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 |