scholarly journals Membrane depolarization kills dormant Bacillus subtilis cells by generating a lethal dose of ROS

2021 ◽  
Author(s):  
Declan Gray ◽  
Biwen Wang ◽  
Pamela Gamba ◽  
Henrik Strahl ◽  
Leendert Hamoen
Keyword(s):  
Bacillus Subtilis ◽  
Fenton Reaction ◽  
Lethal Dose ◽  
Primary Source ◽  
Membrane Depolarization ◽  
Superoxide Radicals ◽  
Complex Iii ◽  
Alternative Mechanism ◽  
Iron Sulfur ◽  
Dormant Cells

Abstract The bactericidal activity of several commonly used antibiotics have been shown to partially rely on the production of reactive oxygen species (ROS). Bacterial persister cells, an important cause of recurring infections, are tolerant to these antibiotics because they are in a dormant state. However, even dormant cells must maintain a membrane potential. Here we used Bacillus subtilis as model system to study the effect of membrane depolarization on dormant cells. Surprisingly, we found that membrane depolarization also leads to ROS production. In contrast to previous studies, this does not require the Fenton reaction and results primarily in superoxide radicals. Genetic analysis revealed that Rieske factor QcrA, the iron-sulfur subunit of complex III, is a primary source of superoxide radicals. Interestingly, the membrane distribution of QcrA changed upon membrane depolarization, suggesting a dissociation of complex III. Our data reveal an alternative mechanism by which antibiotics can cause lethal ROS levels, and may partially explain why membrane-targeting antibiotics are effective in eliminating persisters.

scholarly journals Respiratory chain supercomplexes associate with the cysteine desulfurase complex of the iron–sulfur cluster assembly machinery

2018 ◽  
Vol 29 (7) ◽  
pp. 776-785 ◽  
Author(s):  
Lena Böttinger ◽  
Christoph U. Mårtensson ◽  
Jiyao Song ◽  
Nicole Zufall ◽  
Nils Wiedemann ◽  
...  
Keyword(s):  
Respiratory Chain ◽  
Complex Iii ◽  
Bc1 Complex ◽  
Cytochrome Bc1 Complex ◽  
Respiratory Chain Complexes ◽  
Cysteine Desulfurase ◽  
Complex Iv ◽  
Iron Sulfur Cluster ◽  
Iron Sulfur ◽  
Chain Complexes

Mitochondria are the powerhouses of eukaryotic cells. The activity of the respiratory chain complexes generates a proton gradient across the inner membrane, which is used by the F1FO-ATP synthase to produce ATP for cellular metabolism. In baker’s yeast, Saccharomyces cerevisiae, the cytochrome bc1 complex (complex III) and cytochrome c oxidase (complex IV) associate in respiratory chain supercomplexes. Iron–sulfur clusters (ISC) form reactive centers of respiratory chain complexes. The assembly of ISC occurs in the mitochondrial matrix and is essential for cell viability. The cysteine desulfurase Nfs1 provides sulfur for ISC assembly and forms with partner proteins the ISC-biogenesis desulfurase complex (ISD complex). Here, we report an unexpected interaction of the active ISD complex with the cytochrome bc1 complex and cytochrome c oxidase. The individual deletion of complex III or complex IV blocks the association of the ISD complex with respiratory chain components. We conclude that the ISD complex binds selectively to respiratory chain supercomplexes. We propose that this molecular link contributes to coordination of iron–sulfur cluster formation with respiratory activity.

scholarly journals Cellular Distribution of Lysyl-tRNA Synthetase and Its Interaction with Gag during Human Immunodeficiency Virus Type 1 Assembly

