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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...

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Autores principales: Juškauskas, Augustinas, Zajančkauskaitė, Aurelija, Meškys, Rolandas, Ger, Marija, Kaupinis, Algirdas, Valius, Mindaugas, Truncaitė, Lidija
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
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.
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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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