Disease relevance of lysA

• Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli. II. Nucleotide sequence of the lysA gene and its regulatory region [1].
• Within the Bacillus subtilis genome sequencing project, the region between lysA and ilvA was assigned to our laboratory [2].
• A lipopeptide-encoding sequence upstream from the lysA gene of Pseudomonas aeruginosa [3].
• Nucleotide sequence of the lysA gene of Corynebacterium glutamicum and possible mechanisms for modulation of its expression [4].

High impact information on lysA

• An open reading frame (ORF) of 141 bp was observed upstream from the Pseudomonas aeruginosa lysA gene [3].
• The same binding site (73 base-pairs fragment) could be involved in both effects of the LysR product, acting simultaneously as an operator for lysR expression and an initiator for lysA expression [5].
• At the 3' end of the lysA gene an open reading frame was revealed in the opposite direction and was identified as the galR coding region [1].
• The complete nucleotide sequence of the lysA gene and its regulatory region was determined [1].
• A target of the LysR activator protein was localized on a 73 base-pair fragment found 48 base-pairs upstream from the lysA coding region [1].

Chemical compound and disease context of lysA

• The lysA gene of Escherichia coli encodes for a diaminopimelic acid decarboxylase (EC 4.1.1.20) which allows the conversion of diaminopimelic acid into lysine in bacteria [6].

Biological context of lysA

• The presence of this DNA sequence on a multicopy plasmid led to a net decrease of lysA expression, indicating limiting amounts of active LysR protein in the cytoplasm [1].
• Translational gene fusions constructed in vitro with the beta-galactosidase gene were used to identify the lysA initiating ATG [1].
• For example, the removal of lysA and ruvA from ancestral operons that contained essential genes allowed their expression to respond to lysine levels and DNA damage, respectively [7].
• In the intact cell the rate of lysine synthesis is limited by the uptake of DAP which is taken up at only 5% of the rate of lysine. lysA has a potential as a reporter gene in studies of gene expression in mammalian cells [8].

Analytical, diagnostic and therapeutic context of lysA

• Sequence analysis localized the lysA gene of Corynebacterium glutamicum strain AS019 within a 1.35 kb open reading frame, potentially encoding a 445 amino acid product [4].

References