Disease relevance of relA

• Identification and characterization of a second, inducible promoter of relA in Escherichia coli [1].

High impact information on relA

• We find that rRNA synthesized from plasmids does exhibit a relA-dependent, stringent response [2].
• 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].
• 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 [5].
• The presence of a relA mutant allele affects the kinetics of cyclic adenosine 3',5'-monophosphate accumulation during downshift from glucose to succinate [6].

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 [7].
• Effect of amino acid deprivation and chloramphenicol treatment on cell sizes of rel+ and relA- strains of Escherichia coli [8].

Biological context of relA

• Partial suppression of the lysis-resistant phenotype was also observed in a relA genetic background [9].
• Amino acid deprivation resulted in a reduction in the cell sizes of rel+ strains but not of relA- strains [8].

References