IN VITRO FUNGISTASIS BY A BACTERIUM (BACILLUS SUBTILIS VAR. XG AND XY)

CsaA from the Gram-positive bacterium Bacillus subtilis has been identified previously as a suppressor of the growth and protein-export defect of Escherichia coli secA(Ts) mutants. CsaA has chaperone-like activities in vivo and in vitro. To examine the role of CsaA in protein export in B. subtilis, expression of the csaA gene was repressed. While export of most proteins remained unaffected, export of at least two proteins was significantly reduced upon CsaA depletion. CsaA co-immunoprecipitates and co-purifies with the SecA proteins of E. coli and B. subtilis, and binds the B. subtilis preprotein prePhoB. Purified CsaA stimulates the translocation of prePhoB into E. coli membrane vesicles bearing the B. subtilis translocase, whereas it interferes with the SecB-mediated translocation of proOmpA into membrane vesicles of E. coli. The specific interaction with the SecA translocation ATPase and preproteins suggests that CsaA acts as a chaperone that promotes the export of a subset of preproteins in B. subtilis.

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Antibacterial activity of antagonistic bacterium Bacillus subtilis DJM-51 against phytopathogenic Clavibacter michiganense subsp. michiganense ATCC 7429 in vitro

Microbial Pathogenesis ◽

10.1016/j.micpath.2014.10.008 ◽

2014 ◽

Vol 77 ◽

pp. 13-16 ◽

Cited By ~ 7

Author(s):

W.J. Jung ◽

F. Mabood ◽

A. Souleimanov ◽

L.G. Whyte ◽

T.D. Niederberger ◽

...

Keyword(s):

Antibacterial Activity ◽

Bacillus Subtilis ◽

Antagonistic Bacterium ◽

Bacterium Bacillus Subtilis ◽

Bacterium Bacillus

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In vitro and in vivo antibiofilm potential of 2,4-Di- tert -butylphenol from seaweed surface associated bacterium Bacillus subtilis against group A streptococcus

Microbiological Research ◽

10.1016/j.micres.2016.05.010 ◽

2016 ◽

Vol 191 ◽

pp. 19-31 ◽

Cited By ~ 23

Author(s):

Dharmaprakash Viszwapriya ◽

Udayakumar Prithika ◽

Sundaresan Deebika ◽

Krishnaswamy Balamurugan ◽

Shunmugiah Karutha Pandian

Keyword(s):

Bacillus Subtilis ◽

Group A Streptococcus ◽

Group A ◽

Bacterium Bacillus Subtilis ◽

Bacterium Bacillus

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Functional investigation of Bacillus subtilis YrkF’s involvement in sulfur transfer reactions

Peptidomics ◽

10.1515/ped-2015-0008 ◽

2016 ◽

Vol 2 (1) ◽

Cited By ~ 3

Author(s):

Hannah L. Martin ◽

Katherine A. Black ◽

Patricia C. Dos Santos

Keyword(s):

Bacillus Subtilis ◽

Bioinformatic Analysis ◽

Transfer Reactions ◽

Initial Reaction ◽

Cysteine Desulfurase ◽

Sulfur Transfer ◽

Bacterium Bacillus Subtilis ◽

Bacterium Bacillus ◽

Functional Investigation

AbstractSulfur incorporation into the molybdenum cofactor (Moco) in the Gram-negative bacterium Escherichia coli involves six enzymes. The initial reaction includes the cysteine desulfurase IscS, the sulfurtransferase TusA, and the rhodanese domaincontaining protein YnjE. The Gram-positive bacterium Bacillus subtilis contains no direct homologs for IscS, but rather four distinct cysteine desulfurases (YrvO, NifS, NifZ, SufS) and YrkF, a two-domain rhodanese protein with an N-terminal domain similar to TusA. Bioinformatic analysis was used to identify potential enzymes involved in the B. subtilis Moco thiolation pathway and in vitro reactions demonstrated that YrkF can accept sulfur from and enhance the activity of YrvO.

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Antagonism of isolates of Bacillus subtilis to Phytophthora cactorum

Canadian Journal of Botany ◽

10.1139/b84-142 ◽

1984 ◽

Vol 62 (5) ◽

pp. 1032-1035 ◽

Cited By ~ 21

Author(s):

R. S. Utkhede

Keyword(s):

Bacillus Subtilis ◽

Inhibition Zone ◽

Crown Rot ◽

Root Weight ◽

Phytophthora Cactorum ◽

Sclerotium Cepivorum ◽

Greenhouse Trial ◽

Bacterium Bacillus Subtilis ◽

Bacterium Bacillus

Twenty-one isolates of the bacterium Bacillus subtilis isolated from local and exotic sclerotia of Sclerotium cepivorum were tested on cornmeal agar (CMA) for antagonism to six isolates of Phytophthora cactorum, causal agent of apple crown rot. All bacterial isolates produced diffusible antibiotics antagonistic to growth of all P. cactorum isolates on CMA. Antagonists were further evaluated in a replicated greenhouse trial for their ability to control crown rot infection on McIntosh apple seedlings in sterile soil. Six isolates of B. subtilis provided statistically significant reductions of infection on McIntosh seedlings. No correlation was observed between width of inhibition zone in vitro and protection from P. cactorum infections in McIntosh apple seedlings in a greenhouse trial. Significant negative correlations were observed between percent seedling infection and root weight.

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Release factor-dependent ribosome rescue by BrfA in the Gram-positive bacterium Bacillus subtilis

Nature Communications ◽

10.1038/s41467-019-13408-7 ◽

2019 ◽

Vol 10 (1) ◽

Cited By ~ 5

Author(s):

Naomi Shimokawa-Chiba ◽

Claudia Müller ◽

Keigo Fujiwara ◽

Bertrand Beckert ◽

Koreaki Ito ◽

...

Keyword(s):

Bacillus Subtilis ◽

Stop Codon ◽

Release Factor ◽

Positive Bacterium ◽

Gram Positive ◽

E Coli ◽

Cryo Electron Microscopy ◽

Dead End ◽

Bacterium Bacillus Subtilis ◽

Bacterium Bacillus

AbstractRescue of the ribosomes from dead-end translation complexes, such as those on truncated (non-stop) mRNA, is essential for the cell. Whereas bacteria use trans-translation for ribosome rescue, some Gram-negative species possess alternative and release factor (RF)-dependent rescue factors, which enable an RF to catalyze stop-codon-independent polypeptide release. We now discover that the Gram-positive Bacillus subtilis has an evolutionarily distinct ribosome rescue factor named BrfA. Genetic analysis shows that B. subtilis requires the function of either trans-translation or BrfA for growth, even in the absence of proteotoxic stresses. Biochemical and cryo-electron microscopy (cryo-EM) characterization demonstrates that BrfA binds to non-stop stalled ribosomes, recruits homologous RF2, but not RF1, and induces its transition into an open active conformation. Although BrfA is distinct from E. coli ArfA, they use convergent strategies in terms of mode of action and expression regulation, indicating that many bacteria may have evolved as yet unidentified ribosome rescue systems.

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