Page 57 - Read Online

Page 16 of 17 Mezhyrova et al. Microbiome Res Rep 2023;2:28 https://dx.doi.org/10.20517/mrr.2023.28

Ethical approval and consent to participate
Not applicable.

Consent for publication
Not applicable.

Copyright
© The Author(s) 2023.

REFERENCES
1. Walderich B, Ursinus-Wössner A, van Duin J, Höltje JV. Induction of the autolytic system of Escherichia coli by specific insertion of
bacteriophage MS2 lysis protein into the bacterial cell envelope. J Bacteriol 1988;170:5027-33. DOI PubMed PMC
2. Witte A, Reisinger GR, Säckl W, Wanner G, Lubitz W. Characterization of Escherichia coli lysis using a family of chimeric E-L
genes. FEMS Microbiol Lett 1998;164:159-67. DOI PubMed
3. Berkhout B, de Smit MH, Spanjaard RA, Blom T, van Duin J. The amino terminal half of the MS2-coded lysis protein is dispensable
for function: implications for our understanding of coding region overlaps. EMBO J 1985;4:3315-20. DOI PubMed PMC
4. Chamakura KR, Tran JS, Young R. MS2 lysis of escherichia coli depends on host chaperone DnaJ. J Bacteriol 2017;199:e00058-17.
DOI PubMed PMC
5. Walderich B, Höltje JV. Specific localization of the lysis protein of bacteriophage MS2 in membrane adhesion sites of Escherichia
coli. J Bacteriol 1989;171:3331-6. DOI PubMed PMC
6. Goessens WH, Driessen AJ, Wilschut J, van Duin J. A synthetic peptide corresponding to the C-terminal 25 residues of phage MS2
coded lysis protein dissipates the protonmotive force in Escherichia coli membrane vesicles by generating hydrophilic pores. EMBO J
1988;7:867-73. DOI PubMed PMC
7. Chamakura K, Young R. Phage single-gene lysis: Finding the weak spot in the bacterial cell wall. J Biol Chem 2019;294:3350-8. DOI
PubMed PMC
8. Bernhardt TG, Wang IN, Struck DK, Young R. Breaking free: “protein antibiotics” and phage lysis. Res Microbiol 2002;153:493-501.
DOI PubMed
9. Chamakura KR, Young R. Single-gene lysis in the metagenomic era. Curr Opin Microbiol 2020;56:109-17. DOI PubMed PMC
10. Langemann T, Koller VJ, Muhammad A, Kudela P, Mayr UB, Lubitz W. The Bacterial Ghost platform system: production and
applications. Bioeng Bugs 2010;1:326-36. DOI PubMed PMC
11. Fu X, Himes BA, Ke D, Rice WJ, Ning J, Zhang P. Controlled bacterial lysis for electron tomography of native cell membranes.
Structure 2014;22:1875-82. DOI PubMed PMC
12. Bernhardt TG, Roof WD, Young R. Genetic evidence that the bacteriophage ϕ X174 lysis protein inhibits cell wall synthesis. Proc
Natl Acad Sci U S A 2000;97:4297-302. DOI PubMed PMC
13. Bernhardt TG, Roof WD, Young R. The Escherichia coli FKBP-type PPIase SlyD is required for the stabilization of the E lysis protein
of bacteriophage φX174. Mol Microbiol 2002;45:99-108. DOI PubMed
14. Mendel S, Holbourn JM, Schouten JA, Bugg TDH. Interaction of the transmembrane domain of lysis protein E from bacteriophage ϕ
X174 with bacterial translocase MraY and peptidyl-prolyl isomerase SlyD. Microbiology 2006;152:2959-67. DOI PubMed
15. Tanaka S, Clemons WM Jr. Minimal requirements for inhibition of MraY by lysis protein E from bacteriophage ΦX174. Mol
Microbiol 2012;85:975-85. DOI PubMed PMC
16. Rodolis MT, Mihalyi A, O’Reilly A, et al. Identification of a novel inhibition site in translocase MraY based upon the site of
interaction with lysis protein E from bacteriophage ϕX174. Chembiochem 2014;15:1300-8. DOI PubMed
17. Mezhyrova J, Martin J, Peetz O, et al. Membrane insertion mechanism and molecular assembly of the bacteriophage lysis toxin Φ
X174-E. FEBS J 2021;288:3300-16. DOI
18. Haberstock S, Roos C, Hoevels Y, et al. A systematic approach to increase the efficiency of membrane protein production in cell-free
expression systems. Protein Expr Purif 2012;82:308-16. DOI
19. Schwarz D, Junge F, Durst F, et al. Preparative scale expression of membrane proteins in Escherichia coli-based continuous exchange
cell-free systems. Nat Protoc 2007;2:2945-57. DOI
20. Baba T, Ara T, Hasegawa M, et al. Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection.
Mol Syst Biol 2006;2:2006.0008. DOI PubMed PMC
21. Roos C, Kai L, Haberstock S, et al. High-level cell-free production of membrane proteins with nanodiscs. In: Alexandrov K, Johnston
WA, editors. Cell-Free Protein Synthesis. Totowa: Humana Press; 2014. p. 109-30. DOI
22. Rues R, Henrich E, Boland C, Caffrey M, Bernhard F. Cell-free production of membrane proteins in escherichia coli lysates for
functional and structural studies. In: Mus-veteau I, editor. Heterologous Expression of Membrane Proteins. New York: Springer; 2016.
p. 1-21. DOI
23. Denisov IG, Grinkova YV, Lazarides AA, Sligar SG. Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with
controlled size. J Am Chem Soc 2004;126:3477-87. DOI