Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes
Abstract Unique opportunities are provided by phylogenetically closely related organisms thriving in stably cold, or temperate milieus to study adaptive modifications of structurally homologous molecules. These modifications are of keen interest in basic science as well as in biotechnology. This rev...
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crwiley:10.1002/iub.228 2024-06-23T07:47:56+00:00 Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes Alimenti, Claudio Vallesi, Adriana Pedrini, Bill Wüthrich, Kurt Luporini, Pierangelo 2009 http://dx.doi.org/10.1002/iub.228 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fiub.228 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/iub.228 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor IUBMB Life volume 61, issue 8, page 838-845 ISSN 1521-6543 1521-6551 journal-article 2009 crwiley https://doi.org/10.1002/iub.228 2024-06-13T04:22:03Z Abstract Unique opportunities are provided by phylogenetically closely related organisms thriving in stably cold, or temperate milieus to study adaptive modifications of structurally homologous molecules. These modifications are of keen interest in basic science as well as in biotechnology. This review highlights structural and functional specificities that differentiate two homologous families of psychrophilic and mesophilic water‐borne proteins (designated as pheromones) that signal mitotic growth and sexual mating in two marine species of the protozoan ciliate Euplotes , i.e., E. nobilii , which is distributed in Antarctic and Arctic waters, and E. raikovi , which inhabits temperate waters. The two protein families show strict conservation of a common three‐helix bundle in a compact core of the molecular structure, which provides long‐lasting integrity and biological activity to these molecules in their natural environment. In the psychrophilic pheromone family, cold‐adaptation appears to have been achieved by superimposing an integrated complex of structural modifications on this conserved scaffold. Functionally most relevant appear to be extensions of polypeptide segments devoid of regular secondary structures, a specific distribution of polar and hydrophobic amino acids, the presence of solvent‐exposed clusters of negatively charged amino acid side chains, and a unique role of aromatic residues in anchoring the molecular architecture. Due to these modifications, the psychrophilic pheromones are an example of an elegant combination of high stability of the three‐dimensional structures with sufficient structural plasticity for efficient functioning at their physiologically low temperatures. © 2009 IUBMB IUBMB Life 61(8): 838–845, 2009 Article in Journal/Newspaper Antarc* Antarctic Arctic Wiley Online Library Antarctic Arctic IUBMB Life 61 8 838 845 |
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Wiley Online Library |
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English |
description |
Abstract Unique opportunities are provided by phylogenetically closely related organisms thriving in stably cold, or temperate milieus to study adaptive modifications of structurally homologous molecules. These modifications are of keen interest in basic science as well as in biotechnology. This review highlights structural and functional specificities that differentiate two homologous families of psychrophilic and mesophilic water‐borne proteins (designated as pheromones) that signal mitotic growth and sexual mating in two marine species of the protozoan ciliate Euplotes , i.e., E. nobilii , which is distributed in Antarctic and Arctic waters, and E. raikovi , which inhabits temperate waters. The two protein families show strict conservation of a common three‐helix bundle in a compact core of the molecular structure, which provides long‐lasting integrity and biological activity to these molecules in their natural environment. In the psychrophilic pheromone family, cold‐adaptation appears to have been achieved by superimposing an integrated complex of structural modifications on this conserved scaffold. Functionally most relevant appear to be extensions of polypeptide segments devoid of regular secondary structures, a specific distribution of polar and hydrophobic amino acids, the presence of solvent‐exposed clusters of negatively charged amino acid side chains, and a unique role of aromatic residues in anchoring the molecular architecture. Due to these modifications, the psychrophilic pheromones are an example of an elegant combination of high stability of the three‐dimensional structures with sufficient structural plasticity for efficient functioning at their physiologically low temperatures. © 2009 IUBMB IUBMB Life 61(8): 838–845, 2009 |
format |
Article in Journal/Newspaper |
author |
Alimenti, Claudio Vallesi, Adriana Pedrini, Bill Wüthrich, Kurt Luporini, Pierangelo |
spellingShingle |
Alimenti, Claudio Vallesi, Adriana Pedrini, Bill Wüthrich, Kurt Luporini, Pierangelo Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes |
author_facet |
Alimenti, Claudio Vallesi, Adriana Pedrini, Bill Wüthrich, Kurt Luporini, Pierangelo |
author_sort |
Alimenti, Claudio |
title |
Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes |
title_short |
Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes |
title_full |
Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes |
title_fullStr |
Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes |
title_full_unstemmed |
Molecular cold‐adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes |
title_sort |
molecular cold‐adaptation: comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, euplotes |
publisher |
Wiley |
publishDate |
2009 |
url |
http://dx.doi.org/10.1002/iub.228 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fiub.228 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/iub.228 |
geographic |
Antarctic Arctic |
geographic_facet |
Antarctic Arctic |
genre |
Antarc* Antarctic Arctic |
genre_facet |
Antarc* Antarctic Arctic |
op_source |
IUBMB Life volume 61, issue 8, page 838-845 ISSN 1521-6543 1521-6551 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/iub.228 |
container_title |
IUBMB Life |
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61 |
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8 |
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838 |
op_container_end_page |
845 |
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1802638232122294272 |