Disease relevance of relA

• The nucleotide sequence and characterization of the relA gene of Escherichia coli [1].

High impact information on relA

• We find that rRNA synthesized from plasmids does exhibit a relA-dependent, stringent response [2].
• A promoter has been identified that directs relA gene transcription towards the pyrG gene, in a counterclockwise direction on the E. coli chromosome [1].
• The relA gene product of Escherichia coli is known to be responsible for the synthesis of guanosine 3',5'-bispyrophosphate (ppGpp) during the stringent response to amino acid starvation [1].
• The activation was dependent on relA and spoT, which encode enzymes for the synthesis and degradation of ppGpp, and on dksA, which encodes an RNA polymerase accessory protein required for the stringent response [3].
• The genome of Borrelia burgdorferi encodes a single chromosomal rel gene (BB0198) (B. burgdorferi rel [rel(Bbu)]) homologous to relA and spoT of E. coli [4].

Chemical compound and disease context of relA

• The global transcriptional regulator (p)ppGpp (guanosine-3'-diphosphate-5'-triphosphate and guanosine-3',5'-bisphosphate, collectively) produced by the relA and spoT genes in Escherichia coli allows bacteria to adapt to different environmental stresses [4].
• In this study, we demonstrate that overexpression of the relA gene, encoding ppGpp synthetase, increases the accumulation of amino acids, such as glutamate and lysine, in amino-acid-overproducing strains of E. coli [5].
• High amplification rates of pBR322 plasmid DNA were observed in E. coli CP79 (relA) and E. coli CP143 (relA) in both batch and fed-batch cultivation after exhaustion of the amino acid arginine [6].

Biological context of relA

• Genomic Southern blot analyses verify that the relA regions cloned and subjected to nucleotide sequence analysis correspond to homologous regions on the E. coli chromosome [1].
• The effects of inhibition of protein synthesis on the cell size distributions of rel+ and relA- derivatives of Escherichia coli K-12 were determined [7].

Anatomical context of relA

• Subsequent in vitro assays using ribosomes isolated from wild-type and relA and relC mutant strains confirmed that (p)ppGpp is synthesized by ribosomes and that mutation of RelA or L11 blocks that activity [8].

Associations of relA with chemical compounds

• In contrast, derepression of the tryptophan biosynthetic enzyme, but not of the arginine biosynthetic enzyme, was inhibited during the relaxed response produced in an isogenic relA strain by the partial deprivation of valyl transfer ribonucleic acid [9].

Other interactions of relA

• In the absence of rpoZ, the promoter for the relA gene was severely impaired, but the promoters from the ribosomal protein genes were not affected as much [10].

Analytical, diagnostic and therapeutic context of relA

• The apparent molecular mass of the cloned relA gene product is calculated to be 83,856 daltons and as visualized by immunoblotting is identical to that of the previously characterized protein [1].

References