scholarly journals Physical interaction and assembly of Bacillus subtilis spore coat proteins CotE and CotZ studied by atomic force microscopy

2016 ◽  
Vol 195 (2) ◽  
pp. 245-251 ◽  
Author(s):  
Huiqing Liu ◽  
Haiyan Qiao ◽  
Daniela Krajcikova ◽  
Zhe Zhang ◽  
Hongda Wang ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Bacillus Subtilis ◽  
Physical Interaction ◽  
Spore Coat ◽  
Coat Proteins ◽  
Subtilis Spore ◽  
Force Microscopy ◽  
Bacillus Subtilis Spore ◽  
Atomic Force ◽  
Spore Coat Proteins

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 Bacillus subtilis Spore Coat

1999 ◽  
Vol 63 (1) ◽  
pp. 1-20 ◽  
Author(s):  
Adam Driks
Keyword(s):  
Bacillus Subtilis ◽  
Posttranslational Processing ◽  
Spore Coat ◽  
Coat Proteins ◽  
Spore Surface ◽  
Subtilis Spore ◽  
Cell Type ◽  
Dormant Cell ◽  
Bacillus Subtilis Spore ◽  
Specialized Program

SUMMARY In response to starvation, bacilli and clostridia undergo a specialized program of development that results in the production of a highly resistant dormant cell type known as the spore. A proteinacious shell, called the coat, encases the spore and plays a major role in spore survival. The coat is composed of over 25 polypeptide species, organized into several morphologically distinct layers. The mechanisms that guide coat assembly have been largely unknown until recently. We now know that proper formation of the coat relies on the genetic program that guides the synthesis of spore components during development as well as on morphogenetic proteins dedicated to coat assembly. Over 20 structural and morphogenetic genes have been cloned. In this review, we consider the contributions of the known coat and morphogenetic proteins to coat function and assembly. We present a model that describes how morphogenetic proteins direct coat assembly to the specific subcellular site of the nascent spore surface and how they establish the coat layers. We also discuss the importance of posttranslational processing of coat proteins in coat morphogenesis. Finally, we review some of the major outstanding questions in the field.

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.

Display of Bombyx mori Nucleopolyhedrovirus GP64 on the Bacillus subtilis Spore Coat

2011 ◽  
Vol 62 (5) ◽  
pp. 1368-1373 ◽  
Author(s):  
Guohui Li ◽  
Qi Tang ◽  
Huiqing Chen ◽  
Qin Yao ◽  
Degang Ning ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Bombyx Mori ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Bombyx Mori Nucleopolyhedrovirus ◽  
Bacillus Subtilis Spore

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 Temporal and spatial regulation of protein cross-linking by the pre-assembled substrates of a Bacillus subtilis spore coat transglutaminase

PLoS Genetics ◽  
2019 ◽  
Vol 15 (4) ◽  
pp. e1007912 ◽  
Author(s):  
Catarina G. Fernandes ◽  
Diogo Martins ◽  
Guillem Hernandez ◽  
Ana L. Sousa ◽  
Carolina Freitas ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Cross Linking ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Spatial Regulation ◽  
Bacillus Subtilis Spore ◽  
Temporal And Spatial ◽  
Protein Cross Linking

scholarly journals Localization of Proteins to Different Layers and Regions of Bacillus subtilis Spore Coats

2009 ◽  
Vol 192 (2) ◽  
pp. 518-524 ◽  
Author(s):  
Daisuke Imamura ◽  
Ritsuko Kuwana ◽  
Hiromu Takamatsu ◽  
Kazuhito Watabe
Keyword(s):  
Bacillus Subtilis ◽  
Mother Cell ◽  
Fluorescent Proteins ◽  
Bacterial Spores ◽  
Spore Coat ◽  
Subtilis Spore ◽  
Proximal Pole ◽  
Outer Coat ◽  
Outermost Layer ◽  
Bacillus Subtilis Spore

ABSTRACT Bacterial spores are encased in a multilayered proteinaceous shell known as the coat. In Bacillus subtilis, over 50 proteins are involved in spore coat assembly but the locations of these proteins in the spore coat are poorly understood. Here, we describe methods to estimate the positions of protein fusions to fluorescent proteins in the spore coat by using fluorescence microscopy. Our investigation suggested that CotD, CotF, CotT, GerQ, YaaH, YeeK, YmaG, YsnD, and YxeE are present in the inner coat and that CotA, CotB, CotC, and YtxO reside in the outer coat. In addition, CotZ and CgeA appeared in the outermost layer of the spore coat and were more abundant at the mother cell proximal pole of the forespore, whereas CotA and CotC were more abundant at the mother cell distal pole of the forespore. These polar localizations were observed both in sporangia prior to the release of the forespore from the mother cell and in mature spores after release. Moreover, CotB was observed at the middle of the spore as a ring- or spiral-like structure. Formation of this structure required cotG expression. Thus, we conclude not only that the spore coat is a multilayered assembly but also that it exhibits uneven spatial distribution of particular proteins.

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