Abstract
Holins are bacteriophage membrane proteins responsible for the lysis of the cytosolic membrane in host cells. During the morphogenesis period of the infection cycle, canonical holin accumulates in the cytoplasmic membrane until they suddenly trigger to form lethal lesions known as holes. Canonical holin is also known as S105 protein of phage λ. Canonical holin consists of 105 amino acid sequence with three transmembrane domains spanning the membrane bilayer. The structural topology, dynamics, and oligomerization states of canonical holin are not well understood in its native-like environment. In this study, we have successfully overexpressed several mutants of canonical holin in E. Coli and purified into DDM detergent micelles. Purified proteins were spin-labeled and further reconstituted into POPC/POPG liposomes. Solid-state nuclear magnetic resonance (SSNMR) technique was used to confirm the interaction of canonical holin with phospholipid membrane. We are developing continuous wave electron paramagnetic resonance (CW-EPR) and pulsed EPR techniques to investigate structural topology, dynamics, and oligomerization states of canonical holin in different lipid bilayer membrane environments. This study will open a path to understanding the structural-functional relationship of canonical holin in native-like membrane environments.
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