DnaK and GroEL chaperones are recruited to the Bacillus subtilis membrane after short-term ethanol stress

Seydlová, Gabriela; Halada, Petr; Fišer, Radovan; Toman, Ondřej; Ulrych, Aleš; Svobodová, J

doi:10.1111/j.1365-2672.2012.05238.x

Cited by 48 publications

(35 citation statements)

References 44 publications

(70 reference statements)

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“…Ethanol increases membrane leakage and affects the properties of all biological molecules in bacteria (6,26). In B. subtilis, ethanol induces recruitment of the molecular chaperones DnaK and GroEL to the cell membrane (52). Interestingly, the DEAD-box RNA helicase CrhR of the cyanobacterium Synechocystis sp.…”

Section: Resultsmentioning

confidence: 99%

Roles of Four Putative DEAD-Box RNA Helicase Genes in Growth of Listeria monocytogenes EGD-e under Heat, pH, Osmotic, Ethanol, and Oxidative Stress Conditions

Markkula

Lindström

Johansson

et al. 2012

Appl Environ Microbiol

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ABSTRACTTo examine the role of the four putative DEAD-box RNA helicase genes ofListeria monocytogenesEGD-e in stress tolerance, the growth of the Δlmo0866, Δlmo1246, Δlmo1450, and Δlmo1722deletion mutant strains at 42.5°C, at pH 5.6 or pH 9.4, in 6% NaCl, in 3.5% ethanol, and in 5 mM H2O2was studied. Restricted growth of the Δlmo0866deletion mutant strain in 3.5% ethanol suggests that Lmo0866 contributes to ethanol stress tolerance ofL. monocytogenesEGD-e. The Δlmo1450mutant strain showed negligible growth at 42.5°C, at pH 9.4, and in 5 mM H2O2and a lower maximum growth temperature than the wild-type EGD-e, suggesting that Lmo1450 is involved in the tolerance ofL. monocytogenesEGD-e to heat, alkali, and oxidative stresses. The altered stress tolerance of the Δlmo0866and Δlmo1450deletion mutant strains did not correlate with changes in relative expression levels oflmo0866andlmo1450genes under corresponding stresses, suggesting that Lmo0866- and Lmo1450-dependent tolerance to heat, alkali, ethanol, or oxidative stress is not regulated at the transcriptional level. Growth of the Δlmo1246and Δlmo1722deletion mutant strains did not differ from that of the wild-type EGD-e under any of the conditions tested, suggesting that Lmo1246 and Lmo1722 have no roles in the growth ofL. monocytogenesEGD-e under heat, pH, osmotic, ethanol, or oxidative stress. This study shows that the putative DEAD-box RNA helicase geneslmo0866andlmo1450play important roles in tolerance ofL. monocytogenesEGD-e to ethanol, heat, alkali, and oxidative stresses.

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Section: Resultsmentioning

confidence: 99%

Roles of Four Putative DEAD-Box RNA Helicase Genes in Growth of Listeria monocytogenes EGD-e under Heat, pH, Osmotic, Ethanol, and Oxidative Stress Conditions

Markkula

Lindström

Johansson

et al. 2012

Appl Environ Microbiol

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“…This may be due to the phospholipid composition of the L. lactis membrane which is composed of saturated, unsaturated, and cyclic fatty acids (37), similar to the O. oeni membrane. In contrast, the B. subtilis membrane has a high saturated fatty acid content (90%) (11). Phospholipid composition also influences the degree to which temperature affects the lipid organization (termed "lipid bilayer phase behavior").…”

Section: Discussionmentioning

confidence: 99%

“…The stabilizing effect of Lo18 on other natural membranes was checked by using liposomes made from phospholipids extracted from B. subtilis or L. lactis. These two bacteria have a fatty acid content distinct from that of O. oeni (11,37). B. subtilis contains predominantly branched saturated fatty acids, leading to a membrane of higher rigidity (R ϭ 0.191 units) than O. oeni (R ϭ 0.163) and L. lactis (R ϭ 0.177).…”

Section: Interaction Ofmentioning

confidence: 99%

“…For example, the cyanobacterium Synechocystis synthesizes Hsp70 (also known as the molecular chaperone DnaK) in response to the membrane fluidizer bimoclomol, a hydroxylamine derivative (10). Several Hsp, such as DnaK and GroEL, can bind membranes (11). Torok et al also showed that during heat shock in vitro, Synechocystis GroEL interacts with model lipid membranes, resulting in the increase of the molecular order of lipid bilayers and stabilization of the membrane (12).…”

mentioning

confidence: 99%

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Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity

