| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
The Effect of Crowding on Protein Stability, Rigidity, and High Pressure Sensitivity in Whole Cells
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| Autores: |
Golub, Maksym
Martinez, Nicolas
Michoud, Gregoire
Ollivier, Jacques
Jebbar, Mohamed
Oger, Philippe
Peters, Judith
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| Data: |
2018-09
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| Ano: |
2018
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| Resumo: |
In live cells, high concentrations up to 300–400 mg/mL, as in Eschericia coli (Ellis, R. J. Curr. Opin. Struct. Biol. 2001, 11, 114) are achieved which have effects on their proper functioning. However, in many experiments only individual parts of the cells as proteins or membranes are studied in order to get insight into these specific components and to avoid the high complexity of whole cells, neglecting by the way the influence of crowding. In the present study, we investigated cells of the order of Thermococcales, which are known to live under extreme conditions, in their intact form and after cell lysis to extract the effect of crowding on the molecular dynamics of the proteome and of water molecules. We found that some parameters characterizing the dynamics within the cells seem to be intrinsic to the cell type, as flexibility typical for the proteome, others are more specific to the cellular environment, as bulk water’s residence time and some fractions of particles participating to the different motions, which make the lysed cells’ dynamics similar to the one of another Thermococcale adapted to live under high hydrostatic pressure. In contrast to studies on the impact of crowding on pure proteins we show here that the release of crowding constraints on proteins leads to an increase in the rigidity and a decrease in the high pressure sensitivity. In a way similar to high pressure adaptation in piezophiles, the hydration water layer is decreased for the lysed cells, demonstrating a first link between protein adaptation and the impact of crowding or osmolytes on proteins.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
https://archimer.ifremer.fr/doc/00454/56526/58329.pdf
DOI:10.1021/acs.langmuir.8b01240
https://archimer.ifremer.fr/doc/00454/56526/
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| Editor: |
Amer Chemical Soc
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| Formato: |
application/pdf
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| Fonte: |
Langmuir (0743-7463) (Amer Chemical Soc), 2018-09 , Vol. 34 , N. 35 , P. 10419-10425
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| Direitos: |
2018 American Chemical Society
info:eu-repo/semantics/openAccess
restricted use
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