Article
The crystal structure of bacteriophage λ RexA provides novel insights into the DNA binding properties of Rex-like phage exclusion proteins.
Nucleic acids research - 8 May 2024
Adams Myfanwy C, Schiltz Carl J, Sun Jing, Hosford Christopher J, Johnson Virginia M, Pan Hao, Borbat Peter P, Freed Jack H, Thomason Lynn C, Court Carolyn, Court Donald L, Chappie Joshua S
Abstract excerpt
RexA and RexB function as an exclusion system that prevents bacteriophage T4rII mutants from growing on Escherichia coli λ phage lysogens. Recent data established that RexA is a non-specific DNA binding protein that can act independently of RexB to bias the λ bistable switch toward the lytic state, preventing conversion back to lysogeny. The molecular interactions underlying these activities are unknown, owing in...
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