scholarly journals Role of DNA repair in Bacillus subtilis spore resistance.

1996 ◽  
Vol 178 (12) ◽  
pp. 3486-3495 ◽  
Author(s):  
B Setlow ◽  
P Setlow
Keyword(s):  
Dna Repair ◽  
Bacillus Subtilis ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore ◽  
Spore Resistance

scholarly journals Role of DNA repair in Bacillus subtilis spore resistance to high energy and low energy electron beam treatments

2020 ◽  
Vol 87 ◽  
pp. 103353 ◽  
Author(s):  
Yifan Zhang ◽  
Nina Huber ◽  
Ralf Moeller ◽  
Jörg Stülke ◽  
Barbora Dubovcova ◽  
...  
Keyword(s):  
Dna Repair ◽  
Bacillus Subtilis ◽  
Electron Beam ◽  
High Energy ◽  
Low Energy ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore ◽  
Spore Resistance ◽  
Low Energy Electron

scholarly journals Role of DNA Repair by Nonhomologous-End Joining in Bacillus subtilis Spore Resistance to Extreme Dryness, Mono- and Polychromatic UV, and Ionizing Radiation

2007 ◽  
Vol 189 (8) ◽  
pp. 3306-3311 ◽  
Author(s):  
Ralf Moeller ◽  
Erko Stackebrandt ◽  
Günther Reitz ◽  
Thomas Berger ◽  
Petra Rettberg ◽  
...  
Keyword(s):  
Dna Repair ◽  
Bacillus Subtilis ◽  
Ionizing Radiation ◽  
Ultrahigh Vacuum ◽  
Nonhomologous End Joining ◽  
Wild Type ◽  
Dna Double Strand Breaks ◽  
End Joining ◽  
Spore Resistance

ABSTRACT The role of DNA repair by nonhomologous-end joining (NHEJ) in spore resistance to UV, ionizing radiation, and ultrahigh vacuum was studied in wild-type and DNA repair mutants (recA, splB, ykoU, ykoV, and ykoU ykoV mutants) of Bacillus subtilis. NHEJ-defective spores with mutations in ykoU, ykoV, and ykoU ykoV were significantly more sensitive to UV, ionizing radiation, and ultrahigh vacuum than wild-type spores, indicating that NHEJ provides an important pathway during spore germination for repair of DNA double-strand breaks.

scholarly journals Assembly of Multiple CotC Forms into the Bacillus subtilis Spore Coat

2004 ◽  
Vol 186 (4) ◽  
pp. 1129-1135 ◽  
Author(s):  
Rachele Isticato ◽  
Giovanni Esposito ◽  
Rita Zilhão ◽  
Sofia Nolasco ◽  
Giuseppina Cangiano ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Posttranslational Modifications ◽  
Mother Cell ◽  
Spore Coat ◽  
Spore Surface ◽  
Subtilis Spore ◽  
Cell Compartment ◽  
Bacillus Subtilis Spore ◽  
Molecular Masses

ABSTRACT We report evidence that the CotC polypeptide, a previously identified component of the Bacillus subtilis spore coat, is assembled into at least four distinct forms. Two of these, having molecular masses of 12 and 21 kDa, appeared 8 h after the onset of sporulation and were probably assembled on the forming spore immediately after their synthesis, since no accumulation of either of them was detected in the mother cell compartment, where their synthesis occurs. The other two components, 12.5 and 30 kDa, were generated 2 h later and were probably the products of posttranslational modifications of the two early forms occurring directly on the coat surface during spore maturation. None of the CotC forms was found either on the spore coat or in the mother cell compartment of a cotH mutant. This indicates that CotH serves a dual role of stabilizing the early forms of CotC and promoting the assembly of both early and late forms on the spore surface.

scholarly journals Protective Role of Spore Structural Components in Determining Bacillus subtilis Spore Resistance to Simulated Mars Surface Conditions

2012 ◽  
Vol 78 (24) ◽  
pp. 8849-8853 ◽  
Author(s):  
Ralf Moeller ◽  
Andrew C. Schuerger ◽  
Günther Reitz ◽  
Wayne L. Nicholson
Keyword(s):  
Bacillus Subtilis ◽  
Dipicolinic Acid ◽  
Protective Role ◽  
Structural Components ◽  
Wild Type ◽  
Content Type ◽  
Surface Conditions ◽  
Bacillus Subtilis Spore ◽  
Spore Resistance

ABSTRACTSpores of wild-type and mutantBacillus subtilisstrains lacking various structural components were exposed to simulated Martian atmospheric and UV irradiation conditions. Spore survival and mutagenesis were strongly dependent on the functionality of all of the structural components, with small acid-soluble spore proteins, coat layers, and dipicolinic acid as key protectants.

scholarly journals Bacillus subtilis Spore Resistance to Simulated Mars Surface Conditions

2019 ◽  
Vol 10 ◽  
Author(s):  
Marta Cortesão ◽  
Felix M. Fuchs ◽  
Fabian M. Commichau ◽  
Patrick Eichenberger ◽  
Andrew C. Schuerger ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Subtilis Spore ◽  
Surface Conditions ◽  
Bacillus Subtilis Spore ◽  
Spore Resistance

scholarly journals Laccase and Its Mutant Displayed on the Bacillus subtilis Spore Coat for Oxidation of Phenolic Compounds in Organic Solvents

Catalysts ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 606
Author(s):  
Silu Sheng ◽  
Edgardo T. Farinas
Keyword(s):  
Bacillus Subtilis ◽  
Organic Solvents ◽  
Environmental Changes ◽  
Sinapic Acid ◽  
Product Yield ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Bacillus Subtilis Spore ◽  
Cota Laccase ◽  
Inert Surface

Enzymes displayed on the Bacillus subtilis spore coat have several features that are useful for biocatalysis. The enzyme is preimmobilized on an inert surface of the spore coat, which is due to the natural sporulation process. As a result, protein stability can be increased, and they are resistant to environmental changes. Next, they would not lyse under extreme conditions, such as in organic solvents. Furthermore, they can be easily removed from the reaction solution and reused. The laboratory evolved CotA laccase variant T480A-CotA was used to oxidize the following phenolic substrates: (+)-catechin, (−)-epicatechin, and sinapic acid. The kinetic parameters were determined and T480A-CotA had a greater Vmax/Km than wt-CotA for all substrates. The Vmax/Km for T480A-CotA was 4.1, 5.6, and 1.4-fold greater than wt-CotA for (+)-catechin, (−)-epicatechin, and sinapic acid, respectively. The activity of wt-CotA and T480A-CotA was measured at different concentrations from 0–70% in organic solvents (dimethyl sulfoxide, ethanol, methanol, and acetonitrile). The Vmax for T480A-CotA was observed to be greater than the wt-CotA in all organic solvents. Finally, the T480A-CotA was recycled 7 times over a 23-h period and up to 60% activity for (+)-catechin remained. The product yield was up to 3.1-fold greater than the wild-type.

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