Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium
Antifreeze proteins or ice-binding proteins (IBPs) facilitate the survival of certain cellular organisms in freezing environment by inhibiting the growth of ice crystals in solution. Present study identifies orthologs of the IBP of Colwellia sp. SLW05 , which were obtained from a wide range of taxa....
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ftdatacite:10.6084/m9.figshare.1162508.v1 2023-05-15T13:49:30+02:00 Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium Rachana Banerjee Pratim Chakraborti Bhowmick, Rupa Subhasish Mukhopadhyay 2015 https://dx.doi.org/10.6084/m9.figshare.1162508.v1 https://tandf.figshare.com/articles/journal_contribution/Distinct_molecular_features_facilitating_ice_binding_mechanisms_in_hyperactive_antifreeze_proteins_closely_related_to_an_Antarctic_sea_ice_bacterium/1162508/1 unknown Taylor & Francis https://dx.doi.org/10.1080/07391102.2014.952665 https://dx.doi.org/10.6084/m9.figshare.1162508 Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 CC-BY 60506 Virology FOS Biological sciences 110309 Infectious Diseases FOS Health sciences Developmental Biology Biological Sciences Immunology FOS Clinical medicine Chemistry Earth and Environmental Sciences Evolutionary Biology Genetics Cell Biology Microbiology Medicine Biochemistry Biophysics Text article-journal Journal contribution ScholarlyArticle 2015 ftdatacite https://doi.org/10.6084/m9.figshare.1162508.v1 https://doi.org/10.1080/07391102.2014.952665 https://doi.org/10.6084/m9.figshare.1162508 2021-11-05T12:55:41Z Antifreeze proteins or ice-binding proteins (IBPs) facilitate the survival of certain cellular organisms in freezing environment by inhibiting the growth of ice crystals in solution. Present study identifies orthologs of the IBP of Colwellia sp. SLW05 , which were obtained from a wide range of taxa. Phylogenetic analysis on the basis of conserved regions (predicted as the ‘ice-binding domain’ [IBD]) present in all the orthologs, separates the bacterial and archaeal orthologs from that of the eukaryotes’. Correspondence analysis pointed out that the bacterial and archaeal IBDs have relatively higher average hydrophobicity than the eukaryotic members. IBDs belonging to bacterial as well as archaeal AFPs contain comparatively more strands, and therefore are revealed to be under higher evolutionary selection pressure. Molecular docking studies prove that the ice crystals form more stable complex with the bacterial as well as archaeal proteins than the eukaryotic orthologs. Analysis of the docked structures have traced out the ice-binding sites (IBSs) in all the orthologs which continue to facilitate ice-binding activity even after getting mutated with respect to the well-studied IBSs of Typhula ishikariensis and notably, all these mutations performing ice-binding using ‘anchored clathrate mechanism’ have been found to prefer polar and hydrophilic amino acids. Horizontal gene transfer studies point toward a strong selection pressure favoring independent evolution of the IBPs in some polar organisms including prokaryotes as well as eukaryotes because these proteins facilitate the polar organisms to acclimatize to the adversities in their niche, thus safeguarding their existence. Text Antarc* Antarctic Sea ice DataCite Metadata Store (German National Library of Science and Technology) Antarctic |
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Open Polar |
collection |
DataCite Metadata Store (German National Library of Science and Technology) |
op_collection_id |
ftdatacite |
language |
unknown |
topic |
60506 Virology FOS Biological sciences 110309 Infectious Diseases FOS Health sciences Developmental Biology Biological Sciences Immunology FOS Clinical medicine Chemistry Earth and Environmental Sciences Evolutionary Biology Genetics Cell Biology Microbiology Medicine Biochemistry Biophysics |
spellingShingle |
60506 Virology FOS Biological sciences 110309 Infectious Diseases FOS Health sciences Developmental Biology Biological Sciences Immunology FOS Clinical medicine Chemistry Earth and Environmental Sciences Evolutionary Biology Genetics Cell Biology Microbiology Medicine Biochemistry Biophysics Rachana Banerjee Pratim Chakraborti Bhowmick, Rupa Subhasish Mukhopadhyay Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium |
topic_facet |
60506 Virology FOS Biological sciences 110309 Infectious Diseases FOS Health sciences Developmental Biology Biological Sciences Immunology FOS Clinical medicine Chemistry Earth and Environmental Sciences Evolutionary Biology Genetics Cell Biology Microbiology Medicine Biochemistry Biophysics |
description |
Antifreeze proteins or ice-binding proteins (IBPs) facilitate the survival of certain cellular organisms in freezing environment by inhibiting the growth of ice crystals in solution. Present study identifies orthologs of the IBP of Colwellia sp. SLW05 , which were obtained from a wide range of taxa. Phylogenetic analysis on the basis of conserved regions (predicted as the ‘ice-binding domain’ [IBD]) present in all the orthologs, separates the bacterial and archaeal orthologs from that of the eukaryotes’. Correspondence analysis pointed out that the bacterial and archaeal IBDs have relatively higher average hydrophobicity than the eukaryotic members. IBDs belonging to bacterial as well as archaeal AFPs contain comparatively more strands, and therefore are revealed to be under higher evolutionary selection pressure. Molecular docking studies prove that the ice crystals form more stable complex with the bacterial as well as archaeal proteins than the eukaryotic orthologs. Analysis of the docked structures have traced out the ice-binding sites (IBSs) in all the orthologs which continue to facilitate ice-binding activity even after getting mutated with respect to the well-studied IBSs of Typhula ishikariensis and notably, all these mutations performing ice-binding using ‘anchored clathrate mechanism’ have been found to prefer polar and hydrophilic amino acids. Horizontal gene transfer studies point toward a strong selection pressure favoring independent evolution of the IBPs in some polar organisms including prokaryotes as well as eukaryotes because these proteins facilitate the polar organisms to acclimatize to the adversities in their niche, thus safeguarding their existence. |
format |
Text |
author |
Rachana Banerjee Pratim Chakraborti Bhowmick, Rupa Subhasish Mukhopadhyay |
author_facet |
Rachana Banerjee Pratim Chakraborti Bhowmick, Rupa Subhasish Mukhopadhyay |
author_sort |
Rachana Banerjee |
title |
Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium |
title_short |
Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium |
title_full |
Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium |
title_fullStr |
Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium |
title_full_unstemmed |
Distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an Antarctic sea ice bacterium |
title_sort |
distinct molecular features facilitating ice-binding mechanisms in hyperactive antifreeze proteins closely related to an antarctic sea ice bacterium |
publisher |
Taylor & Francis |
publishDate |
2015 |
url |
https://dx.doi.org/10.6084/m9.figshare.1162508.v1 https://tandf.figshare.com/articles/journal_contribution/Distinct_molecular_features_facilitating_ice_binding_mechanisms_in_hyperactive_antifreeze_proteins_closely_related_to_an_Antarctic_sea_ice_bacterium/1162508/1 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic Sea ice |
genre_facet |
Antarc* Antarctic Sea ice |
op_relation |
https://dx.doi.org/10.1080/07391102.2014.952665 https://dx.doi.org/10.6084/m9.figshare.1162508 |
op_rights |
Creative Commons Attribution 4.0 International https://creativecommons.org/licenses/by/4.0/legalcode cc-by-4.0 |
op_rightsnorm |
CC-BY |
op_doi |
https://doi.org/10.6084/m9.figshare.1162508.v1 https://doi.org/10.1080/07391102.2014.952665 https://doi.org/10.6084/m9.figshare.1162508 |
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