Xenogeneic modulation of the ClpCP protease of Bacillus subtilis by a phage-encoded adaptor-like protein
| Autor: | Mulvenna, N., Hantke, I., Burchell, L., Nicod, S., Bell, D., Turgay, K., Wigneshweraraj, S. |
|---|---|
| Přispěvatelé: | Wellcome Trust |
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
gp53 gene
host cell Dewey Decimal Classification::500 | Naturwissenschaften::570 | Biowissenschaften Biologie heat shock protein Bacillus Bacillus Phages bacterial growth protein gp 53 Bacterial protein antibacterial activity bacteriophage SPO1 gene chaperone Bacteriophages bacteria 11 Medical and Health Sciences Cell proliferation ClpCP proteinase gene product unclassified drug Bacillus Subtilis priority journal Cellular process protein protein interaction proteinase ATP-dependent protease enzyme regulation bacterial gene 03 Chemical Sciences Transcription Cell Division DNA Replication Biochemistry & Molecular Biology bacteriophage DNA Cellular pathway Biosynthesis progeny Microbiology Article Viral Proteins ddc:570 Endopeptidases controlled study xenograft gene identification nonhuman Proteins Bacteriology 06 Biological Sciences Plant shutdowns bacterial DNA DNA Viral Cytotoxic proteins Systematic analysis Phage progeny production adaptor protein |
| Zdroj: | The Journal of Biological Chemistry Journal of Biological Chemistry 294 (2019), Nr. 46 |
| DOI: | 10.15488/10186 |
| Popis: | Like eukaryotic and archaeal viruses, which coopt the host's cellular pathways for their replication, bacteriophages have evolved strategies to alter the metabolism of their bacterial host. SPO1 bacteriophage infection of Bacillus subtilis results in comprehensive remodeling of cellular processes, leading to conversion of the bacterial cell into a factory for phage progeny production. Acluster of 26 genes in the SPO1 genome, called the host takeover module, encodes for potentially cytotoxic proteins that specifically shut down various processes in the bacterial host, including transcription, DNA synthesis, and cell division. However, the properties and bacterial targets of many genes of the SPO1 host takeover module remain elusive. Through a systematic analysis of gene products encoded by the SPO1 host takeover module, here we identified eight gene products that attenuated B. subtilis growth. Of the eight phage gene products that attenuated bacterial growth, a 25-kDa protein called Gp53 was shown to interact with the AAA4 chaperone protein ClpC of the ClpCP protease of B. subtilis. Our results further reveal that Gp53 is a phage-encoded adaptor-like protein that modulates the activity of the ClpCP protease to enable efficient SPO1 phage progeny development. In summary, our findings indicate that the bacterial ClpCP protease is the target of xenogeneic (dys)regulation by a SPO1 phage-derived factor and add Gp53 to the list of antibacterial products that target bacterial protein degradation and therefore may have utility for the development of novel antibacterial agents. © 2019 Mulvenna et al. |
| Databáze: | OpenAIRE |
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