Back to Search
Start Over
Interaction between Phage T4 Protein RIII and Host Ribosomal Protein S1 Inhibits Endoribonuclease RegB Activation
- Source :
- International Journal of Molecular Sciences; Volume 23; Issue 16; Pages: 9483, International journal of molecular sciences, Basel : MDPI, 2022, vol. 23, iss. 16, art. no. 9483, p. [1-18]
- Publication Year :
- 2022
- Publisher :
- MDPI AG, 2022.
-
Abstract
- 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.
- Subjects :
- Ribosomal Proteins
Organic Chemistry
E. coli ribosomal protein S1
bacteriophage T4
RIII protein
RNase RegB
lysis inhibition
General Medicine
Catalysis
Computer Science Applications
Inorganic Chemistry
Viral Proteins
Endoribonucleases
Escherichia coli
Bacteriophage T4
Physical and Theoretical Chemistry
Molecular Biology
Spectroscopy
Subjects
Details
- ISSN :
- 14220067
- Volume :
- 23
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences
- Accession number :
- edsair.doi.dedup.....d70bfd929ec00adeb633e6876f442ad3
- Full Text :
- https://doi.org/10.3390/ijms23169483