Disease relevance of trpC

• For this purpose an in-frame gene fusion between the A. niger trpC and Escherichia coli lacZ genes was constructed and shown to be functionally expressed after introduction into A. niger by cotransformation with the pyrA gene as selective marker [1].
• Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium [2].
• We have cloned the trifunctional trpC gene from Aspergillus nidulans by hybrid phage lambda complementation of an Escherichia coli trpC mutant lacking phosphoribosylanthranilate isomerase activity [3].
• The products of trpE, trpG, and trpC from S. solfataricus were compared to the homologous products from a eukaryote, a eubacterium, and two archaebacteria, namely, a methanogen and an extreme halophile [4].
• The sequence of a symbiotically essential Bradyrhizobium japonicum operon consisting of trpD, trpC and a moaC-like gene [5].

High impact information on trpC

• We have determined the nucleotide sequence of a secondary lambda attachment site in trpC [6].
• This 6 nucleotide sequence is also present in the intact trpC genome at the attachment site, as shown by analysis of trpC mRNA spanning this region [6].
• Plasmid subclones containing this region also complemented the E. coli trpC mutant [3].
• Results from nutritional experiments with an A. nidulans trpC mutant suggest that developmental regulation of trpC mRNA levels may be related to a high requirement for tryptophan or a compound derived from tryptophan during conidiation [3].
• Based on comparisons of TRP3 amino acid sequence with homologous sequences from E. coli and Neurospora crassa, an 11-amino acid residue connecting segment was identified which fuses the trpG and trpC functions of the bifunctional TRP3 protein chain [7].

Chemical compound and disease context of trpC

• Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions [8].
• We have completed the nucleotide sequence determination of trpD and trpC, the second and third genes of the trp operon of Salmonella typhimurium [2].
• An attempt was made to transform Alternaria alternata protoplasts using a plasmid vector, pDH25, bearing the Escherichia coli hygromycin B (Hy) phosphotransferase gene (hph) under the control of the Aspergillus nidulans trpC promoter [9].
• The E. coli trp fragment is cloned in a HindIII site within a chloramphenicol acetyltransferase gene present on pPL608, and as a result, expression of the E. coli trpC gene product is inducible by chloramphenicol [10].

Biological context of trpC

• Biochemical analysis of the cotransformants indicated that in nearly all cases the fusion gene had replaced the wild-type trpC gene [1].
• To obtain A. niger trpC mutants in a direct way, gene inactivation by cotransformation was performed [1].
• Tryptophan auxotrophic mutants in Aspergillus niger: inactivation of the trpC gene by cotransformation mutagenesis [1].
• E. coli trpE polar mutations are 10 time more polar on trpD gene expression than on downstream (trpC, B, or A) gene expression [11].
• Genetic analysis suggested the presence of an internal promoter upstream from the trpC gene, yet no typical consensus sequences were found [12].

Associations of trpC with chemical compounds

• These genes encode two bifunctional proteins thought to have arisen by gene fusions: the trpD polypeptide contains the glutamine amido transferase and the phosphoribosyl anthranilate transferase activities, and the trpC protein possesses the N-(5'-phosphoribosyl)-anthranilic acid isomerase and the indole-3-glycerol phosphate synthetase activities [2].
• To obtain a better understanding of this sluggishness, we used DNA shuffling to mutagenize the trpC gene, which encodes indoleglycerol phosphate synthase, from the hyperthermophile Sulfolobus solfataricus [13].
• Phosphoribosylanthranilate (PRA) isomerase activity, which is also carried by the trpC protein, is unstable during starvation for ammonium, cysteine, or sulfate but is stable under other nongrowing conditions where InGP synthetase is not [14].

Regulatory relationships of trpC

• The plasmid pAJ24JI suppressed trpA, B and F mutants, pAJ73JI suppressed trpC and D and pAJ88JI suppressed a trpE mutant [15].

Other interactions of trpC

• The products of the operator-distal structural genes trpC, trpB, and trpA are formed at rates approximately 15-fold higher than those of wild type [16].
• High-level expression of TrpC-TonB protein in the absence of tryptophan results in virtually immediate cessation of growth for strains carrying the trpC-tonB plasmid [17].
• An amdS320 strain was transformed to AmdS+ and cotransformed with a DNA fragment containing a fusion between a non-functional A. nidulans trpC gene and the Escherichia coli lacZ gene [18].
• We have shown that the Aspergillus nidulans ans1 sequence enhances the efficiency of transformation when introduced into vectors containing argB or trpC genes [19].

Analytical, diagnostic and therapeutic context of trpC

• Southern blot analysis of DNA from these Trp+ transformants showed that plasmid DNA was present but that this DNA was not integrated at the site of the chromosomal trpC locus [20].
• The A. niger trpC gene was localized on the cloned fragment by heterologous hybridization experiments and sequence analysis [20].
• The utility of this "instant gene bank" technique is demonstrated here by the molecular cloning of the P. canescens trpC gene [21].

References