Journal
VIRUSES-BASEL
Volume 12, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/v12090976
Keywords
phage-induced acetylation; host transcriptional shutdown; phage-host interactions
Categories
Funding
- Russian Foundation for Basic Research [12-04-31069, 12-04-01600]
- Fonds voorWetenschappelijk Onderzoek Vlaanderen [G.0323.09, 100042]
- National Institutes of Health [NCRR 1S10RR15859, NCRR 1S10RR021056]
- Research Foundation-Flanders [12V5219N]
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In this study, we describe the biological function of the phage-encoded protein RNA polymerase alpha subunit cleavage protein (Rac), a predicted Gcn5-related acetyltransferase encoded by phiKMV-like viruses. These phages encode a single-subunit RNA polymerase for transcription of their late (structure- and lysis-associated) genes, whereas the bacterial RNA polymerase is used at the earlier stages of infection. Rac mediates the inactivation of bacterial transcription by introducing a specific cleavage in the alpha subunit of the bacterial RNA polymerase. This cleavage occurs within the flexible linker sequence and disconnects the C-terminal domain, required for transcription initiation from most highly active cellular promoters. To achieve this, Rac likely taps into a novel post-translational modification (PTM) mechanism within the hostPseudomonas aeruginosa. From an evolutionary perspective, this novel phage-encoded regulation mechanism confirms the importance of PTMs in the prokaryotic metabolism and represents a new way by which phages can hijack the bacterial host metabolism.
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