ArticleBiochemistry2009
Purification and functional characterization of phiX174 lysis protein E.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 37 citations in OpenAlex.
- Functional Activity of the Lysis Protein E From Phage ID52: Dependence on SecB for Efficient Host Cell Lysis.Biotechnology journal · 2026Article
- Temperature-Dependent Recombinase-Based Genetic Circuits.International journal of molecular sciences · 2025Article
- The mechanism of the phage-encoded protein antibiotic from ΦX174.Science (New York, N.Y.) · 2023Article
- VirulentFrontiers in microbiology · 2021Article
- Single-gene lysis in the metagenomic era.Current opinion in microbiology · 2020Review
- Phage single-gene lysis: Finding the weak spot in the bacterial cell wall.The Journal of biological chemistry · 2019Review
- Mutational analysis of the MS2 lysis protein L.Microbiology (Reading, England) · 2017Article
- Bacterial Virus Ontology; Coordinating across Databases.Viruses · 2017Article
- Re-directing bacterial microcompartment systems to enhance recombinant expression of lysis protein E from bacteriophage ϕX174 in Escherichia coli.Microbial cell factories · 2017Article
- Bacteriophage endolysins and their applications.Science progress · 2016Article
- Genetically Determined Variation in Lysis Time Variance in the Bacteriophage φX174.G3 (Bethesda, Md.) · 2016Article
- Cell Walls and the Convergent Evolution of the Viral Envelope.Microbiology and molecular biology reviews : MMBR · 2015Review
- Autotransporter-based antigen display in bacterial ghosts.Applied and environmental microbiology · 2015Article
- Controlled bacterial lysis for electron tomography of native cell membranes.Structure (London, England : 1993) · 2014Article
- Inhibitory mechanism of the Qβ lysis protein A2.Molecular microbiology · 2012Article
- Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174.Molecular microbiology · 2012Article
- A common, non-optimal phenotypic endpoint in experimental adaptations of bacteriophage lysis time.BMC evolutionary biology · 2012Article
- Engineering Escherichia coli BL21(DE3) derivative strains to minimize E. coli protein contamination after purification by immobilized metal affinity chromatography.Applied and environmental microbiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Two classes of bacteriophages, the single-stranded DNA Microviridae and the single-stranded RNA Alloleviviridae, accomplish lysis by expressing "protein antibiotics", or polypeptides that inhibit cell wall biosynthesis. Previously, we have provided genetic and physiological evidence that E, a 91-amino acid membrane protein encoded by the prototype microvirus, varphiX174, is a specific inhibitor of the translocase MraY, an essential membrane-embedded enzyme that catalyzes the formation of the murein precursor, Lipid I, from UDP-N-acetylmuramic acid-pentapeptide and the lipid carrier, undecaprenol phosphate. Here we report the first purification of E, which has been refractory to overexpression because of its lethality to Escherichia coli. Moreover, using a fluorescently labeled analogue of the sugar-nucleotide substrate, we demonstrate that E acts as a noncompetitive inhibitor of detergent-solubilized MraY, with respect to both soluble and lipid substrates. In addition, we show that the E sensitivity of five MraY mutant proteins, produced from alleles selected for resistance to E, can be correlated to the apparent affinities determined by in vivo multicopy suppression experiments. These results are inconsistent with previous reports that E inhibited membrane-embedded MraY but not the detergent-solubilized enzyme, which led to a model in which E functions by binding MraY and blocking the formation of an essential heteromultimeric complex involving MraY and other murein biosynthesis enzymes. We discuss a new model in which E binds to MraY at a site composed of the two transmembrane domains within which the E resistance mutations map and the fact that the result of this binding is a conformational change that inactivates the enzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.