Comparative proteomics of Mn(II)‐oxidizing and non‐oxidizing Roseobacter clade bacteria reveal an operative manganese transport system but minimal Mn(II)‐induced expression of manganese oxidation and antioxidant enzymes. Issue 5 (5th May 2014)
- Record Type:
- Journal Article
- Title:
- Comparative proteomics of Mn(II)‐oxidizing and non‐oxidizing Roseobacter clade bacteria reveal an operative manganese transport system but minimal Mn(II)‐induced expression of manganese oxidation and antioxidant enzymes. Issue 5 (5th May 2014)
- Main Title:
- Comparative proteomics of Mn(II)‐oxidizing and non‐oxidizing Roseobacter clade bacteria reveal an operative manganese transport system but minimal Mn(II)‐induced expression of manganese oxidation and antioxidant enzymes
- Authors:
- Learman, D. R.
Hansel, C. M. - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>Manganese (Mn) is an essential nutrient and precipitates as minerals with technological and environmental relevance. To gain a proteomic understanding of how bacteria respond to Mn(II) and its connection to oxidation, a comparative examination of the proteomic response of Mn(II)‐oxidizing (<italic>R</italic><italic>oseobacter</italic> sp. AzwK‐3b) and non‐oxidizing (<italic>R</italic><italic>uegeria</italic> sp. TM1040) alphaproteobacteria was conducted. Both bacteria show an operative Mn(II) transport system. In the absence of Mn(II), both bacteria have higher expression of proteins that were homologous to SitA and SitB, known proteins in the Mn(II) transport system of other alphaproteobacteria. Overall, each bacterium demonstrated a varied response to Mn(II). <italic>R</italic><italic>u</italic>. TM1040 had a greater number of proteins differentially expressed in response to Mn(II) and also had a group of proteins related to chemotaxis at higher concentrations of Mn(II), suggesting a potential stress response. While both bacteria are able to generate extracellular superoxide and Mn(II) is a known antioxidant, the presence of Mn(II) did not significantly alter the expression of proteins related to antioxidant activity. Heme peroxidases, previously connected to Mn(II) oxidation, were found in the soluble protein extract of <italic>R</italic>. AzwK‐3b, but only minor differential expression was observed as a function<abstract abstract-type="main"> <title>Summary</title> <p>Manganese (Mn) is an essential nutrient and precipitates as minerals with technological and environmental relevance. To gain a proteomic understanding of how bacteria respond to Mn(II) and its connection to oxidation, a comparative examination of the proteomic response of Mn(II)‐oxidizing (<italic>R</italic><italic>oseobacter</italic> sp. AzwK‐3b) and non‐oxidizing (<italic>R</italic><italic>uegeria</italic> sp. TM1040) alphaproteobacteria was conducted. Both bacteria show an operative Mn(II) transport system. In the absence of Mn(II), both bacteria have higher expression of proteins that were homologous to SitA and SitB, known proteins in the Mn(II) transport system of other alphaproteobacteria. Overall, each bacterium demonstrated a varied response to Mn(II). <italic>R</italic><italic>u</italic>. TM1040 had a greater number of proteins differentially expressed in response to Mn(II) and also had a group of proteins related to chemotaxis at higher concentrations of Mn(II), suggesting a potential stress response. While both bacteria are able to generate extracellular superoxide and Mn(II) is a known antioxidant, the presence of Mn(II) did not significantly alter the expression of proteins related to antioxidant activity. Heme peroxidases, previously connected to Mn(II) oxidation, were found in the soluble protein extract of <italic>R</italic>. AzwK‐3b, but only minor differential expression was observed as a function of Mn(II), indicating that their expression was not induced by Mn(II).</p> </abstract> … (more)
- Is Part Of:
- Environmental microbiology reports. Volume 6:Issue 5(2014)
- Journal:
- Environmental microbiology reports
- Issue:
- Volume 6:Issue 5(2014)
- Issue Display:
- Volume 6, Issue 5 (2014)
- Year:
- 2014
- Volume:
- 6
- Issue:
- 5
- Issue Sort Value:
- 2014-0006-0005-0000
- Page Start:
- 501
- Page End:
- 509
- Publication Date:
- 2014-05-05
- Subjects:
- Microbial ecology -- Periodicals
Environmental Microbiology -- Periodicals
Electronic journals
579.17 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1758-2229 ↗
http://www3.interscience.wiley.com/journal/121641579/home ↗
https://onlinelibrary.wiley.com/journal/17582229#pane-01cbe741-499a-4611-874e-1061f1f4679e01 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/1758-2229.12164 ↗
- Languages:
- English
- ISSNs:
- 1758-2229
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3791.522650
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3573.xml