In silico characterization of the global Geobacillus and Parageobacillus secretome

Show simple item record

dc.contributor.author Lebre, Pedro H.
dc.contributor.author Aliyu, Habibu
dc.contributor.author De Maayer, Pieter
dc.contributor.author Cowan, Don A.
dc.date.accessioned 2019-10-25T12:31:45Z
dc.date.available 2019-10-25T12:31:45Z
dc.date.issued 2018-10-03
dc.description Additional file 1: Table S1. Similarity matrix. Table showing the percentage of orthology between the secretomes of the 64 genomes used in this study. This similarity matrix was used to generate the orthology dendogram in Fig. 6. en_ZA
dc.description Additional file 2: Table S2. Presence/absence matrix of the global secretome of Geobacillus and Parageobacillus. Table showing the presence or absence of the 772 protein sequences constituting the global secretome (annotated in the first row) across the 64 genomes used in this study (annotated in the first column). Presence/absence is indicated using a binary code of 1 and 0 to represent presence and absence, respectively. en_ZA
dc.description Additional file 3: Figure S1. Distribution of GH families across the 51 glycoside hydrolases present in the global secretome. Pie-chart showing the distribution of glycoside hydrolase families in the global secretome of Geobacillus and Parageobacillus. The four most abundant families represented in the dataset include beta-galactosidases (GH2), alpha-amylases (GH13), chitinases (GH18), and lytic transglycosylases (GH23). The following families were also found to be present in the global secretome: GH1– beta-glucosidases and beta-galactosidases; GH 3–beta-d-glucosidases, alpha-l-arabinofuranosidases; GH5–cellulases; GH10–endo-beta-1,3-xylanases; GH19–chitinases; GH25–chalaropsis-type lysozymes; GH27–alphagalactosidases and alpha-N-acetylgalactosaminidases; GH32–invertases; GH43–endo-alpha-l-arabinanases and beta-d-xylosidases; GH52–betaxylosidases; GH53–beta-1,4-galactanases; GH70–transglucosylases; GH73–beta-N-acetylglucosaminidases. en_ZA
dc.description Additional file 4: Figure S2. Xylanase activity assay of Geobacillus and Parageobacillus type strains on Oat Spelt Xylan. Bar-plot showing the xylan degrading activity of the supernatant of selected Geobacillus and Parageobacillus strains, as measured using the DNS protocol [91]. The concentration of reduced sugars was determined by measuring the average absorbance of each sample against a xylose standard. Strains were labelled as follow: T1–P. thermoglucosidasius DSM 2542T; T2–G. subterraneus DSM 15332T; T3–P. caldoxylosilyticus DSM 12041T; T4–G. thermodenitrificans DSM 465T; T5–G. stearothermophilus ATCC 12980T; T6–G. kaustophilus DSM 7263T; T7–P. thermoantarcticus M1T; T8 - P. toebii DSM 14590T. en_ZA
dc.description Additional file 5: Figure S3. Qualitative amylase activity plate assays. Description of data: 1% Starch agar plates showing the starch-degrading activity of the supernatant of the Geobacilus and Parageobacillus strains tested. The plates were stained with iodine tincture (2.5% w/v Iodine, 2.5% Potassium Iodide), and the areas of clearance represent starch degradation and corresponding amylase activity. The strains were labelled as described for Figure S2, and the positive control used in this assay (+) is α-amylase from Aspergillus oryzae, provided by Sigma-Aldrich® (Product Code: 9001-19-8). en_ZA
dc.description Additional file 6: Figure S4. PNPB Lipase activity assay of Geobacillus and Parageobacillus strains. Description of data: Bar-plot showing the degradation rates of PNPB by the supernatant of the eight Geobacillus and Parageobacillus strains tested. The labelling for the different strains is the same as described for Additional file 4: Figure S2. en_ZA
dc.description Additional file 7: Table S3. Blast results for proteins with homology to biotechnologically relevant enzymes. Description of data: Table showing the blast results for the most significant hits between protein sequences from the global secretome and enzymes from the Uniprot database that have been previously highlighted as being of biotechnological relevance. The scores and e-values, as well as the accession numbers were obtained using the Blast function against the UniprotDB. en_ZA
dc.description.abstract BACKGROUND : Geobacillus and Parageobacillus are two ecologically diverse thermophilic genera within the phylum Firmicutes. These taxa have long been of biotechnological interest due to their ability to secrete thermostable enzymes and other biomolecules that have direct applications in various industrial and clinical fields. Despite the commercial and industrial interest in these microorganisms, the full scope of the secreted protein, i.e. the secretome, of Geobacillus and Parageobacillus species remains largely unexplored, with most studies focusing on single enzymes. A genome-wide exploration of the global secretome can provide a platform for understanding the extracellular functional “protein cloud” and the roles that secreted proteins play in the survival and adaptation of these biotechnologically relevant organisms. RESULTS : In the present study, the global secretion profile of 64 Geobacillus and Parageobacillus strains, comprising 772 distinct proteins, was predicted using comparative genomic approaches. Thirty-one of these proteins are shared across all strains used in this study and function in cell-wall/membrane biogenesis as well as transport and metabolism of carbohydrates, amino acids and inorganic ions. An analysis of the clustering patterns of the secretomes of the 64 strains according to shared functional orthology revealed a correlation between the secreted profiles of different strains and their phylogeny, with Geobacillus and Parageobacillus species forming two distinct functional clades. CONCLUSIONS : The in silico characterization of the global secretome revealed a metabolically diverse set of secreted proteins, which include proteases, glycoside hydrolases, nutrient binding proteins and toxins. en_ZA
dc.description.department Biochemistry en_ZA
dc.description.department Genetics en_ZA
dc.description.department Microbiology and Plant Pathology en_ZA
dc.description.librarian am2019 en_ZA
dc.description.sponsorship This study was funded through a University of Pretoria (UP) Postdoctoral Researcher fellowship. en_ZA
dc.description.sponsorship A University of Pretoria (UP) Postdoctoral Researcher fellowship. en_ZA
dc.description.uri http://www.microbialcellfactories.com en_ZA
dc.identifier.citation Lebre, P.H., Aliyu, H., De Maayer, P. et al. 2018, 'In silico characterization of the global Geobacillus and Parageobacillus secretome', Microbial Cell Factories, vol. 17, art. 156, pp. 1-19. en_ZA
dc.identifier.issn 1475-2859
dc.identifier.other 10.1186/s12934-018-1005-9
dc.identifier.uri http://hdl.handle.net/2263/72013
dc.language.iso en en_ZA
dc.publisher BioMed Central en_ZA
dc.rights © The Author(s) 2018. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License. en_ZA
dc.subject Geobacillus en_ZA
dc.subject Parageobacillus en_ZA
dc.subject Thermophilic en_ZA
dc.subject Global secretome en_ZA
dc.subject Comparative genomics en_ZA
dc.subject Biotechnological potential en_ZA
dc.title In silico characterization of the global Geobacillus and Parageobacillus secretome en_ZA
dc.type Article en_ZA


Files in this item

This item appears in the following Collection(s)

Show simple item record