ArticleProtein science : a publication of the Protein Society2012
Protein determinants of phage T4 lysis inhibition.
Article in Protein science : a publication of the Protein Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 41 citations in OpenAlex.
- Optical Density-Based Methods in Phage Biology: Titering, Lysis Timing, Host Range, and Phage-Resistance Evolution.Viruses · 2025Review
- Genetic insights into novel lysis suppression by phage CSP1 in Escherichia coli.Journal of microbiology (Seoul, Korea) · 2025Article
- Bacteriophage titering by optical density means: KOTE assays.Open life sciences · 2025Review
- The short cytoplasmic region of phage T4 holin is essential for the transition from impermeable membrane protein complexes to permeable pores.Frontiers in microbiology · 2025Article
- A dimeric holin/antiholin complex controls lysis by phage T4.Frontiers in microbiology · 2024Article
- Automating Predictive Phage Therapy Pharmacology.Antibiotics (Basel, Switzerland) · 2023Review
- Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation.International journal of molecular sciences · 2022Article
- In Silico Predictions of Ecological Plasticity Mediated by Protein Family Expansions in Early-Diverging Fungi.Journal of fungi (Basel, Switzerland) · 2022Article
- The Phage T4 Antiholin RI Has a Cleavable Signal Peptide, Not a SAR Domain.Frontiers in microbiology · 2021Article
- Structure and Function of the T4 Spackle Protein Gp61.3.Viruses · 2020Article
- The Structural Basis of T4 Phage Lysis Control: DNA as the Signal for Lysis Inhibition.Journal of molecular biology · 2020Article
- DominanteLife · 2020Article
- Look Who's Talking: T-Even Phage Lysis Inhibition, the Granddaddy of Virus-Virus Intercellular Communication Research.Viruses · 2019Review
- Understanding and Exploiting Phage-Host Interactions.Viruses · 2019Review
- Commentary: A Host-Produced Quorum-Sensing Autoinducer Controls a Phage Lysis-Lysogeny Decision.Frontiers in microbiology · 2019Article
- Phage-Antibiotic Synergy via Delayed Lysis.Applied and environmental microbiology · 2018Article
- Mutational analysis of the MS2 lysis protein L.Microbiology (Reading, England) · 2017Article
- MS2 Lysis of Escherichia coli Depends on Host Chaperone DnaJ.Journal of bacteriology · 2017Article
- Energetic cost of building a virus.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- The temperate Burkholderia phage AP3 of the Peduovirinae shows efficient antimicrobial activity against B. cenocepacia of the IIIA lineage.Applied microbiology and biotechnology · 2017Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Genetic studies have established that lysis inhibition in bacteriophage T4 infections occurs when the RI antiholin inhibits the lethal hole-forming function of the T holin. The T-holin is composed of a single N-terminal transmembrane domain and a ~20 kDa periplasmic domain. It accumulates harmlessly throughout the bacteriophage infection cycle until suddenly causing permeabilization of the inner membrane, thereby initiating lysis. The RI antiholin has a SAR domain that directs its secretion to the periplasm, where it can either be inactivated and degraded or be activated as a specific inhibitor of T. Previously, it was shown that the interaction of the soluble domains of these two proteins within the periplasm was necessary for lysis inhibition. We have purified and characterized the periplasmic domains of both T and RI. Both proteins were purified in a modified host that allows disulfide bond formation in the cytoplasm, due to the functional requirement of conserved disulfide bonds. Analytical centrifugation and circular dichroism spectroscopy showed that RI was monomeric and exhibited ~80% alpha-helical content. In contrast, T exhibited a propensity to oligomerize and precipitate at high concentrations. Incubation of RI with T inhibits this aggregation and results in a complex of equimolar T and RI content. Although gel filtration analysis indicated a complex mass of 45 kDa, intermediate between the predicted 30 kDa heterodimer and 60 kDa heterotetramer, sedimentation velocity analysis indicated that the predominant species is the former. These results suggest that RI binding to T is necessary and sufficient for lysis inhibition.
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