Details
| Original language | English |
|---|---|
| Pages (from-to) | 423-440 |
| Number of pages | 18 |
| Journal | Molecular microbiology |
| Volume | 111 |
| Issue number | 2 |
| Early online date | 4 Dec 2018 |
| Publication status | Published - 8 Feb 2019 |
Abstract
Small heat shock proteins (sHsp) occur in all domains of life. By interacting with misfolded or aggregated proteins these chaperones fulfill a protective role in cellular protein homeostasis. Here, we demonstrate that the sHsp YocM of the Gram-positive model organism Bacillus subtilis is part of the cellular protein quality control system with a specific role in salt stress response. In the absence of YocM the survival of salt shocked cells is impaired, and increased levels of YocM protect B. subtilis exposed to heat or salt. We observed a salt and heat stress-induced localization of YocM to intracellular protein aggregates. Interestingly, purified YocM appears to accelerate protein aggregation of different model substrates in vitro. In addition, the combined presence of YocM and chemical chaperones, which accumulate in salt stressed cells, can facilitate in vitro a synergistic protective effect on protein misfolding. Therefore, the beneficial role of YocM during salt stress could be related to a mutual functional relationship with chemical chaperones and adds a new possible functional aspect to sHsp chaperone activities.
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Biochemistry, Genetics and Molecular Biology(all)
- Molecular Biology
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In: Molecular microbiology, Vol. 111, No. 2, 08.02.2019, p. 423-440.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - YocM a small heat shock protein can protect Bacillus subtilis cells during salt stress
AU - Hantke, Ingo
AU - Schäfer, Heinrich
AU - Janczikowski, Armgard
AU - Turgay, Kürşad
N1 - Funding Information: We want to thank Ulf Gerth (University of Greifswald), Dave Dubnau (PHRI, Newark, NJ) for strains and David Dougan (LaTrobe University, Melbourne) for critical reading of our manuscript. Work in our Lab was supported by the Deutsche Forschungsgemeinschaft (Tu106/6-2, Tu106/8-1) and by a PhD fellowship of the Hannover School for Biomolecular Drug Research (HSBDR) to IH.
PY - 2019/2/8
Y1 - 2019/2/8
N2 - Small heat shock proteins (sHsp) occur in all domains of life. By interacting with misfolded or aggregated proteins these chaperones fulfill a protective role in cellular protein homeostasis. Here, we demonstrate that the sHsp YocM of the Gram-positive model organism Bacillus subtilis is part of the cellular protein quality control system with a specific role in salt stress response. In the absence of YocM the survival of salt shocked cells is impaired, and increased levels of YocM protect B. subtilis exposed to heat or salt. We observed a salt and heat stress-induced localization of YocM to intracellular protein aggregates. Interestingly, purified YocM appears to accelerate protein aggregation of different model substrates in vitro. In addition, the combined presence of YocM and chemical chaperones, which accumulate in salt stressed cells, can facilitate in vitro a synergistic protective effect on protein misfolding. Therefore, the beneficial role of YocM during salt stress could be related to a mutual functional relationship with chemical chaperones and adds a new possible functional aspect to sHsp chaperone activities.
AB - Small heat shock proteins (sHsp) occur in all domains of life. By interacting with misfolded or aggregated proteins these chaperones fulfill a protective role in cellular protein homeostasis. Here, we demonstrate that the sHsp YocM of the Gram-positive model organism Bacillus subtilis is part of the cellular protein quality control system with a specific role in salt stress response. In the absence of YocM the survival of salt shocked cells is impaired, and increased levels of YocM protect B. subtilis exposed to heat or salt. We observed a salt and heat stress-induced localization of YocM to intracellular protein aggregates. Interestingly, purified YocM appears to accelerate protein aggregation of different model substrates in vitro. In addition, the combined presence of YocM and chemical chaperones, which accumulate in salt stressed cells, can facilitate in vitro a synergistic protective effect on protein misfolding. Therefore, the beneficial role of YocM during salt stress could be related to a mutual functional relationship with chemical chaperones and adds a new possible functional aspect to sHsp chaperone activities.
UR - http://www.scopus.com/inward/record.url?scp=85057717164&partnerID=8YFLogxK
U2 - 10.1111/mmi.14164
DO - 10.1111/mmi.14164
M3 - Article
C2 - 30431188
AN - SCOPUS:85057717164
VL - 111
SP - 423
EP - 440
JO - Molecular microbiology
JF - Molecular microbiology
SN - 0950-382X
IS - 2
ER -