Maitre¹,

Weidmann²,

Dubois‐Brissonnet

et al. 2014

Appl Environ Microbiol

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cMalolactic fermentation in wine is often carried out by Oenococcus oeni. Wine is a stressful environment for bacteria because ethanol is a toxic compound that impairs the integrity of bacterial membranes. The small heat shock protein (sHsp) Lo18 is an essential actor of the stress response in O. oeni. Lo18 prevents the thermal aggregation of proteins and plays a crucial role in membrane quality control. Here, we investigated the interaction between Lo18 and four types of liposomes: one was prepared from O. oeni grown under optimal growth conditions (here, control liposomes), one was prepared from O. oeni grown in the presence of 8% ethanol (here, ethanol liposomes), one was prepared from synthetic phospholipids, and one was prepared from phospholipids from Bacillus subtilis or Lactococcus lactis. We observed the strongest interaction between Lo18 and control liposomes. The lipid binding activity of Lo18 required the dissociation of oligomeric structures into dimers. Protein protection experiments carried out in the presence of the liposomes from O. oeni suggested that Lo18 had a higher affinity for control liposomes than for a model protein. In anisotropy experiments, we mimicked ethanol action by temperature-dependent fluidization of the liposomes. Results suggest that the principal determinant of Lo18-membrane interaction is lipid bilayer phase behavior rather than phospholipid composition. We suggest a model to describe the ethanol adaptation of O. oeni. This model highlights the dual role of Lo18 in the protection of proteins from aggregation and membrane stabilization and suggests how modifications of phospholipid content may be a key factor determining the balance between these two functions.

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“…Bukau et al (1993) showed the presence of DnaK on the membrane of E. coli, as detected by electron microscopy, an observation that has been forgotten for many years. The presence of DnaK in membranes has also been reported in Fusobacterium nucleatum (Skar et al 2003) and Bacillus subtilis (Seydlova et al 2012). The latter was observed after ethanol stress suggesting that changes in membrane fluidity may play a role in its insertion (Horváth et al 2008).…”

Section: Hsp70mentioning

confidence: 65%

Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes

López¹,

Cauvi

Arispe

et al. 2016

Cell Stress and Chaperones

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The cellular response to stress is orchestrated by the expression of a family of proteins termed heat shock proteins (hsp) that are involved in the stabilization of basic cellular processes to preserve cell viability and homeostasis. The bulk of hsp function occurs within the cytosol and subcellular compartments. However, some hsp have also been found outside cells released by an active mechanism independent of cell death. Extracellular hsp act as signaling molecules directed at activating a systemic response to stress. The export of hsp requires the translocation from the cytosol into the extracellular milieu across the plasma membrane. We have proposed that membrane insertion is the initial step in this export process. We investigated the interaction of the major inducible hsp from mammalian (Hsp70) and bacterial (DnaK) species with liposomes. We found that mammalian Hsp70 displayed a high specificity for negatively charged phospholipids, such as phosphatidyl serine, whereas DnaK interacted with all lipids tested regardless of the charge. Both proteins were inserted into the lipid bilayer as demonstrated by resistance to acid or basic washes that was confirmed by partial protection from proteolytic cleavage. Several regions of mammalian Hsp70 were inserted into the membrane with a small portion of the N-terminus end exposed to the outer phase of the liposome. In contrast, the N-terminus end of DnaK was inserted into the membrane, exposing the C-terminus end outside the liposome. Mammalian Hsp70 was found to make high oligomeric complexes upon insertion into the membranes whereas DnaK only formed dimers within the lipid bilayer. These observations suggest that both Hsp70s interact with lipids, but mammalian Hsp70 displays a high degree of specificity and structure as compared with the bacterial form.

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DnaK and GroEL chaperones are recruited to the Bacillus subtilis membrane after short-term ethanol stress

Cited by 48 publications

References 44 publications

Roles of Four Putative DEAD-Box RNA Helicase Genes in Growth of Listeria monocytogenes EGD-e under Heat, pH, Osmotic, Ethanol, and Oxidative Stress Conditions

Roles of Four Putative DEAD-Box RNA Helicase Genes in Growth of Listeria monocytogenes EGD-e under Heat, pH, Osmotic, Ethanol, and Oxidative Stress Conditions

Adaptation of the Wine Bacterium Oenococcus oeni to Ethanol Stress: Role of the Small Heat Shock Protein Lo18 in Membrane Integrity

Bacterial Hsp70 (DnaK) and mammalian Hsp70 interact differently with lipid membranes

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