Lyle A. Simmons

The DnaAcos allele of Escherichia coli: hyperactive initiation is caused by substitution of A184V and Y271H, resulting in defective ATP binding and aberrant DNA replication control.

DnaA Protein of Escherichia coli: oligomerization at the E. coli chromosomal origin is required for initiation and involves specific N-terminal amino acids.

Hyperinitiation of DNA replication in Escherichia coli leads to replication fork collapse and inviability.

An essential tryptophan of Escherichia coli DnaA protein functions in oligomerization at the E. coli replication origin.

Y-family DNA polymerases respond to DNA damage-independent inhibition of replication fork progression.

Replication is required for the RecA localization response to DNA damage in Bacillus subtilis.

Multiple Ku orthologues mediate DNA non-homologous end-joining in the free-living form and during chronic infection of Sinorhizobium meliloti.

Beta clamp directs localization of mismatch repair in Bacillus subtilis.

Clp and Lon proteases occupy distinct subcellular positions in Bacillus subtilis.

Comparison of responses to double-strand breaks between Escherichia coli and Bacillus subtilis reveals different requirements for SOS induction.

Sinorhizobium meliloti CpdR1 is critical for co-ordinating cell cycle progression and the symbiotic chronic infection.

Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia coli.

Mutations in the Bacillus subtilis beta clamp that separate its roles in DNA replication from mismatch repair.

Structure of the endonuclease domain of MutL: unlicensed to cut.

Role of Escherichia coli YbeY, a highly conserved protein, in rRNA processing.

DNA damage and reactive nitrogen species are barriers to Vibrio cholerae colonization of the infant mouse intestine.

Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork.