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Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation
Lytic viruses of bacteria (bacteriophages, phages) are intracellular parasites that take over hosts’ biosynthetic processes for their propagation. Most of the knowledge on the host hijacking mechanisms has come from the studies of the lytic phage T4, which infects Escherichia coli. The integrity of...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9409239/ https://www.ncbi.nlm.nih.gov/pubmed/36012768 http://dx.doi.org/10.3390/ijms23169483 |
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author | Juškauskas, Augustinas Zajančkauskaitė, Aurelija Meškys, Rolandas Ger, Marija Kaupinis, Algirdas Valius, Mindaugas Truncaitė, Lidija |
author_facet | Juškauskas, Augustinas Zajančkauskaitė, Aurelija Meškys, Rolandas Ger, Marija Kaupinis, Algirdas Valius, Mindaugas Truncaitė, Lidija |
author_sort | Juškauskas, Augustinas |
collection | PubMed |
description | Lytic viruses of bacteria (bacteriophages, phages) are intracellular parasites that take over hosts’ biosynthetic processes for their propagation. Most of the knowledge on the host hijacking mechanisms has come from the studies of the lytic phage T4, which infects Escherichia coli. The integrity of T4 development is achieved by strict control over the host and phage processes and by adjusting them to the changing infection conditions. In this study, using in vitro and in vivo biochemical methods, we detected the direct interaction between the T4 protein RIII and ribosomal protein S1 of the host. Protein RIII is known as a cytoplasmic antiholin, which plays a role in the lysis inhibition function of T4. However, our results show that RIII also acts as a viral effector protein mainly targeting S1 RNA-binding domains that are central for all the activities of this multifunctional protein. We confirm that the S1–RIII interaction prevents the S1-dependent activation of endoribonuclease RegB. In addition, we propose that by modulating the multiple processes mediated by S1, RIII could act as a regulator of all stages of T4 infection including the lysis inhibition state. |
format | Online Article Text |
id | pubmed-9409239 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-94092392022-08-26 Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation Juškauskas, Augustinas Zajančkauskaitė, Aurelija Meškys, Rolandas Ger, Marija Kaupinis, Algirdas Valius, Mindaugas Truncaitė, Lidija Int J Mol Sci Article Lytic viruses of bacteria (bacteriophages, phages) are intracellular parasites that take over hosts’ biosynthetic processes for their propagation. Most of the knowledge on the host hijacking mechanisms has come from the studies of the lytic phage T4, which infects Escherichia coli. The integrity of T4 development is achieved by strict control over the host and phage processes and by adjusting them to the changing infection conditions. In this study, using in vitro and in vivo biochemical methods, we detected the direct interaction between the T4 protein RIII and ribosomal protein S1 of the host. Protein RIII is known as a cytoplasmic antiholin, which plays a role in the lysis inhibition function of T4. However, our results show that RIII also acts as a viral effector protein mainly targeting S1 RNA-binding domains that are central for all the activities of this multifunctional protein. We confirm that the S1–RIII interaction prevents the S1-dependent activation of endoribonuclease RegB. In addition, we propose that by modulating the multiple processes mediated by S1, RIII could act as a regulator of all stages of T4 infection including the lysis inhibition state. MDPI 2022-08-22 /pmc/articles/PMC9409239/ /pubmed/36012768 http://dx.doi.org/10.3390/ijms23169483 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Juškauskas, Augustinas Zajančkauskaitė, Aurelija Meškys, Rolandas Ger, Marija Kaupinis, Algirdas Valius, Mindaugas Truncaitė, Lidija Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation |
title | Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation |
title_full | Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation |
title_fullStr | Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation |
title_full_unstemmed | Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation |
title_short | Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation |
title_sort | interaction between phage t4 protein riii and host ribosomal protein s1 inhibits endoribonuclease regb activation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9409239/ https://www.ncbi.nlm.nih.gov/pubmed/36012768 http://dx.doi.org/10.3390/ijms23169483 |
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