arg) (fimU) and expression of SEF14 and SEF21 in Salmonella enteritidis. Clouthier, S.C., Collinson, S.K., White, A.P., Banser, P.A., Kay, W.W. J. Bacteriol. (1998) [Pubmed]
  4. Inhibition of 3C protease from human rhinovirus strain 1B by peptidyl bromomethylketonehydrazides. Kati, W.M., Sham, H.L., McCall, J.O., Montgomery, D.A., Wang, G.T., Rosenbrook, W., Miesbauer, L., Buko, A., Norbeck, D.W. Arch. Biochem. Biophys. (1999) [Pubmed]
  5. Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli. Chen, G.T., Inouye, M. Genes Dev. (1994) [Pubmed]
  6. Overproduction in Escherichia coli and characterization of yeast replication factor C lacking the ligase homology domain. Gomes, X.V., Gary, S.L., Burgers, P.M. J. Biol. Chem. (2000) [Pubmed]
  7. Control of FimY translation and type 1 fimbrial production by the arginine tRNA encoded by fimU in Salmonella enterica serovar Typhimurium. Tinker, J.K., Clegg, S. Mol. Microbiol. (2001) [Pubmed]
  8. The Escherichia coli argU10(Ts) phenotype is caused by a reduction in the cellular level of the argU tRNA for the rare codons AGA and AGG. Sakamoto, K., Ishimaru, S., Kobayashi, T., Walker, J.R., Yokoyama, S. J. Bacteriol. (2004) [Pubmed]
  9. A modified uridine in the first position of the anticodon of a minor species of arginine tRNA, the argU gene product, from Escherichia coli. Sakamoto, K., Kawai, G., Niimi, T., Satoh, T., Sekine, M., Yamaizumi, Z., Nishimura, S., Miyazawa, T., Yokoyama, S. Eur. J. Biochem. (1993) [Pubmed]
  10. The expression of proUK in Escherichia coli: the vgb promoter replaces IPTG and coexpression of argU compensates for rare codons in a hypoxic induction model. Jiang, L., Yang, Y., Chatterjee, S., Seidel, B., Wolf, G., Yang, S. Biosci. Biotechnol. Biochem. (1999) [Pubmed]
  11. The xthA gene product of Archaeoglobus fulgidus is an unspecific DNase. Miertzschke, M., Greiner-Stöffele, T. Eur. J. Biochem. (2003) [Pubmed]
  12. Expression of argU, the Escherichia coli gene coding for a rare arginine tRNA. Saxena, P., Walker, J.R. J. Bacteriol. (1992) [Pubmed]
  13. Lysine 2,3-aminomutase from Clostridium subterminale SB4: mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli. Ruzicka, F.J., Lieder, K.W., Frey, P.A. J. Bacteriol. (2000) [Pubmed]
  14. The P2 phage old gene: sequence, transcription and translational control. Haggård-Ljungquist, E., Barreiro, V., Calendar, R., Kurnit, D.M., Cheng, H. Gene (1989) [Pubmed]
  15. High level, context dependent misincorporation of lysine for arginine in Saccharomyces cerevisiae a1 homeodomain expressed in Escherichia coli. Forman, M.D., Stack, R.F., Masters, P.S., Hauer, C.R., Baxter, S.M. Protein Sci. (1998) [Pubmed]
  16. Use of modified BL21(DE3) Escherichia coli cells for high-level expression of recombinant peanut allergens affected by poor codon usage. Kleber-Janke, T., Becker, W.M. Protein Expr. Purif. (2000) [Pubmed]
 
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