Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/133154
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Type: | Journal article |
Title: | Instability of CII is needed for efficient switching between lytic and lysogenic development in bacteriophage 186 |
Author: | Murchland, I.M. Ahlgren-Berg, N. Pietsch, J.M.J. Isabel, A. Dodd, I.B. Shearwin, K.E. |
Citation: | Nucleic Acids Research, 2020; 48(21):1-12 |
Publisher: | Oxford University Press |
Issue Date: | 2020 |
ISSN: | 0305-1048 1362-4962 |
Statement of Responsibility: | Iain M Murchland, Alexandra Ahlgren-Berg, Julian M J Pietsch, Alejandra Isabel, Ian B Dodd, Keith E Shearwin |
Abstract: | The CII protein of temperate coliphage 186, like the unrelated CII protein of phage λ, is a transcriptional activator that primes expression of the CI immunity repressor and is critical for efficient establishment of lysogeny. 186-CII is also highly unstable, and we show that in vivo degradation is mediated by both FtsH and RseP. We investigated the role of CII instability by constructing a 186 phage encoding a protease resistant CII. The stabilised-CII phage was defective in the lysis-lysogeny decision: choosing lysogeny with close to 100% frequency after infection, and forming prophages that were defective in entering lytic development after UV treatment. While lysogenic CI concentration was unaffected by CII stabilisation, lysogenic transcription and CI expression was elevated after UV. A stochastic model of the 186 network after infection indicated that an unstable CII allowed a rapid increase in CI expression without a large overshoot of the lysogenic level, suggesting that instability enables a decisive commitment to lysogeny with a rapid attainment of sensitivity to prophage induction. |
Keywords: | Escherichia coli Coliphages Prophages ATP-Dependent Proteases Endopeptidases Escherichia coli Proteins Membrane Proteins Viral Proteins Models, Statistical Stochastic Processes Ultraviolet Rays Lysogeny Transcriptional Activation Protein Stability Proteolysis |
Rights: | © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
DOI: | 10.1093/nar/gkaa1065 |
Grant ID: | http://purl.org/au-research/grants/arc/DP150103009 http://purl.org/au-research/grants/arc/DP160101450 |
Published version: | http://dx.doi.org/10.1093/nar/gkaa1065 |
Appears in Collections: | Biochemistry publications |
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hdl_133154.pdf | Published version | 1.08 MB | Adobe PDF | View/Open |
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