| Autor: |
Julien Mortier, Elisa Gayán, Ronald Van Eyken, Oscar Enrique Torres Montaguth, Ladan Khodaparast, Laleh Khodaparast, Bert Houben, Sebastien Carpentier, Frederic Rousseau, Joost Schymkowitz, Abram Aertsen |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
mBio, Vol 12, Iss 4 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2150-7511 |
| DOI: |
10.1128/mBio.01129-21 |
| Popis: |
ABSTRACT Despite our extensive knowledge of the genetic regulation of heat shock proteins (HSPs), the evolutionary routes that allow bacteria to adaptively tune their HSP levels and corresponding proteostatic robustness have been explored less. In this report, directed evolution experiments using the Escherichia coli model system unexpectedly revealed that seemingly random single mutations in its tnaA gene can confer significant heat resistance. Closer examination, however, indicated that these mutations create folding-deficient and aggregation-prone TnaA variants that in turn can endogenously and preemptively trigger HSP expression to cause heat resistance. These findings, importantly, demonstrate that even erosive mutations with disruptive effects on protein structure and functionality can still yield true gain-of-function alleles with a selective advantage in adaptive evolution. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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