Proteomic investigation of the secretome of Cellvibrio japonicus during growth on chitin. Issue 13 (30th May 2016)
- Record Type:
- Journal Article
- Title:
- Proteomic investigation of the secretome of Cellvibrio japonicus during growth on chitin. Issue 13 (30th May 2016)
- Main Title:
- Proteomic investigation of the secretome of Cellvibrio japonicus during growth on chitin
- Authors:
- Tuveng, Tina Rise
Arntzen, Magnus Øverlie
Bengtsson, Oskar
Gardner, Jeffrey G.
Vaaje‐Kolstad, Gustav
Eijsink, Vincent G.H. - Abstract:
- Abstract : Studies of the secretomes of microbes grown on insoluble substrates are important for the discovery of novel proteins involved in biomass conversion. However, data in literature and this study indicate that secretome samples tend to be contaminated with cytoplasmic proteins. We have examined the secretome of the Gram‐negative soil bacterium Cellvibrio japonicus using a simple plate‐based culturing technique that yields samples with high fractions (60–75%) of proteins that are predicted to be secreted. By combining this approach with label‐free quantification using the MaxLFQ algorithm, we have mapped and quantified proteins secreted by C. japonicus during growth on α‐ and β‐chitin. Hierarchical clustering of the detected protein quantities revealed groups of up‐regulated proteins that include all five putative C. japonicus chitinases as well as a chitin‐specific lytic polysaccharide monooxygenase ( Cj LPMO10A). A small set of secreted proteins were co‐regulated with known chitin‐specific enzymes, including several with unknown catalytic functions. These proteins provide interesting targets for further studies aimed at unraveling the enzymatic machineries used by C. japonicus for recalcitrant polysaccharide degradation. Studies of chitin degradation indicated that C. japonicus indeed produces an efficient chitinolytic enzyme cocktail. All MS data have been deposited in the ProteomeXchange with the dataset identifier PXD002843Abstract : Studies of the secretomes of microbes grown on insoluble substrates are important for the discovery of novel proteins involved in biomass conversion. However, data in literature and this study indicate that secretome samples tend to be contaminated with cytoplasmic proteins. We have examined the secretome of the Gram‐negative soil bacterium Cellvibrio japonicus using a simple plate‐based culturing technique that yields samples with high fractions (60–75%) of proteins that are predicted to be secreted. By combining this approach with label‐free quantification using the MaxLFQ algorithm, we have mapped and quantified proteins secreted by C. japonicus during growth on α‐ and β‐chitin. Hierarchical clustering of the detected protein quantities revealed groups of up‐regulated proteins that include all five putative C. japonicus chitinases as well as a chitin‐specific lytic polysaccharide monooxygenase ( Cj LPMO10A). A small set of secreted proteins were co‐regulated with known chitin‐specific enzymes, including several with unknown catalytic functions. These proteins provide interesting targets for further studies aimed at unraveling the enzymatic machineries used by C. japonicus for recalcitrant polysaccharide degradation. Studies of chitin degradation indicated that C. japonicus indeed produces an efficient chitinolytic enzyme cocktail. All MS data have been deposited in the ProteomeXchange with the dataset identifier PXD002843 (http://proteomecentral.proteomexchange.org/dataset/PXD002843 ). … (more)
- Is Part Of:
- Proteomics. Volume 16:Issue 13(2016)
- Journal:
- Proteomics
- Issue:
- Volume 16:Issue 13(2016)
- Issue Display:
- Volume 16, Issue 13 (2016)
- Year:
- 2016
- Volume:
- 16
- Issue:
- 13
- Issue Sort Value:
- 2016-0016-0013-0000
- Page Start:
- 1904
- Page End:
- 1914
- Publication Date:
- 2016-05-30
- Subjects:
- Cellvibrio japonicus -- Chitin -- Chitinase -- Label‐free quantification -- Microbiology -- Secretome
Proteins -- Separation -- Periodicals
Bioinformatics -- Periodicals
Proteomics -- Periodicals
Genomes -- Periodicals
Molecular genetics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1615-9861 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/pmic.201500419 ↗
- Languages:
- English
- ISSNs:
- 1615-9853
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 2750.xml