A quick new way to screen virus proteins for antibiotic properties BerkeleyLab nchembio
and confirmed that Sgllethality can be rescued by expression of heterologous lipid II flippase MurJ, strongly suggesting it to be a target of Sglis not an L-like Sgl. Overall, the Dub-seq genetic screen successfully uncovered high-confidence multicopy suppressors that play a role in PG biosynthesis or are known to alleviate OM stress response and provide insights into Sgl target/repair pathways at a genome-wide scale that may be challenging to obtain via traditional approaches.
Recently, the number of experimentally validated Sgls has expanded by 35, and they share no detectable similarity to the previously characterized Sgls. The high sequence diversity of Sgls naturally implies possible diversity in molecular targets to affect host cell lysis. However, we speculate that evolution of Sgls is highly constrained as being part of compact ssRNA phage genomes, in addition to being commonly found as overlapped or encoded within other phage genes.
. We demonstrate here that repurposing Dub-seq technology for carrying out high-throughput suppressor screens will greatly expedite hypothesis generation and target identification of Sgl lysis proteins, providing a new avenue for antibiotic and phage-derived biotechnological discovery.strains were grown at 37 °C and 180 r.p.m. in Lysogeny Broth supplemented with antibiotics, unless stated otherwise. When appropriate, 50 µg mlchloramphenicol were added to media.
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