Abstract
DNA replication forks often encounter template DNA lesions that can stall their progression. The PriA-dependent pathway is the major replication restart mechanism in Gram-positive bacteria, and it requires several primosome proteins. Among them, PriA protein—a 30 to 50 superfamily-2 DNA helicase—is the key factor in recognizing DNA lesions and it also recruits other proteins. Here, we investigated the ATPase and helicase activities ofStreptococcus pneumoniae PriA (SpPriA) through biochemical and kinetic analyses.
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