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pmid:33673118

Chitin Degradation Machinery and Secondary Metabolite Profiles in the Marine Bacterium Pseudoalteromonas rubra S4059.

Xiyan Wang · Thomas Isbrandt · Mikael Lenz Strube · Sara Skøtt Paulsen · Maike Wennekers Nielsen · Yannick Buijs · Erwin M Schoof · Thomas Ostenfeld Larsen · Lone Gram · Sheng-Da Zhang

Marine drugs · 2021 doi:10.3390/md19020108

Paper

complete

Experiment

complete

Data

partial

Analysis

partial

Execution

absent

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Chitin Degradation Machinery and Secondary Metabolite Profiles in the Marine Bacterium Pseudoalteromonas rubra S4059.
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10.3390/md19020108
pmid
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Xiyan Wang
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Thomas Isbrandt
[2]
Mikael Lenz Strube
[3]
Sara Skøtt Paulsen
[4]
Maike Wennekers Nielsen
[5]
Yannick Buijs
[6]
Erwin M Schoof
[7]
Thomas Ostenfeld Larsen
[8]
Lone Gram
[9]
Sheng-Da Zhang
journal
Marine drugs
year
2021
abstract
Genome mining of pigmented Pseudoalteromonas has revealed a large potential for the production of bioactive compounds and hydrolytic enzymes. The purpose of the present study was to explore this bioactivity potential in a potent antibiotic and enzyme producer, Pseudoalteromonas rubra strain S4059. Proteomic analyses (data are available via ProteomeXchange with identifier PXD023249) indicated that a highly efficient chitin degradation machinery was present in the red-pigmented P. rubra S4059 when grown on chitin. Four GH18 chitinases and two GH20 hexosaminidases were significantly upregulated under these conditions. GH19 chitinases, which are not common in bacteria, are consistently found in pigmented Pseudoalteromonas, and in S4059, GH19 was only detected when the bacterium was grown on chitin. To explore the possible role of GH19 in pigmented Pseudoalteromonas, we developed a protocol for genetic manipulation of S4059 and deleted the GH19 chitinase, and compared phenotypes of the mutant and wild type. However, none of the chitin degrading ability, secondary metabolite profile, or biofilm-forming capacity was affected by GH19 deletion. In conclusion, we developed a genetic manipulation protocol that can be used to unravel the bioactive potential of pigmented pseudoalteromonads. An efficient chitinolytic enzyme cocktail was identified in S4059, suggesting that this strain could be a candidate with industrial potential.
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To identify proteins with significantly different abundances when S4059 were grown on chitin compared to on mannose, the FDR were estimated using Benjamini–Hochberg method, and a two-tailed unpaired t-test was used with a combination of p-value ≤ 0.05 and Log2 fold-change ≥1.5 [51].
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To identify proteins with significantly different abundances when S4059 were grown on chitin compared to on mannose, the FDR were estimated using Benjamini–Hochberg method, and a two-tailed unpaired t-test was used with a combination of p-value ≤ 0.05 and Log2 fold-change ≥1.5 [51].
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Proteomic data are available via ProteomeXchange with identifier PXD023249 (http://www.proteomexchange.org/) and the genome of Pseudoalteromonas rubra S4059 is available at the National Center for Biotechnology Information (NCBI) under the accession number CP045429 (https://www.ncbi.nlm.nih.gov/nuccore/CP045429.1/ (accessed on 23 November 2020)) and CP045430 (https://www.ncbi.nlm.nih.gov/nuccore/CP045430.1/ (accessed on 23 November 2020)). Further inquiries can be directed to the corresponding author/s.
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Chitin degradation machinery and secondary metabolite profiles in the marine bacterium Pseudoalteromonas rubra S4059
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The chitinolytic machinery in Pseudoalteromonas rubra S4059 according to the prediction of the proteome from Uniprot (Proteome ID UP000305729). The signal peptide was predicted using amino acid sequence by SignalIP-5.0 (http://www.cbs.dtu.dk/services/SignalP/ (accessed on 22 September 2018)).
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To identify proteins with significantly different abundances when S4059 were grown on chitin compared to on mannose, the FDR were estimated using Benjamini–Hochberg method, and a two-tailed unpaired t-test was used with a combination of p-value ≤ 0.05 and Log2 fold-change ≥1.5 [51].
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