Disease relevance of asr

• Molecular characterization of the acid-inducible asr gene of Escherichia coli and its role in acid stress response [1].

High impact information on asr

• Deletion of amino acids encompassing the processing site required for release of the 8-kDa protein resulted in an acid-sensitive phenotype similar to that observed for the asr null mutant, suggesting that the 8-kDa product plays an important role in the adaptation to acid shock [1].
• Transcription of the chromosomal asr was abolished in the presence of a phoB-phoR (a two-component regulatory system, controlling the pho regulon inducible by phosphate starvation) deletion mutant [2].
• Analysis of the asr DNA sequence revealed an open reading frame coding for a 111-amino-acid polypeptide with a deduced molecular mass of approximately 11.6 kDa [2].
• The acid-inducible asr gene in Escherichia coli: transcriptional control by the phoBR operon [2].
• Primer extension analysis of the asr transcript revealed a region similar to the Pho box (the consensus sequence found in promoters transcriptionally activated by the PhoB protein) upstream from the determined transcription start [2].

Biological context of asr

• The acid-inducible RNA was purified, and the gene encoding it, designated asr (for acid shock RNA), mapped at 35.98 min on the E. coli chromosome [2].
• However, asr expression by the fusion plasmid was not affected by site-specific mutations within the apparent FNR-binding site [3].

Analytical, diagnostic and therapeutic context of asr

• Sequence alignment of the asr promoters from different enterobacterial species identified a highly conserved region located at position -70 to -30 relative to the asr transcriptional start site [4].

References