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

• A modified uridine in the first position of the anticodon of a minor species of arginine tRNA, the argU gene product, from Escherichia coli [9].
• 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 [10].

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