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Article

Functional Dissection of P1 Bacteriophage Holin-like Proteins Reveals the Biological Sense of P1 Lytic System Complexity

1
Institute of Biochemistry and Biophysics of the Polish Academy of Sciences, 02-106 Warsaw, Poland
2
Autonomous Department of Microbiology, Faculty of Agriculture and Biology, Warsaw University of Life Sciences, SGGW, 02-776 Warsaw, Poland
*
Author to whom correspondence should be addressed.
Academic Editor: Alicja Wegrzyn
Int. J. Mol. Sci. 2022, 23(8), 4231; https://doi.org/10.3390/ijms23084231
Received: 12 December 2021 / Revised: 1 April 2022 / Accepted: 7 April 2022 / Published: 11 April 2022
(This article belongs to the Special Issue Bacteriophage—Molecular Studies 3.0)
P1 is a model temperate myovirus. It infects different Enterobacteriaceae and can develop lytically or form lysogens. Only some P1 adaptation strategies to propagate in different hosts are known. An atypical feature of P1 is the number and organization of cell lysis-associated genes. In addition to SAR-endolysin Lyz, holin LydA, and antiholin LydB, P1 encodes other predicted holins, LydC and LydD. LydD is encoded by the same operon as Lyz, LydA and LydB are encoded by an unlinked operon, and LydC is encoded by an operon preceding the lydA gene. By analyzing the phenotypes of P1 mutants in known or predicted holin genes, we show that all the products of these genes cooperate with the P1 SAR-endolysin in cell lysis and that LydD is a pinholin. The contributions of holins/pinholins to cell lysis by P1 appear to vary depending on the host of P1 and the bacterial growth conditions. The pattern of morphological transitions characteristic of SAR-endolysin–pinholin action dominates during lysis by wild-type P1, but in the case of lydC lydD mutant it changes to that characteristic of classical endolysin-pinholin action. We postulate that the complex lytic system facilitates P1 adaptation to various hosts and their growth conditions. View Full-Text
Keywords: bacteriophage P1; bacterial cell lysis; holin; pinholin; endolysin; SAR-endolysin; Escherichia coli; Enterobacter cloacae bacteriophage P1; bacterial cell lysis; holin; pinholin; endolysin; SAR-endolysin; Escherichia coli; Enterobacter cloacae
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MDPI and ACS Style

Bednarek, A.; Cena, A.; Izak, W.; Bigos, J.; Łobocka, M. Functional Dissection of P1 Bacteriophage Holin-like Proteins Reveals the Biological Sense of P1 Lytic System Complexity. Int. J. Mol. Sci. 2022, 23, 4231. https://doi.org/10.3390/ijms23084231

AMA Style

Bednarek A, Cena A, Izak W, Bigos J, Łobocka M. Functional Dissection of P1 Bacteriophage Holin-like Proteins Reveals the Biological Sense of P1 Lytic System Complexity. International Journal of Molecular Sciences. 2022; 23(8):4231. https://doi.org/10.3390/ijms23084231

Chicago/Turabian Style

Bednarek, Agnieszka, Agata Cena, Wioleta Izak, Joanna Bigos, and Małgorzata Łobocka. 2022. "Functional Dissection of P1 Bacteriophage Holin-like Proteins Reveals the Biological Sense of P1 Lytic System Complexity" International Journal of Molecular Sciences 23, no. 8: 4231. https://doi.org/10.3390/ijms23084231

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