The T4 Bacteriophage Protein MOTB Remodels Host DNA

Abstract

In previous studies, we showed that the T4 bacteriophage MotB protein is a DNA binding protein that co-purifies with H-NS and its paralog, StpA. in bacteria, histone-like proteins such as H-NS and StpA, regulate genome-wide transcription by preferentially binding AT-rich DNA regions. Consequently, H-NS may offer some protection from phage infections by binding to phage DNA, which typically have a higher AT-content then their host. in this study, we visualized the interactions of MotB with DNA in the presence and absence of H-NS using atomic force microscopy (AFM).