Disease relevance of trpE

• Nucleotide sequence of Escherichia coli trpE. Anthranilate synthetase component I contains no tryptophan residues [1].
• 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 [2].
• Plasmid vectors were constructed which expressed three adenovirus tumor antigens fused to a portion of the trpE protein of Escherichia coli [3].
• The ribonucleoprotein gene of infectious hematopoietic necrosis virus (IHNV) has been expressed in Escherichia coli as a trpE fusion protein [4].
• To permit the isolation of large quantities of the gene product, we expressed various portions of the pol gene of Moloney murine leukemia virus (M-MuLV) as trpE fusion proteins in Escherichia coli [5].

High impact information on trpE

• Restriction fragments of DNA derived from a cDNA clone of the alpha subunit of the acetylcholine receptor were subcloned in Escherichia coli by using the trpE fusion vector, pATH2 [6].
• The v-abl oncogene was expressed in Escherichia coli as a trpE/v-abl fusion protein from the trp promoter [7].
• A region in the skeletal muscle ryanodine receptor between amino acids 4014 and 4765 was expressed as a trpE fusion protein [8].
• Using antibodies against synthetic peptides and trpE fusion proteins, we detected an 81-kDa protein encoded by this open reading frame in mitochondrial preparations from the plasmid-containing strains [9].
• We have prepared fusion polypeptide genes from fragments of chloroplast DNA homologous to bacterial RNA polymerase subunit genes and expression vectors carrying portions of the anthranilate synthetase gene (trpE) [10].

Chemical compound and disease context of trpE

• The genes trpE and trpG of the hyperthermophilic archaeon Sulfolobus solfataricus, encoding the components I and II of anthranilate synthase, were cloned and co-expressed in Escherichia coli [11].
• All the mutated genes except one, the gene encoding an ASI mutant with histidine in place of Arg452 (R452H ASI) complemented an E. coli (trpE) [12].

Biological context of trpE

• The 5'-flanking region encodes two open reading frames (ORFs); one corresponds to trpL, while the other corresponds to the N-terminal half of the trpE gene [13].
• This plasmid construct promotes a high level of expression of the trpE/COR1 hybrid protein [14].
• The amino acid sequences, alpha 184-200 and alpha 184-196 of the Torpedo californica alpha-subunit of the nicotinic acetylcholine receptor were expressed as trpE fusion proteins via the expression vector pATH2 and a method for the enrichment of these fusion proteins is described [15].
• The expression system was programmed with a plasmid containing a trpE-prfB fusion gene so that each of the products of the competing events could be measured [16].
• Abolition of secondary structure increased mu protein expression over ninety-fold, to a level approximately equal to that of a trpE -mu fusion protein using the native trpE ribosome binding site [17].

Associations of trpE with chemical compounds

• One of the genomic clones had high sequence similarity to the tryptophan synthesis gene anthranilate synthase component I (trpE) [18].
• We propose that pabB and trpE arose from a common ancestor and hence that there is a common ancestry of genes encoding p-aminobenzoate synthetase and anthranilate synthetase [19].
• Nucleotide sequence of trpE, anthranilate synthase I gene, of Bacillus caldotenax [20].
• We conclude that during transcription of the trp operon RNA polymerase frequently is rejected at a specific site ahead of the first structural gene, trpE [21].
• The N-terminal amino acid sequence is the same as expected from DNA sequence of trpE except that the N-terminal methionine is lacking [12].

Other interactions of trpE

• Here we present the nucleotide sequence of pabB and compare it with that of trpE [19].

Analytical, diagnostic and therapeutic context of trpE

• The resulting plasmids, pXL2, pXL3, and pXL7, encoded trpE-G fusion proteins subsequently detected with anti-infectious hematopoietic necrosis virus sera by Western immunoblots [22].
• Molecular cloning and nucleotide sequence of Thermus thermophilus HB8 trpE and trpG [23].

References