Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae)
Antifreeze proteins (AFPs) provide protection for organisms subjected to the presence of ice crystals. The psychrophilic diatom Fragilariopsis cylindrus which is frequently found in polar sea ice carries a multitude of AFP isoforms. In this study we report the heterologous expression of two antifree...
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ftpangaea:oai:pangaea.de:doi:10.1594/PANGAEA.804854 2023-05-15T18:18:29+02:00 Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) Uhlig, Christiane Kabisch, Johannes Palm, Gottfried J Valentin, Klaus Schweder, Thomas Krell, Andreas 2011-01-08 application/zip, 2 datasets https://doi.pangaea.de/10.1594/PANGAEA.804854 https://doi.org/10.1594/PANGAEA.804854 en eng PANGAEA https://doi.pangaea.de/10.1594/PANGAEA.804854 https://doi.org/10.1594/PANGAEA.804854 CC-BY-3.0: Creative Commons Attribution 3.0 Unported Access constraints: unrestricted info:eu-repo/semantics/openAccess CC-BY Supplement to: Uhlig, Christiane; Kabisch, Johannes; Palm, Gottfried J; Valentin, Klaus; Schweder, Thomas; Krell, Andreas (2011): Heterologous expression, refolding and functional characterization of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae). Cryobiology, 63(3), 220-228, https://doi.org/10.1016/j.cryobiol.2011.08.005 Dataset 2011 ftpangaea https://doi.org/10.1594/PANGAEA.804854 https://doi.org/10.1016/j.cryobiol.2011.08.005 2023-01-20T07:32:50Z Antifreeze proteins (AFPs) provide protection for organisms subjected to the presence of ice crystals. The psychrophilic diatom Fragilariopsis cylindrus which is frequently found in polar sea ice carries a multitude of AFP isoforms. In this study we report the heterologous expression of two antifreeze protein isoforms from F. cylindrus in Escherichia coli. Refolding from inclusion bodies produced proteins functionally active with respect to crystal deformation, recrystallization inhibition and thermal hysteresis. We observed a reduction of activity in the presence of the pelB leader peptide in comparison with the GS-linked SUMO-tag. Activity was positively correlated to protein concentration and buffer salinity. Thermal hysteresis and crystal deformation habit suggest the affiliation of the proteins to the hyperactive group of AFPs. One isoform, carrying a signal peptide for secretion, produced a thermal hysteresis up to 1.53 °C ± 0.53 °C and ice crystals of hexagonal bipyramidal shape. The second isoform, which has a long preceding N-terminal sequence of unknown function, produced thermal hysteresis of up to 2.34 °C ± 0.25 °C. Ice crystals grew in form of a hexagonal column in presence of this protein. The different sequences preceding the ice binding domain point to distinct localizations of the proteins inside or outside the cell. We thus propose that AFPs have different functions in vivo, also reflected in their specific TH capability. Dataset Sea ice PANGAEA - Data Publisher for Earth & Environmental Science |
institution |
Open Polar |
collection |
PANGAEA - Data Publisher for Earth & Environmental Science |
op_collection_id |
ftpangaea |
language |
English |
description |
Antifreeze proteins (AFPs) provide protection for organisms subjected to the presence of ice crystals. The psychrophilic diatom Fragilariopsis cylindrus which is frequently found in polar sea ice carries a multitude of AFP isoforms. In this study we report the heterologous expression of two antifreeze protein isoforms from F. cylindrus in Escherichia coli. Refolding from inclusion bodies produced proteins functionally active with respect to crystal deformation, recrystallization inhibition and thermal hysteresis. We observed a reduction of activity in the presence of the pelB leader peptide in comparison with the GS-linked SUMO-tag. Activity was positively correlated to protein concentration and buffer salinity. Thermal hysteresis and crystal deformation habit suggest the affiliation of the proteins to the hyperactive group of AFPs. One isoform, carrying a signal peptide for secretion, produced a thermal hysteresis up to 1.53 °C ± 0.53 °C and ice crystals of hexagonal bipyramidal shape. The second isoform, which has a long preceding N-terminal sequence of unknown function, produced thermal hysteresis of up to 2.34 °C ± 0.25 °C. Ice crystals grew in form of a hexagonal column in presence of this protein. The different sequences preceding the ice binding domain point to distinct localizations of the proteins inside or outside the cell. We thus propose that AFPs have different functions in vivo, also reflected in their specific TH capability. |
format |
Dataset |
author |
Uhlig, Christiane Kabisch, Johannes Palm, Gottfried J Valentin, Klaus Schweder, Thomas Krell, Andreas |
spellingShingle |
Uhlig, Christiane Kabisch, Johannes Palm, Gottfried J Valentin, Klaus Schweder, Thomas Krell, Andreas Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) |
author_facet |
Uhlig, Christiane Kabisch, Johannes Palm, Gottfried J Valentin, Klaus Schweder, Thomas Krell, Andreas |
author_sort |
Uhlig, Christiane |
title |
Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) |
title_short |
Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) |
title_full |
Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) |
title_fullStr |
Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) |
title_full_unstemmed |
Thermal hysteresis of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae) |
title_sort |
thermal hysteresis of two antifreeze proteins from fragilariopsis cylindrus (bacillariophyceae) |
publisher |
PANGAEA |
publishDate |
2011 |
url |
https://doi.pangaea.de/10.1594/PANGAEA.804854 https://doi.org/10.1594/PANGAEA.804854 |
genre |
Sea ice |
genre_facet |
Sea ice |
op_source |
Supplement to: Uhlig, Christiane; Kabisch, Johannes; Palm, Gottfried J; Valentin, Klaus; Schweder, Thomas; Krell, Andreas (2011): Heterologous expression, refolding and functional characterization of two antifreeze proteins from Fragilariopsis cylindrus (Bacillariophyceae). Cryobiology, 63(3), 220-228, https://doi.org/10.1016/j.cryobiol.2011.08.005 |
op_relation |
https://doi.pangaea.de/10.1594/PANGAEA.804854 https://doi.org/10.1594/PANGAEA.804854 |
op_rights |
CC-BY-3.0: Creative Commons Attribution 3.0 Unported Access constraints: unrestricted info:eu-repo/semantics/openAccess |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.1594/PANGAEA.804854 https://doi.org/10.1016/j.cryobiol.2011.08.005 |
_version_ |
1766195074157248512 |