Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria
AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2018
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| In: |
Proceedings of the National Academy of Sciences of the United States of America
Year: 2017, Jahrgang: 115, Heft: 2, Pages: E273-E282 |
| ISSN: | 1091-6490 |
| DOI: | 10.1073/pnas.1712051115 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.1073/pnas.1712051115 Verlag: https://www.pnas.org/content/115/2/E273 
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| Verfasserangaben: | Changhan Lee, Kamila B. Franke, Shady Mansour Kamal, Hyunhee Kim, Heinrich Lünsdorf, Jasmin Jäger, Manfred Nimtz, Janja Trček, Lothar Jänsch, Bernd Bukau, Axel Mogk, and Ute Römling |
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| 245 | 1 | 0 | |a Stand-alone ClpG disaggregase confers superior heat tolerance to bacteria |c Changhan Lee, Kamila B. Franke, Shady Mansour Kamal, Hyunhee Kim, Heinrich Lünsdorf, Jasmin Jäger, Manfred Nimtz, Janja Trček, Lothar Jänsch, Bernd Bukau, Axel Mogk, and Ute Römling |
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| 520 | |a AAA+ disaggregases solubilize aggregated proteins and confer heat tolerance to cells. Their disaggregation activities crucially depend on partner proteins, which target the AAA+ disaggregases to protein aggregates while concurrently stimulating their ATPase activities. Here, we report on two potent ClpG disaggregase homologs acquired through horizontal gene transfer by the species Pseudomonas aeruginosa and subsequently abundant P. aeruginosa clone C. ClpG exhibits high, stand-alone disaggregation potential without involving any partner cooperation. Specific molecular features, including high basal ATPase activity, a unique aggregate binding domain, and almost exclusive expression in stationary phase distinguish ClpG from other AAA+ disaggregases. Consequently, ClpG largely contributes to heat tolerance of P. aeruginosa primarily in stationary phase and boosts heat resistance 100-fold when expressed in Escherichia coli. This qualifies ClpG as a potential persistence and virulence factor in P. aeruginosa. | ||
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| 650 | 4 | |a heat tolerance | |
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| 650 | 4 | |a mobile genetic element | |
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