Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii.
Molecular adaptation at low temperature requires specificities represented mainly by modifications in the gene sequence and consequently in the protein primary structure. To characterize the molecular mechanisms responsible for ribosome cold-adaptation, we compared the ribosomal P0 and P2 genes from...
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ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/107390 2024-04-14T08:04:39+00:00 Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. PUCCIARELLI, Sandra BARCHETTA, Sabrina MICELI, Cristina MARZIALE F DI GIUSEPPE G Pucciarelli, Sandra Marziale, F DI GIUSEPPE, G Barchetta, Sabrina Miceli, Cristina 2006 http://hdl.handle.net/11581/107390 https://doi.org/10.1016/j.gene.2005.06.007 eng eng info:eu-repo/semantics/altIdentifier/wos/WOS:000233058400003 volume:360(2) issue:2 firstpage:103 lastpage:110 numberofpages:8 journal:GENE http://hdl.handle.net/11581/107390 doi:10.1016/j.gene.2005.06.007 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-26844555780 info:eu-repo/semantics/article 2006 ftuncamerinoiris https://doi.org/10.1016/j.gene.2005.06.007 2024-03-21T20:36:40Z Molecular adaptation at low temperature requires specificities represented mainly by modifications in the gene sequence and consequently in the protein primary structure. To characterize the molecular mechanisms responsible for ribosome cold-adaptation, we compared the ribosomal P0 and P2 genes from the Antarctic ciliate Euplotes focardii with homologous genes from mesophilic organisms, including the ciliates Tetrahymena thermophila and non cold-adapted Euplotes species. This analysis revealed the presence of non synonymous mutations unique to E. focardii. In the P0 protein the mutations produced amino acid substitutions that increased the molecular flexibility that may facilitate a conformational adjustment associated with the interaction with the GTPase center of the large subunit rRNA, and increased the hydrophobicity of the region involved in the interaction with P1/P2 heterodimer, probably to keep associated the ribosomal stalk in the cold. In the P2 protein the mutations produced amino acid substitutions that increased the N-terminus flexibility, which may facilitate interactions with P1 protein in the formation of the heterodimer, and reduced the mobility of the C-terminus, to stabilize the stalk during ribosomal activity. Finally, P proteins appeared to be valid markers for investigating the phylogenetic origin of early eukaryotes. Article in Journal/Newspaper Antarc* Antarctic CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) Antarctic The Antarctic Gene 360 2 103 110 |
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Open Polar |
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CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) |
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ftuncamerinoiris |
language |
English |
description |
Molecular adaptation at low temperature requires specificities represented mainly by modifications in the gene sequence and consequently in the protein primary structure. To characterize the molecular mechanisms responsible for ribosome cold-adaptation, we compared the ribosomal P0 and P2 genes from the Antarctic ciliate Euplotes focardii with homologous genes from mesophilic organisms, including the ciliates Tetrahymena thermophila and non cold-adapted Euplotes species. This analysis revealed the presence of non synonymous mutations unique to E. focardii. In the P0 protein the mutations produced amino acid substitutions that increased the molecular flexibility that may facilitate a conformational adjustment associated with the interaction with the GTPase center of the large subunit rRNA, and increased the hydrophobicity of the region involved in the interaction with P1/P2 heterodimer, probably to keep associated the ribosomal stalk in the cold. In the P2 protein the mutations produced amino acid substitutions that increased the N-terminus flexibility, which may facilitate interactions with P1 protein in the formation of the heterodimer, and reduced the mobility of the C-terminus, to stabilize the stalk during ribosomal activity. Finally, P proteins appeared to be valid markers for investigating the phylogenetic origin of early eukaryotes. |
author2 |
Pucciarelli, Sandra Marziale, F DI GIUSEPPE, G Barchetta, Sabrina Miceli, Cristina |
format |
Article in Journal/Newspaper |
author |
PUCCIARELLI, Sandra BARCHETTA, Sabrina MICELI, Cristina MARZIALE F DI GIUSEPPE G |
spellingShingle |
PUCCIARELLI, Sandra BARCHETTA, Sabrina MICELI, Cristina MARZIALE F DI GIUSEPPE G Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. |
author_facet |
PUCCIARELLI, Sandra BARCHETTA, Sabrina MICELI, Cristina MARZIALE F DI GIUSEPPE G |
author_sort |
PUCCIARELLI, Sandra |
title |
Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. |
title_short |
Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. |
title_full |
Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. |
title_fullStr |
Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. |
title_full_unstemmed |
Ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal P0 and P2 proteins from the Antarctic ciliate Euplotes focardii. |
title_sort |
ribosomal cold-adaptation: characterization of the genes encoding the acidic ribosomal p0 and p2 proteins from the antarctic ciliate euplotes focardii. |
publishDate |
2006 |
url |
http://hdl.handle.net/11581/107390 https://doi.org/10.1016/j.gene.2005.06.007 |
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:000233058400003 volume:360(2) issue:2 firstpage:103 lastpage:110 numberofpages:8 journal:GENE http://hdl.handle.net/11581/107390 doi:10.1016/j.gene.2005.06.007 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-26844555780 |
op_doi |
https://doi.org/10.1016/j.gene.2005.06.007 |
container_title |
Gene |
container_volume |
360 |
container_issue |
2 |
container_start_page |
103 |
op_container_end_page |
110 |
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1796301333493448704 |