A dimeric holin/antiholin complex controls lysis by phage T4.

ABSTRACT: Lytic phages control the timepoint of host cell lysis by timing the holin-mediated release of cell wall-degrading endolysins. In phage T4, the antiholin RI inhibits the holin T, thereby preventing the early release of the T4 endolysin and lysis. The antiholin achieves lysis inhibition (LIN) in response to phage superinfections, thereby increasing the chance for lysis in an environment with a lower phage concentration. The holin T consists of a small N-terminal cytoplasmic domain, a transmembrane helix, and a periplasmic C-terminal domain. The antiholin is targeted to the periplasm by a cleavable signal peptide. Recently, the periplasmic soluble domains of the holin and the antiholin were found to form T₂/RI₂ tetramers in crystals. To investigate the functional relevan

SUBMITTER: Schwarzkopf JMF 

PROVIDER: S-EPMC11413866 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature