scholarly journals The yabG gene of Bacillus subtilis encodes a sporulation specific protease which is involved in the processing of several spore coat proteins

2000 ◽  
Vol 192 (1) ◽  
pp. 33-38 ◽  
Author(s):  
Hiromu Takamatsu ◽  
Atsuo Imamura ◽  
Takeko Kodama ◽  
Kei Asai ◽  
Naotake Ogasawara ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Spore Coat ◽  
Coat Proteins ◽  
Specific Protease ◽  
Spore Coat Proteins

scholarly journals Localization of the Cortex Lytic Enzyme CwlJ in Spores of Bacillus subtilis

2002 ◽  
Vol 184 (4) ◽  
pp. 1219-1224 ◽  
Author(s):  
Irina Bagyan ◽  
Peter Setlow
Keyword(s):  
Bacillus Subtilis ◽  
Spore Germination ◽  
Dipicolinic Acid ◽  
High Salt ◽  
Lytic Enzyme ◽  
Spore Coat ◽  
Coat Proteins ◽  
His Tag ◽  
Spore Coat Proteins ◽  
Triton X

ABSTRACT The enzyme CwlJ is involved in the depolymerization of cortex peptidoglycan during germination of spores of Bacillus subtilis. CwlJ with a C-terminal His tag was functional and was extracted from spores by procedures that remove spore coat proteins. However, this CwlJ was not extracted from disrupted spores by dilute buffer, high salt concentrations, Triton X-100, Ca2+-dipicolinic acid, dithiothreitol, or peptidoglycan digestion, disappeared during spore germination, and was not present in cotE spores in which the spore coat is aberrant. These findings indicate the following: (i) the reason decoated and cotE spores germinate poorly with dipicolinic acid is the absence of CwlJ from these spores; and (ii) CwlJ is located in the spore coat, presumably tightly associated with one or more other coat proteins.

scholarly journals Involvement of Superoxide Dismutase in Spore Coat Assembly in Bacillus subtilis

1998 ◽  
Vol 180 (9) ◽  
pp. 2285-2291 ◽  
Author(s):  
Adriano O. Henriques ◽  
Lawrence R. Melsen ◽  
Charles P. Moran
Keyword(s):  
Superoxide Dismutase ◽  
Bacillus Subtilis ◽  
Spore Coat ◽  
Coat Proteins ◽  
Wild Type ◽  
Outer Coat ◽  
Sod Activity ◽  
Cell Extracts ◽  
Spore Coat Proteins ◽  
Coat Layer

ABSTRACT Endospores of Bacillus subtilis are enclosed in a proteinaceous coat which can be differentiated into a thick, striated outer layer and a thinner, lamellar inner layer. We found that the N-terminal sequence of a 25-kDa protein present in a preparation of spore coat proteins matched that of the Mn-dependent superoxide dismutase (SOD) encoded by the sodA locus.sodA is transcribed throughout the growth and sporulation of a wild-type strain and is responsible for the SOD activity detected in total cell extracts prepared from B. subtilis. Disruption of the sodA locus produced a mutant that lacked any detectable SOD activity during vegetative growth and sporulation. The sodA mutant was not impaired in the ability to form heat- or lysozyme-resistant spores. However, examination of the coat layers of sodA mutant spores revealed increased extractability of the tyrosine-rich outer coat protein CotG. We showed that this condition was not accompanied by augmented transcription of the cotG gene in sporulating cells of the sodA mutant. We conclude that SodA is required for the assembly of CotG into the insoluble matrix of the spore and suggest that CotG is covalently cross-linked into the insoluble matrix by an oxidative reaction dependent on SodA. Ultrastructural analysis revealed that the inner coat formed by a sodA mutant was incomplete. Moreover, the outer coat lacked the characteristic striated appearance of wild-type spores, a pattern that was accentuated in acotG mutant. These observations suggest that the SodA-dependent formation of the insoluble matrix containing CotG is largely responsible for the striated appearance of this coat layer.

