Topological examination of the bacteriophage lambda S holin by EPR spectroscopy.

ABSTRACT: The S protein from bacteriophage lambda is a three-helix transmembrane protein produced by the prophage which accumulates in the host membrane during late gene expression. It is responsible for the first step in lysing the host cell at the end of the viral life cycle by multimerizing together to form large pores which permeabilize the host membrane to allow the escape of virions. Several previous studies have established a model for the assembly of holin into functional holes and the manner in which they pack together, but it is still not fully understood how the very rapid transition from monomer or dimer to multimeric pore occurs with such precise timing once the requisite threshold is reached. Here, site-directed spin labeling with a nitroxide label at introduced cysteine residues is us

SUBMITTER: Morris AK 

PROVIDER: S-EPMC9771973 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature