Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 1036-1052 |
| Seitenumfang | 17 |
| Fachzeitschrift | Molecular microbiology |
| Jahrgang | 91 |
| Ausgabenummer | 5 |
| Publikationsstatus | Veröffentlicht - 14 Jan. 2014 |
Abstract
Using Bacillus subtilis as a model organism, we investigated thermotolerance development by analysing cell survival and in vivo protein aggregate formation in severely heat-shocked cells primed by a mild heat shock. We observed an increased survival during severe heat stress, accompanied by a strong reduction of heat-induced cellular protein aggregates in cells lacking the ClpXP protease. We could demonstrate that the transcription factor Spx, a regulatory substrate of ClpXP, is critical for the prevention of protein aggregate formation because its regulon encodes redox chaperones, such as thioredoxin, required for protection against thiol-specific oxidative stress. Consequently B.subtilis cells grown in the absence of oxygen were more protected against severe heat shock and much less protein aggregates were detected compared to aerobically grown cells. The presented results indicate that in B.subtilisSpx and its regulon plays not only an important role for oxidative but also for heat stress response and thermotolerance development. In addition, our experiments suggest that the protection of misfolded proteins from thiol oxidation during heat shock can be critical for the prevention of cellular protein aggregation in vivo.
ASJC Scopus Sachgebiete
- Immunologie und Mikrobiologie (insg.)
- Mikrobiologie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
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in: Molecular microbiology, Jahrgang 91, Nr. 5, 14.01.2014, S. 1036-1052.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis
AU - Runde, Stephanie
AU - Molière, Noël
AU - Heinz, Anja
AU - Maisonneuve, Etienne
AU - Janczikowski, Armgard
AU - Elsholz, Alexander K.W.
AU - Gerth, Ulf
AU - Hecker, Michael
AU - Turgay, Kürşad
N1 - Copyright: Copyright 2014 Elsevier B.V., All rights reserved.
PY - 2014/1/14
Y1 - 2014/1/14
N2 - Using Bacillus subtilis as a model organism, we investigated thermotolerance development by analysing cell survival and in vivo protein aggregate formation in severely heat-shocked cells primed by a mild heat shock. We observed an increased survival during severe heat stress, accompanied by a strong reduction of heat-induced cellular protein aggregates in cells lacking the ClpXP protease. We could demonstrate that the transcription factor Spx, a regulatory substrate of ClpXP, is critical for the prevention of protein aggregate formation because its regulon encodes redox chaperones, such as thioredoxin, required for protection against thiol-specific oxidative stress. Consequently B.subtilis cells grown in the absence of oxygen were more protected against severe heat shock and much less protein aggregates were detected compared to aerobically grown cells. The presented results indicate that in B.subtilisSpx and its regulon plays not only an important role for oxidative but also for heat stress response and thermotolerance development. In addition, our experiments suggest that the protection of misfolded proteins from thiol oxidation during heat shock can be critical for the prevention of cellular protein aggregation in vivo.
AB - Using Bacillus subtilis as a model organism, we investigated thermotolerance development by analysing cell survival and in vivo protein aggregate formation in severely heat-shocked cells primed by a mild heat shock. We observed an increased survival during severe heat stress, accompanied by a strong reduction of heat-induced cellular protein aggregates in cells lacking the ClpXP protease. We could demonstrate that the transcription factor Spx, a regulatory substrate of ClpXP, is critical for the prevention of protein aggregate formation because its regulon encodes redox chaperones, such as thioredoxin, required for protection against thiol-specific oxidative stress. Consequently B.subtilis cells grown in the absence of oxygen were more protected against severe heat shock and much less protein aggregates were detected compared to aerobically grown cells. The presented results indicate that in B.subtilisSpx and its regulon plays not only an important role for oxidative but also for heat stress response and thermotolerance development. In addition, our experiments suggest that the protection of misfolded proteins from thiol oxidation during heat shock can be critical for the prevention of cellular protein aggregation in vivo.
UR - http://www.scopus.com/inward/record.url?scp=84896718349&partnerID=8YFLogxK
U2 - 10.1111/mmi.12521
DO - 10.1111/mmi.12521
M3 - Article
C2 - 24417481
AN - SCOPUS:84896718349
VL - 91
SP - 1036
EP - 1052
JO - Molecular microbiology
JF - Molecular microbiology
SN - 0950-382X
IS - 5
ER -