Disease relevance of arcA

• Regulation of the citrate synthase (gltA) gene of Escherichia coli in response to anaerobiosis and carbon supply: role of the arcA gene product [1].
• The AD gene, designated arcA, was expressed from recombinant bacteriophage or in cells harboring plasmid subclones from this phage at a level up to 1,000-fold lower than the level in fully derepressed S. sanguis but apparently under the control of its own promoter [2].
• Knockout mutations were constructed in the arcA gene of a virulent type b strain of Haemophilus influenzae, and the behavior of the resulting mutants was investigated in a number of conditions that mimicked distinct steps in the natural infection pathway [3].
• We assessed the effects of different arcA mutations on poly(3-hydroxybutyrate) (PHB) synthesis in recombinant Escherichia coli strains carrying the pha synthesis genes from Azotobacter sp. strain FA8 [4].

High impact information on arcA

• Deletion of the arcA gene caused about a 2-fold increase in the ptsG expression, and overexpression of ArcA significantly decreased glucose consumption [5].
• The arcA (dye) and arcB genes of Escherichia coli are responsible for anaerobic repression of target operons and regulons of aerobic function (the arc modulon) [6].
• The frequency of conjugal DNA transfer of plasmid R1-16, a derepressed variant of R1, was reduced by four orders of magnitude in an Escherichia coli host with a mutation in the arcA gene [7].
• Induction of fexA expression by chloramphenicol and florfenicol occurs via translational attenuation [8].
• fexA, a novel Staphylococcus lentus gene encoding resistance to florfenicol and chloramphenicol [8].

Chemical compound and disease context of arcA

• To systematically investigate the contribution of Arc- and Fnr-dependent regulation in catabolism, glucose-limited chemostat cultures were conducted on wild-type E. coli, an arcA mutant, an fnr mutant, and an arcAfnr double mutant strains under a well-defined semi-aerobic condition [9].
• Poly(3-hydroxybutyrate) synthesis by recombinant Escherichia coli arcA mutants in microaerobiosis [4].
• Functional citric acid cycle in an arcA mutant of Escherichia coli during growth with nitrate under anoxic conditions [10].

Biological context of arcA

• The negative control of sucABCD gene expression seen under anaerobic conditions, like that for the sdhCDAB genes, is provided by the arcA and fnr gene products [11].
• LacZ operon fusions were constructed and were inserted in single copies into strain MC4100 and into its fnr, arcA or hemA carrying derivatives [12].
• The arcA mutations used were an internal deletion and the arcA2 allele, a leaky mutation for some of the characteristics of the Arc phenotype which confers high respiratory capacity [4].
• Results from both the transposon array and insertion mutagenesis indicated that arcA, which is known to be a negative response regulator of genes in aerobic pathways, was important for competitiveness in E. coli PHL628 biofilms [13].
• It binds to a palindromic sequence, very similar to an Escherichia coli Crp binding site, located upstream from arcA [14].

Anatomical context of arcA

• Effect of the arcA Mutation on the Expression of Flagella Genes in Escherichia coli [15].

Associations of arcA with chemical compounds

• Levels of aerobic and anaerobic expression in glucose-containing minimal media were similar; both were unaffected by an arcA mutation [16].
• In an arcA-fnr double mutant, phi(cyd-lac) expression became insignificant, irrespective of the availability of O2 [17].
• In an arcA mutant devoid of the transcriptional regulator ArcA, glycerol was completely oxidized with nitrate as an electron acceptor, demonstrating derepression and function of the complete pathway [10].
• Moreover, an increase of DCCD-inhibited H+ efflux by added K+, as well as the characteristics of DCCD-sensitive H(+)-K(+)-exchange found in a parent strain, were lost in the arcA mutant with a defective Arc system, suggesting a repression of enzymes in respiratory pathways [18].
• It is proposed that the dye (sfrA) gene product is necessary not only for efficient transcription of the F factor genes, but also for some component(s) of the bacterial envelope, loss of which results in sensitivity to toluidine blue [19].

Other interactions of arcA

• Moreover, the expression levels of the FNR regulated genes, yfiD and frdA, were higher in cultures of the arcA mutant strain compared to the wild-type [20].

Analytical, diagnostic and therapeutic context of arcA

• When grown under microaerobic conditions in a bioreactor, the arcA deletion mutant reached a PHB content of 27% +/- 2% [4].

References