Regulation of the ordinal DNA translocation cycle in bacteriophage Φ29 through trans-subunit interactions.

ABSTRACT: Certain viruses such as tailed bacteriophages and herpes simplex virus package double-stranded DNA into empty procapsids via powerful, ring-shaped molecular motors. High-resolution structures and force measurements on the DNA packaging motor of bacteriophage Φ29 revealed that its five ATPase subunits coordinate ATP hydrolysis with each other to maintain the proper cyclic sequence of DNA translocation steps about the ring. Here, we explore how the Φ29 motor regulates translocation by timing key events, namely ATP binding/hydrolysis and DNA gripping, through trans-subunit interactions. We used subunit dimers bound to DNA as our model system, a minimal system that still captures the conformation and trans-subunit interactions of the full pentameric motor complex. Molecular dynamics simulation

SUBMITTER: Dargis R 

PROVIDER: S-EPMC12260519 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature