Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii
Tubulin dimers of psychrophilic eukaryotes can polymerize into microtubules at 4°C, a temperature at which microtubules from mesophiles disassemble. This unique capability requires changes in the primary structure and/or in post-translational modifications of the tubulin subunits. To contribute to t...
Published in: | Proteins: Structure, Function, and Bioinformatics |
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ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/233883 2024-04-14T08:02:33+00:00 Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii Federica Chiappori Ivan Merelli Luciano Milanesi PUCCIARELLI, Sandra BALLARINI, Patrizia MICELI, Cristina Federica, Chiappori Pucciarelli, Sandra Ivan, Merelli Ballarini, Patrizia Miceli, Cristina Luciano, Milanesi 2012 STAMPA http://hdl.handle.net/11581/233883 https://doi.org/10.1002/prot.24016 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000300984700015 volume:80 issue:4 firstpage:1154 lastpage:1166 numberofpages:12 journal:PROTEINS http://hdl.handle.net/11581/233883 doi:10.1002/prot.24016 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84857794404 info:eu-repo/semantics/article 2012 ftuncamerinoiris https://doi.org/10.1002/prot.24016 2024-03-21T20:36:53Z Tubulin dimers of psychrophilic eukaryotes can polymerize into microtubules at 4°C, a temperature at which microtubules from mesophiles disassemble. This unique capability requires changes in the primary structure and/or in post-translational modifications of the tubulin subunits. To contribute to the understanding of mechanisms responsible for microtubule cold stability, here we present a computational structural analysis based on molecular dynamics (MD) and experimental data of three β-tubulin isotypes, named EFBT2, EFBT3, and EFBT4, from the Antarctic protozoon Euplotes focardii that optimal temperature for growth and reproduction is 4°C. In comparison to the β-tubulin from E. crassus, a mesophilic Euplotes species, EFBT2, EFBT3, and EFBT4 possess unique amino acid substitutions that confer different flexible properties of the polypeptide, as well as an increased hydrophobicity of the regions involved in microtubule interdimeric contacts that may overcome the microtubule destabilizing effect of cold temperatures. The structural analysis based on MD indicated that all isotypes display different flexibility properties in the regions involved in the formation of longitudinal and lateral contacts during microtubule polymerization. We also investigated the role of E. focardii β-tubulin isotypes during the process of cilia formation. The unique characteristics of the primary and tertiary structures of psychrophilic β-tubulin isotypes seem responsible for the formation of microtubules with distinct dynamic and functional properties. Article in Journal/Newspaper Antarc* Antarctic CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) Antarctic The Antarctic Proteins: Structure, Function, and Bioinformatics 80 4 1154 1166 |
institution |
Open Polar |
collection |
CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) |
op_collection_id |
ftuncamerinoiris |
language |
English |
description |
Tubulin dimers of psychrophilic eukaryotes can polymerize into microtubules at 4°C, a temperature at which microtubules from mesophiles disassemble. This unique capability requires changes in the primary structure and/or in post-translational modifications of the tubulin subunits. To contribute to the understanding of mechanisms responsible for microtubule cold stability, here we present a computational structural analysis based on molecular dynamics (MD) and experimental data of three β-tubulin isotypes, named EFBT2, EFBT3, and EFBT4, from the Antarctic protozoon Euplotes focardii that optimal temperature for growth and reproduction is 4°C. In comparison to the β-tubulin from E. crassus, a mesophilic Euplotes species, EFBT2, EFBT3, and EFBT4 possess unique amino acid substitutions that confer different flexible properties of the polypeptide, as well as an increased hydrophobicity of the regions involved in microtubule interdimeric contacts that may overcome the microtubule destabilizing effect of cold temperatures. The structural analysis based on MD indicated that all isotypes display different flexibility properties in the regions involved in the formation of longitudinal and lateral contacts during microtubule polymerization. We also investigated the role of E. focardii β-tubulin isotypes during the process of cilia formation. The unique characteristics of the primary and tertiary structures of psychrophilic β-tubulin isotypes seem responsible for the formation of microtubules with distinct dynamic and functional properties. |
author2 |
Federica, Chiappori Pucciarelli, Sandra Ivan, Merelli Ballarini, Patrizia Miceli, Cristina Luciano, Milanesi |
format |
Article in Journal/Newspaper |
author |
Federica Chiappori Ivan Merelli Luciano Milanesi PUCCIARELLI, Sandra BALLARINI, Patrizia MICELI, Cristina |
spellingShingle |
Federica Chiappori Ivan Merelli Luciano Milanesi PUCCIARELLI, Sandra BALLARINI, Patrizia MICELI, Cristina Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii |
author_facet |
Federica Chiappori Ivan Merelli Luciano Milanesi PUCCIARELLI, Sandra BALLARINI, Patrizia MICELI, Cristina |
author_sort |
Federica Chiappori |
title |
Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii |
title_short |
Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii |
title_full |
Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii |
title_fullStr |
Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii |
title_full_unstemmed |
Structural thermal adaptation of β-tubulins from the Antarctic psychrophilic protozoan Euplotes focardii |
title_sort |
structural thermal adaptation of β-tubulins from the antarctic psychrophilic protozoan euplotes focardii |
publishDate |
2012 |
url |
http://hdl.handle.net/11581/233883 https://doi.org/10.1002/prot.24016 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/wos/WOS:000300984700015 volume:80 issue:4 firstpage:1154 lastpage:1166 numberofpages:12 journal:PROTEINS http://hdl.handle.net/11581/233883 doi:10.1002/prot.24016 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84857794404 |
op_doi |
https://doi.org/10.1002/prot.24016 |
container_title |
Proteins: Structure, Function, and Bioinformatics |
container_volume |
80 |
container_issue |
4 |
container_start_page |
1154 |
op_container_end_page |
1166 |
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