Analyse ultrastructurale et biochimique de mutants pléiotropes de Bacillus subtilis affectés dans le contrôle de la sporulation

1984 ◽  
Vol 30 (11) ◽  
pp. 1367-1376
Author(s):  
Joseph Zucca ◽  
Serge Renaudin
Keyword(s):  
Bacillus Subtilis ◽  
Pleiotropic Effect ◽  
Spore Coat ◽  
Coat Proteins ◽  
Extracellular Proteases ◽  
Transmission Electron ◽  
Mutant Strains ◽  
Spore Coat Proteins ◽  
Spore Ultrastructure ◽  
Spore Coat Protein

Derived from a Bacillus subtilis unstable mutant strains which hyperproduce extracellular proteases were found to contain mutations at loci scoC, scoD, or scoE; these were observed by transmission electron microscopy. In scoC and scoD strains, spores formed overproduced spore coat proteins and the spore ultrastructure was deeply altered. In scoE strains, stage III of the sporulation was blocked. The pleiotropic effect of scoC mutations was either positive or negative. In unstable strains, mutations at the scoC locus stimulated α-amylase and levane sucrase hyperproduction. In stable strains, the same mutations led to an absence of α-amylase synthesis but to a normal levane sucrase production. ScoD mutations only induced α-amylase hyperproduction, while scoE mutations allowed neither levane sucrase production nor spore coat protein synthesis.

scholarly journals Identification of Native Cross-Links in Bacillus subtilis Spore Coat Proteins

2021 ◽  
Author(s):  
Rick Ursem ◽  
Bhagyashree Swarge ◽  
Wishwas R. Abhyankar ◽  
Hansuk Buncherd ◽  
Leo J. de Koning ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Spore Coat ◽  
Coat Proteins ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore ◽  
Cross Links ◽  
Spore Coat Proteins

scholarly journals Synthesis and Order of Assembly of Spore Coat Proteins in Bacillus subtilis

Microbiology ◽  
1981 ◽  
Vol 123 (1) ◽  
pp. 1-16 ◽  
Author(s):  
H. F. JENKINSON ◽  
W. D. SAWYER ◽  
J. MANDELSTAM
Keyword(s):  
Bacillus Subtilis ◽  
Spore Coat ◽  
Coat Proteins ◽  
Spore Coat Proteins

scholarly journals Expression and display of Clostridium difficile protein FliD on the surface of Bacillus subtilis spores

2013 ◽  
Vol 62 (9) ◽  
pp. 1379-1385 ◽  
Author(s):  
Alessandro Negri ◽  
Wojciech Potocki ◽  
Adam Iwanicki ◽  
Michał Obuchowski ◽  
Krzysztof Hinc
Keyword(s):  
Bacillus Subtilis ◽  
Clostridium Difficile ◽  
Spore Coat ◽  
Coat Proteins ◽  
Infectious Agents ◽  
Heterologous Proteins ◽  
Oral Vaccines ◽  
Dot Blot ◽  
Protective Layers ◽  
Spore Coat Proteins

The endospores of Bacillus subtilis can serve as a tool for surface presentation of heterologous proteins. The unique properties of the spore protective layers make them perfect vehicles for orally administered vaccines. In this study, we successfully displayed a fragment of Clostridium difficile FliD protein on the surface of B. subtilis spores using the CotB, CotC, CotG and CotZ spore coat proteins. The presence of the fusion proteins in the spore coat was verified by Western blotting and immunofluorescence microscopy. The amount of recombinant proteins was assessed by a dot-blot technique. C. difficile is one of the most common infectious agents in nosocomial infections and is especially associated with antibiotic therapies. FliD is a flagellar cap protein of C. difficile and is known to be one of the immunogenic surface antigens of this bacterium. Therefore, its use in vaccine formulations gives a good perspective for successful immunization with a FliD-based vaccine. The recombinant spores presented here may be good candidates for C. difficile oral vaccines.

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