期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 16, 页码 -出版社
MDPI
DOI: 10.3390/ijms23169483
关键词
E; coli ribosomal protein S1; bacteriophage T4; RIII protein; RNase RegB; lysis inhibition
资金
- Research Council of Lithuania [MIP-002/2014]
The study reveals the direct interaction between the T4 protein RIII and ribosomal protein S1 of the host, demonstrating the important regulatory role of RIII in modulating all stages of T4 infection by targeting the S1 RNA-binding domains.
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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