Effect of arsA, arsenite-specific ATPase, on inhibition of cell division in Escherichia coli

Escherichia coli, which harbored the ars operon from a plasmid pMH12 of Klebsiella oxytoca D12, showed filamentation due to the expression of ars genes in the presence of arsenite. The continued DNA replication in the absence of cell division was revealed, since nucleoids bound with DAPI appeared to be arranged in chains. In contrast to overexpression of arsA, its frame-shift mutant and knock-out mutant lost filamentation in the presence of arsenite, which suggested that ars-induced division block was dependent on expression of arsA. ArsA-induced division inhibition was not a consequence of an inhibition of DNA replication, and the inability of arsenite to induce an SOS response indicated that arsA-mediated division inhibition was dependent on the expression of the gene product encoded by the minB operon. ArsA is a peripheral membrane protein with an ATP-binding domain, which is homologous to MinD that requires ATP-dependent efflux. These results suggested that ArsA could possibly recruit MinC to the membrane and modulate cytoplasmic FtsZ to block assembly at the middle of the cell.