Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology
Very little is known about the hydrophobic proteins of psychrophiles and their roles in cold adaptation. In light of this situation, methods were developed to analyse the hydrophobic proteome (HPP) of the model psychrophilic archaeon Methanococcoides burtonii. Central to this analysis was a novel di...
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ftdatacite:10.26190/unsworks/22949 2023-05-15T13:36:23+02:00 Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology Burg, Dominic William 2009 https://dx.doi.org/10.26190/unsworks/22949 http://hdl.handle.net/1959.4/44761 unknown UNSW Sydney https://creativecommons.org/licenses/by-nc-nd/3.0/au/ cc by-nc-nd 3.0 CC-BY-NC-ND Cold adaptation Hydrophobic proteome Proteomics Psychrophile Differential solubility iTRAQ Morphometry Dissertation thesis Thesis doctoral thesis 2009 ftdatacite https://doi.org/10.26190/unsworks/22949 2022-04-01T18:59:29Z Very little is known about the hydrophobic proteins of psychrophiles and their roles in cold adaptation. In light of this situation, methods were developed to analyse the hydrophobic proteome (HPP) of the model psychrophilic archaeon Methanococcoides burtonii. Central to this analysis was a novel differential solubility fractionation procedure, which resulted in a significant increase in the efficiency of resolving the HPP. Over 50% of the detected proteins were not identified in previous whole cell extract analyses, and these underwent an intensive manual annotation process producing high quality functional assignments. Utilising the functional assignments, biological context analysis of the HPP was performed, revealing novel and often unique biology. The analysis acted as a platform for differential proteomics of the organism s response to both temperature and substrate using stable isotope labelling. The results of which revealed that low temperature growth was associated with an increase in the abundance of surface and secreted proteins, and translation apparatus. Conversely, growth at a higher temperature was associated with an increase in the abundance of general protein folding machinery and indications of an oxidative stress response, emphasising that the temperature for maximum growth rate is stressful. Through investigation of the response of M. burtonii to substrate it was found that growth on methanol was stressful, and its low energy yield resulted in an increase in the abundance of energy conserving systems. The extracellular polymeric substance (EPS) and morphology of M. burtonii was also investigated with respect to both temperature and substrate, using a number of techniques in microscopy. It was found that the EPS was comprised of proteins, sugars and RNA, and that growth at different temperatures resulted in the production of EPS that displayed significantly different properties on dehydration, thus indicating compositional variation. When cells were grown on methanol they took on highly irregular shapes and had electron transparent inclusions. The observations from the ultrastructural analysis were contemplated with respect to the proteomic findings, revealing novel avenues of research. This study has highlighted the roles of hydrophobic proteins in cold adaptation biology, and the value of comprehensive proteomics for the examination of adaptation in microorganisms Doctoral or Postdoctoral Thesis Antarc* Antarctic DataCite Metadata Store (German National Library of Science and Technology) Antarctic The Antarctic |
institution |
Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
unknown |
topic |
Cold adaptation Hydrophobic proteome Proteomics Psychrophile Differential solubility iTRAQ Morphometry |
spellingShingle |
Cold adaptation Hydrophobic proteome Proteomics Psychrophile Differential solubility iTRAQ Morphometry Burg, Dominic William Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
topic_facet |
Cold adaptation Hydrophobic proteome Proteomics Psychrophile Differential solubility iTRAQ Morphometry |
description |
Very little is known about the hydrophobic proteins of psychrophiles and their roles in cold adaptation. In light of this situation, methods were developed to analyse the hydrophobic proteome (HPP) of the model psychrophilic archaeon Methanococcoides burtonii. Central to this analysis was a novel differential solubility fractionation procedure, which resulted in a significant increase in the efficiency of resolving the HPP. Over 50% of the detected proteins were not identified in previous whole cell extract analyses, and these underwent an intensive manual annotation process producing high quality functional assignments. Utilising the functional assignments, biological context analysis of the HPP was performed, revealing novel and often unique biology. The analysis acted as a platform for differential proteomics of the organism s response to both temperature and substrate using stable isotope labelling. The results of which revealed that low temperature growth was associated with an increase in the abundance of surface and secreted proteins, and translation apparatus. Conversely, growth at a higher temperature was associated with an increase in the abundance of general protein folding machinery and indications of an oxidative stress response, emphasising that the temperature for maximum growth rate is stressful. Through investigation of the response of M. burtonii to substrate it was found that growth on methanol was stressful, and its low energy yield resulted in an increase in the abundance of energy conserving systems. The extracellular polymeric substance (EPS) and morphology of M. burtonii was also investigated with respect to both temperature and substrate, using a number of techniques in microscopy. It was found that the EPS was comprised of proteins, sugars and RNA, and that growth at different temperatures resulted in the production of EPS that displayed significantly different properties on dehydration, thus indicating compositional variation. When cells were grown on methanol they took on highly irregular shapes and had electron transparent inclusions. The observations from the ultrastructural analysis were contemplated with respect to the proteomic findings, revealing novel avenues of research. This study has highlighted the roles of hydrophobic proteins in cold adaptation biology, and the value of comprehensive proteomics for the examination of adaptation in microorganisms |
format |
Doctoral or Postdoctoral Thesis |
author |
Burg, Dominic William |
author_facet |
Burg, Dominic William |
author_sort |
Burg, Dominic William |
title |
Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
title_short |
Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
title_full |
Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
title_fullStr |
Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
title_full_unstemmed |
Cold adaptation in the Antarctic archeaon Methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
title_sort |
cold adaptation in the antarctic archeaon methanococcoides burtonii: the role of the hydrophobic proteome and variations in cellular morphology |
publisher |
UNSW Sydney |
publishDate |
2009 |
url |
https://dx.doi.org/10.26190/unsworks/22949 http://hdl.handle.net/1959.4/44761 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_rights |
https://creativecommons.org/licenses/by-nc-nd/3.0/au/ cc by-nc-nd 3.0 |
op_rightsnorm |
CC-BY-NC-ND |
op_doi |
https://doi.org/10.26190/unsworks/22949 |
_version_ |
1766077961929228288 |