CotG-Like Modular Proteins Are Common among Spore-Forming Bacilli

Saggese, Anella; Isticato, Rachele; Cangiano, Giuseppina; Ricca, Ezio; Baccigalupi, Loredana

doi:10.1128/jb.00023-16

Cited by 13 publications

(31 citation statements)

References 27 publications

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“…Our results show that in genomes where CotH is absent, its substrates, CotG and CotB, are also absent [91]. Nevertheless, the role of CotG may be carried out by a non-homologous CotG-like protein with similar structural regions, as previously reported [61]. Other CotH-dependent coat proteins, such as CotC and CotU are conserved in few genomes of the Subtilis group, and they are present when CotH and CotG are present.…”

Section: Discussionsupporting

confidence: 78%

“…. For instance, it has been previously reported that CotG is not highly conserved across the Bacillus genus, although its role may be carried out by a non-homologous CotG-like protein that has similar structural regions to CotG [61]. Therefore, we do not rule out the possibility that non-homologous coat-like proteins with similar structural and chemical features may perform the role of poorly conserved coat proteins.…”

Section: Spore-coat-protein Diversity Across Bacillalesmentioning

confidence: 90%

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Diversity and evolutionary dynamics of spore-coat proteins in spore-forming species of Bacillales

2020

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Among members of the Bacillales order, there are several species capable of forming a structure called an endospore. Endospores enable bacteria to survive under unfavourable growth conditions and germinate when environmental conditions are favourable again. Spore-coat proteins are found in a multilayered proteinaceous structure encasing the spore core and the cortex. They are involved in coat assembly, cortex synthesis and germination. Here, we aimed to determine the diversity and evolutionary processes that have influenced spore-coat genes in various spore-forming species of Bacillales using an in silico approach. For this, we used sequence similarity searching algorithms to determine the diversity of coat genes across 161 genomes of Bacillales. The results suggest that among Bacillales, there is a well-conserved core genome, composed mainly by morphogenetic coat proteins and spore-coat proteins involved in germination. However, some spore-coat proteins are taxa-specific. The best-conserved genes among different species may promote adaptation to changeable environmental conditions. Because most of the Bacillus species harbour complete or almost complete sets of spore-coat genes, we focused on this genus in greater depth. Phylogenetic reconstruction revealed eight monophyletic groups in the Bacillus genus, of which three are newly discovered. We estimated the selection pressures acting over spore-coat genes in these monophyletic groups using classical and modern approaches and detected horizontal gene transfer (HGT) events, which have been further confirmed by scanning the genomes to find traces of insertion sequences. Although most of the genes are under purifying selection, there are several cases with individual sites evolving under positive selection. Finally, the HGT results confirm that sporulation is an ancestral feature in Bacillus .

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Section: Discussionsupporting

confidence: 78%

Section: Spore-coat-protein Diversity Across Bacillalesmentioning

confidence: 90%

Diversity and evolutionary dynamics of spore-coat proteins in spore-forming species of Bacillales

2020

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“…Previous studies on the structural characterization of the cotB/cotH/cotG cluster in 128 B. subtilis made use of polar insertional mutations, and it is unclear how the absence of 129 (Giglio et al, 2011, Sacco et al, 1995, Saggese et al, 2016 (Fig. 1 and S1).…”

Section: Spores 127mentioning

confidence: 99%

“…The SKR G region is also predicted to be disordered and may be susceptible to 530 proteolysis (Giglio et al, 2011, Saggese et al, 2016. The repeat region of B. anthracis 531 ExsB, a CotG homologue, was also found to be extremely sensitive to proteolysis 532 of coat proteins following their synthesis in the mother cell, and in promoting the formation 539 of protein complexes competent for assembly (Isticato et al, 2013, Isticato et al, 2015.…”

Section: And Because the Interaction Between Cotg And 523mentioning

confidence: 99%

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A protein phosphorylation module patterns theBacillus subtilisspore outer coat

Freitas

Plannic

Isticato

et al. 2018

Preprint

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30Assembly of the Bacillus subtilis spore coat involves over 80 protein components, 31 which self-organize into a basal layer, a lamellar inner coat, a striated electrondense outer 32 coat and a more external crust. CotB is an abundant component of the outer coat. Its C-33 terminal moiety contains a region, termed SKR B , formed by a series of serine-rich repeats, 34 which we show is phosphorylated by the coat-associated Ser/Thr kinase CotH at multiple 35 Ser residues. Another coat protein, CotG, which contains a central repeat region, SKR G , 36interacts with the C-terminal moiety of CotB and promotes its phosphorylation by CotH in 37 vivo and in a heterologous system. CotG itself is phosphorylated by CotH but 38 phosphorylation is enhanced in the absence of CotB. Spores of a cotH D288A strain, 39producing an inactive form of the kinase, like those formed by a cotG deletion mutant, lack 40 the characteristic pattern of electrondense outer coat striations, while retaining the crust. 41Specifically, in the absence of CotG or CotH activity, most of the outer coat proteins are 42 assembled but form a layer of amorphous material that peels-off the spore if crust 43 formation is genetically ablated. In contrast, deletion of the SKR B region, has no major 44 impact on the structure of the outer coat. Thus, phosphorylation of CotG by CotH is the 45 principal factor establishing the structural pattern of the spore outer coat. The presence of 46 the cotB/cotH/cotG cluster in several species closely related to B. subtilis and of cotG-like 47

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