Publications by authors named "J Pogliano"
As nucleus-forming phages become better characterized, understanding their unifying similarities and unique differences will help us understand how they occupy varied niches and infect diverse hosts. All identified nucleus-forming phages fall within the Chimalliviridae family and share a core genome of 68 unique genes including chimallin, the major nuclear shell protein. A well-studied but non-essential protein encoded by many nucleus-forming phages is PhuZ, a tubulin homolog which aids in capsid migration, nucleus rotation, and nucleus positioning.
View Article and Find Full Text PDFHachiman is a broad-spectrum antiphage defense system of unknown function. We show here that Hachiman is a heterodimeric nuclease-helicase complex, HamAB. HamA, previously a protein of unknown function, is the effector nuclease.
View Article and Find Full Text PDFAn arylsulfonamide that targets cell wall biosynthesis in .
Antimicrob Agents Chemother
November 2024
Article Synopsis
- - We synthesized a new arylsulfonamide that showed effectiveness against both extracellular and intracellular bacilli, while also displaying selectivity in its action against HepG2 cells.
- - The drug disrupts bacterial cell wall synthesis, likely targeting the MmpL3 protein, which is known to export mycolic acids necessary for the bacterial cell wall.
- - A specific mutation in the MmpL3 protein led to some resistance against the drug, further supporting the idea that MmpL3 is the main target of the compound's action.
Dynamically unstable polymers capture and move cellular cargos in bacteria and eukaryotes, but regulation of their assembly remains poorly understood. Here we describe polymerization of Alp7A, a bacterial actin-like protein (ALP) that distributes copies of plasmid pLS20 among daughter cells in . Purified ATP-Alp7A forms dynamically unstable polymers with a high critical concentration for net assembly (cc = 10.
View Article and Find Full Text PDFArticle Synopsis
- Bacteria and their viruses are in a continuous evolutionary struggle, with bacteria developing systems to defend against viral attacks.
- The study reveals that the bacterial phage anti-restriction-induced system (PARIS) functions as a toxin-antitoxin system, where the antitoxin AriA keeps the toxin AriB inactive until triggered by a specific phage protein, Ocr.
- The research also shows that the structure of AriA allows it to release the active AriB, which then inhibits protein translation and halts cell growth, providing insight into how bacteria detect and respond to phage infections.