2004 ◽  
Vol 78 (14) ◽  
pp. 7553-7564 ◽  
Author(s):  
Rabih Halwani ◽  
Shan Cen ◽  
Hassan Javanbakht ◽  
Jenan Saadatmand ◽  
Sunghoon Kim ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Human Immunodeficiency Virus Type ◽  
Virus Type ◽  
Primary Source ◽  
Free Cell ◽  
Trna Synthetase ◽  
Complex Iii ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT Lysyl-tRNA synthetase (LysRS) is packaged into human immunodeficiency virus type 1 (HIV-1) via its interaction with Gag, and this enzyme facilitates the selective packaging of tRNA3 Lys, the primer for initiating reverse transcription, into HIV-1. The Gag/LysRS interaction is detected at detergent-resistant membrane but not in membrane-free cell compartments that contain Gag and LysRS. LysRS is found (i) in the nucleus, (ii) in a cytoplasmic high-molecular-weight aminoacyl-tRNA synthetase complex (HMW aaRS complex), (iii) in mitochondria, and (iv) associated with plasma membrane. The cytoplasmic form of LysRS lacking the mitochondrial import signal was previously shown to be efficiently packaged into virions, and in this report we also show that LysRS compartments in nuclei, in the HMW aaRS complex, and at the membrane are also not required as a primary source for viral LysRS. Exogenous mutant LysRS species unable to either enter the nucleus or bind to the cell membrane are still incorporated into virions. Many HMW aaRS components are not packaged into the virion along with LysRS, and the interaction of LysRS with p38, a protein that binds tightly to LysRS in the HMW aaRS complex, is not required for the incorporation of LysRS into virions. These data indicate that newly synthesized LysRS may interact rapidly with Gag before the enzyme has the opportunity to move to the above-mentioned cellular compartments. In confirmation of this idea, we found that newly synthesized LysRS is associated with Gag after a 10-min pulse with [35S]cysteine/methionine. This observation is also supported by previous work indicating that the incorporation of LysRS into HIV-1 is very sensitive to the inhibition of new synthesis of LysRS.

scholarly journals The motion control of the iron‐sulfur‐protein in complex III

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Lothar Esser ◽  
Fei Zhou ◽  
Chang‐An Yu ◽  
Di Xia
Keyword(s):  
Motion Control ◽  
Complex Iii ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

scholarly journals Predation by Myxococcus xanthus Induces Bacillus subtilis To Form Spore-Filled Megastructures

2014 ◽  
Vol 81 (1) ◽  
pp. 203-210 ◽  
Author(s):  
Susanne Müller ◽  
Sarah N. Strack ◽  
Sarah E. Ryan ◽  
Daniel B. Kearns ◽  
John R. Kirby
Keyword(s):  
Bacillus Subtilis ◽  
Biofilm Formation ◽  
Myxococcus Xanthus ◽  
Common Mechanism ◽  
Alternative Mechanism ◽  
Dense Matrix ◽  
Interspecies Interactions ◽  
Content Type ◽  
New Type ◽  
Surfactin Production

ABSTRACTBiofilm formation is a common mechanism for surviving environmental stress and can be triggered by both intraspecies and interspecies interactions. Prolonged predator-prey interactions between the soil bacteriumMyxococcus xanthusandBacillus subtiliswere found to induce the formation of a new type ofB. subtilisbiofilm, termed megastructures. Megastructures are tree-like brachiations that are as large as 500 μm in diameter, are raised above the surface between 150 and 200 μm, and are filled with viable endospores embedded within a dense matrix. Megastructure formation did not depend on TasA, EpsE, SinI, RemA, or surfactin production and thus is genetically distinguishable from colony biofilm formation on MSgg medium. AsB. subtilisendospores are not susceptible to predation byM. xanthus, megastructures appear to provide an alternative mechanism for survival. In addition,M. xanthusfruiting bodies were found immediately adjacent to the megastructures in nearly all instances, suggesting thatM. xanthusis unable to acquire sufficient nutrients from cells housed within the megastructures. Lastly, aB. subtilismutant lacking the ability to defend itself via bacillaene production formed megastructures more rapidly than the parent. Together, the results indicate that production of the megastructure facilitatesB. subtilisescape into dormancy via sporulation.

Zinc-Ligand Swapping Mediated Complex Formation and Sulfur Transfer between SufS and SufU for Iron–Sulfur Cluster Biogenesis in Bacillus subtilis

2017 ◽  
Vol 139 (51) ◽  
pp. 18464-18467 ◽  
Author(s):  
Takashi Fujishiro ◽  
Takuya Terahata ◽  
Kouhei Kunichika ◽  
Nao Yokoyama ◽  
Chihiro Maruyama ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Complex Formation ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Sulfur Transfer ◽  
Iron Sulfur

Ischemic Injury to Mitochondrial Electron Transport in the Aging Heart: Damage to the Iron–Sulfur Protein Subunit of Electron Transport Complex III

2001 ◽  
Vol 385 (1) ◽  
pp. 117-128 ◽  
Author(s):  
Edward J. Lesnefsky ◽  
Tatyana I. Gudz ◽  
Catharina T. Migita ◽  
Masao Ikeda-Saito ◽  
Medhat O. Hassan ◽  
...  
Keyword(s):  
Electron Transport ◽  
Ischemic Injury ◽  
Complex Iii ◽  
Protein Subunit ◽  
Aging Heart ◽  
Heart Damage ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Transport Complex
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