<i>Clostridium taeniosporum</i> spore ribbon‐like appendage structure, composition and genes

Walker, James R.; Gnanam, Annie J.; Blinkova, Alexandra; Hermandson, Mary Jo; Karymov, Mikhail A.; Lyubchenko, Yuri L.; Graves, Paul R.; Haystead, Timothy; Linse, Klaus D.

doi:10.1111/j.1365-2958.2006.05494.x

Cited by 24 publications

(49 citation statements)

References 70 publications

(127 reference statements)

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“…The amyloid coat on the merozoite surface was described as patches of regular denticulation in early schizogony and later formed long bristles and filaments that appeared thicker at apices than their stems and thus suggested the presence of a complex formation (42). Interestingly, similar filamentous extracellularly extended structures have also been reported in many eukaryotic and prokaryotic cells termed adhesins, extracellular appendages, fibrils, and filaments (43)(44)(45)(46). However, the components of merozoite's amyloid coat have remained unexplored so far.…”

Section: Discussionmentioning

confidence: 89%

Plasmodium falciparum Merozoite Surface Protein 3

Imam

Singh

Kaushik

et al. 2014

Journal of Biological Chemistry

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Background: Plasmodium falciparum merozoite surface protein 3 (MSP3) oligomerizes and binds heme. Results: MSP3 forms amyloid-like structures that bind ϳ35 heme molecules, and these filamentous structures are also present on the surface of merozoites. Conclusion: Amyloid formation by MSP3 is related to heme binding. Significance: The presence of MSP3 fibrils on merozoite surface and significant heme binding suggest its functional role during erythrocytic stages of P. falciparum.

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Section: Discussionmentioning

confidence: 89%

Plasmodium falciparum Merozoite Surface Protein 3

Imam

Singh

Kaushik

et al. 2014

Journal of Biological Chemistry

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“…There may be some sort of specific docking site for CotA and CotC on the F-pole of the spore. Asymmetric structures known as appendages are observed on the spores of several species (8,29,35,48). However, B. subtilis spores do not exhibit an appendage, so the four polar proteins are a novel asymmetric structure of the spore coat.…”

Section: Discussionmentioning

confidence: 99%

Localization of Proteins to Different Layers and Regions ofBacillus subtilisSpore Coats

et al. 2010

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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.Proper localization and assembly of proteins in cells and subcellular structures are essential features of living organisms. Complex protein assemblies, including ribosomes, flagella, and the cytokinetic machinery, play important roles in bacteria (26,27,40). Studying how these complex structures are formed is a fundamental theme in molecular biology. In this work, we developed a method to analyze one of the most complex bacterial protein assemblies: the spore coat of Bacillus subtilis.Sporulation of B. subtilis is initiated in response to nutrient limitation, and it involves a highly ordered program of gene expression and morphological change (33, 42). The first morphological change of sporulation is the appearance of an asymmetrically positioned septum that divides the cell into a larger mother cell and a smaller forespore. Next, the mother cell membrane migrates around the forespore membrane during a phagocytosislike process called engulfment. The completion of engulfment involves fusion of the mother cell membrane to pinch off the forespore within the mother cell. Compartment-specific gene expression brings about maturation of the spore and its release upon lysis of the mother cell (reviewed in reference 19). Mature spores remain viable during long periods of starvation and are resistant to heat, toxic chemicals, lytic enzymes, and other factors capable of damaging vegetative cells (30). Spores germinate and resume growth when nutrients become available (32).The outer portions of Bacillus spores consist of a cortex, a spore coat layer, and in some cases, an exosporium. The cortex, a thick layer of peptidoglycan, is deposited between the inner and the outer membranes of the forespore, and it is responsible for maintaining the highly dehydrated state of the core, thereby contri...

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“…Most proteins that have been shown to be directly involved in either assembly or production of a subset of spore coat components are small, like SpoIVA or CotE (6,51,63), whereas CrdA, CrdB, and CrdC are large repetitive proteins. Interestingly, two proteins (P29a and P29b) consisting of duplicated copies of the common 132-aa domain are part of the appendages at the surface of Clostridium taeniosporium spores (61). On the other hand, related proteins containing numerous copies of this domain can be found not only in Gram-positive spore-forming bacterial species like Clostridium or Bacillus but also in very diverse nonsporulating species like Methanothermobacter, Enterococcus, or Vibrio (see Table S5 in the supplemental material).…”

Section: Discussionmentioning

confidence: 99%

“…This type of protein is thus not specific for sporulation and may be used for different purposes in different organisms. It has previously been suggested that such repeat domain proteins might be well suited for macrostructure assembly due to their ability to bind more molecules of surrounding proteins than would structural proteins without duplicated structures (61). It could be that these proteins are commonly used to build extracellular matrices or structures at the surface of the cell or the spore in various organisms.…”

Section: Discussionmentioning

confidence: 99%

Evolutionary History and Functional Characterization of Three Large Genes Involved in Sporulation in Bacillus cereus Group Bacteria

et al. 2011

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The Bacillus cereus group of bacteria is a group of closely related species that are of medical and economic relevance, including B. anthracis, B. cereus, and B. thuringiensis. Bacteria from the Bacillus cereus group encode three large, highly conserved genes of unknown function (named crdA, crdB, and crdC) that are composed of 16 to 35 copies of a repeated domain of 132 amino acids at the protein level. Bioinformatic analysis revealed that there is a phylogenetic bias in the genomic distribution of these genes and that strains harboring all three large genes mainly belong to cluster III of the B. cereus group phylogenetic tree. The evolutionary history of the three large genes implicates gain, loss, duplication, internal deletion, and lateral transfer. Furthermore, we show that the transcription of previously identified antisense open reading frames in crdB is simultaneously regulated with its host gene throughout the life cycle in vitro, with the highest expression being at the onset of sporulation. In B. anthracis, different combinations of double-and triple-knockout mutants of the three large genes displayed slower and less efficient sporulation processes than the parental strain. Altogether, the functional studies suggest an involvement of these three large genes in the sporulation process.

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Clostridium taeniosporum spore ribbon‐like appendage structure, composition and genes

Cited by 24 publications

References 70 publications

Plasmodium falciparum Merozoite Surface Protein 3

Plasmodium falciparum Merozoite Surface Protein 3

Localization of Proteins to Different Layers and Regions ofBacillus subtilisSpore Coats

Evolutionary History and Functional Characterization of Three Large Genes Involved in Sporulation in Bacillus cereus Group Bacteria

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