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- W3096748979 endingPage "11736" @default.
- W3096748979 startingPage "11721" @default.
- W3096748979 abstract "Abstract The genome packaging motor of tailed bacteriophages and herpesviruses is a powerful nanomachine built by several copies of a large (TerL) and a small (TerS) terminase subunit. The motor assembles transiently at the portal vertex of an empty precursor capsid (or procapsid) to power genome encapsidation. Terminase subunits have been studied in-depth, especially in classical bacteriophages that infect Escherichia coli or Salmonella, yet, less is known about the packaging motor of Pseudomonas-phages that have increasing biomedical relevance. Here, we investigated the small terminase subunit from three Podoviridae phages that infect Pseudomonas aeruginosa. We found TerS is polymorphic in solution but assembles into a nonamer in its high-affinity heparin-binding conformation. The atomic structure of Pseudomonas phage PaP3 TerS, the first complete structure for a TerS from a cos phage, reveals nine helix-turn-helix (HTH) motifs asymmetrically arranged around a β-stranded channel, too narrow to accommodate DNA. PaP3 TerS binds DNA in a sequence-specific manner in vitro. X-ray scattering and molecular modeling suggest TerS adopts an open conformation in solution, characterized by dynamic HTHs that move around an oligomerization core, generating discrete binding crevices for DNA. We propose a model for sequence-specific recognition of packaging initiation sites by lateral interdigitation of DNA." @default.
- W3096748979 created "2020-11-09" @default.
- W3096748979 creator A5012832733 @default.
- W3096748979 creator A5040815738 @default.
- W3096748979 creator A5042025565 @default.
- W3096748979 creator A5045072018 @default.
- W3096748979 creator A5046791846 @default.
- W3096748979 creator A5060263997 @default.
- W3096748979 creator A5063710793 @default.
- W3096748979 date "2020-10-30" @default.
- W3096748979 modified "2023-10-16" @default.
- W3096748979 title "Biophysical analysis of<i>Pseudomonas</i>-phage PaP3 small terminase suggests a mechanism for sequence-specific DNA-binding by lateral interdigitation" @default.
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