Lyle A. Simmons

This study uses single-molecule tracking to analyze the behavior of three proteins involved in removing RNA-DNA hybrids during lagging-strand replication in Bacillus subtilis, revealing their dynamic interactions with the replisome and nucleoid.

This study identifies 17 rRNA methyltransferases in Bacillus subtilis, revealing their roles in ribosome function and antibiotic sensitivity through genetic and biochemical analyses.

The paper shows that DnaE, not just Pol I, can efficiently repair Okazaki fragments via strand displacement synthesis in B. subtilis.

This study identifies TlyA as an rRNA methyltransferase critical for ribosome assembly in B. subtilis, showing its role in cold sensitivity and antibiotic resistance.

This study compares the efficiency of RNase HII from Bacillus subtilis and Escherichia coli in processing various ribonucleotides, finding B. subtilis is inefficient at repairing damaged rNMPs.

This study identifies bacterial DNA polymerase I as an efficient reverse transcriptase capable of mediating RNA-templated DNA repair synthesis.

This study investigates how DNA replication initiation frequency affects genome stability in Bacillus subtilis, showing that both under-initiation and over-initiation lead to DNA damage sensitivity and replication fork stress.

The paper characterizes MrfB, a DEDDh exonuclease involved in repairing mitomycin C-induced DNA damage in Bacillus subtilis, revealing its structural and biochemical properties.

This study examines the distinct roles of RNase HII and HIII in removing RNA:DNA hybrids and their impact on mutagenesis and DNA replication.

This study identifies two proteases, YlbL and CtpA, that promote DNA damage checkpoint recovery in Bacillus subtilis by cleaving YneA, a checkpoint protein.