Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii
Cell type-specific signal proteins, known as pheromones, are synthesized by ciliated protozoa in association with their self/nonself mating-type systems, and are utilized to control the vegetative growth and mating stages of their life cycle. In species of the most ubiquitous ciliate, Euplotes, thes...
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Online Access: | http://hdl.handle.net/11581/116083 https://doi.org/10.1080/15216540701258165 |
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ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/116083 2024-09-15T17:43:47+00:00 Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii PLACZEK WJ ETEZADY ESFARJANI T HERRMANN T PEDRINI B PETI W WUETHRICH K. ALIMENTI, Claudio LUPORINI, Pierangelo Placzek, Wj ETEZADY ESFARJANI, T Herrmann, T Pedrini, B Peti, W Alimenti, Claudio Luporini, Pierangelo Wuethrich, K. 2007 http://hdl.handle.net/11581/116083 https://doi.org/10.1080/15216540701258165 eng eng volume:59 issue:8-9 firstpage:578 lastpage:585 numberofpages:8 journal:IUBMB LIFE http://hdl.handle.net/11581/116083 doi:10.1080/15216540701258165 info:eu-repo/semantics/article 2007 ftuncamerinoiris https://doi.org/10.1080/15216540701258165 2024-06-24T23:58:56Z Cell type-specific signal proteins, known as pheromones, are synthesized by ciliated protozoa in association with their self/nonself mating-type systems, and are utilized to control the vegetative growth and mating stages of their life cycle. In species of the most ubiquitous ciliate, Euplotes, these pheromones form families of structurally homologous molecules, which are constitutively secreted into the extracellular environment, from where they can be isolated in sufficient amounts for chemical characterization. This paper describes the NMR structures of En-1 and En-2, which are members of the cold-adapted pheromone family produced by Euplotes nobilii, a species inhabiting the freezing coastal waters of Antarctica. The structures were determined with the proteins from the natural source, using homonuclear 1H NMR techniques in combination with automated NOESY peak picking and NOE assignment. En-1 and En-2 have highly homologous global folds, which consist of a central three-a-helix bundle with an up-down-up topology and a 310-helical turn near the N-terminus. This fold is stabilized by four disulfide bonds and the helices are connected by bulging loops. Apparent structural specificity resides in the variable C-terminal regions of the pheromones.TheNMRstructures ofEn-1 and En-2 provide novel insights into the cold-adaptive modifications that distinguish the E. nobilii pheromone family from the closely related E. raikovi pheromone family isolated from temperate waters. Article in Journal/Newspaper Antarc* Antarctic Antarctica CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) IUBMB Life 59 8 578 585 |
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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 |
Cell type-specific signal proteins, known as pheromones, are synthesized by ciliated protozoa in association with their self/nonself mating-type systems, and are utilized to control the vegetative growth and mating stages of their life cycle. In species of the most ubiquitous ciliate, Euplotes, these pheromones form families of structurally homologous molecules, which are constitutively secreted into the extracellular environment, from where they can be isolated in sufficient amounts for chemical characterization. This paper describes the NMR structures of En-1 and En-2, which are members of the cold-adapted pheromone family produced by Euplotes nobilii, a species inhabiting the freezing coastal waters of Antarctica. The structures were determined with the proteins from the natural source, using homonuclear 1H NMR techniques in combination with automated NOESY peak picking and NOE assignment. En-1 and En-2 have highly homologous global folds, which consist of a central three-a-helix bundle with an up-down-up topology and a 310-helical turn near the N-terminus. This fold is stabilized by four disulfide bonds and the helices are connected by bulging loops. Apparent structural specificity resides in the variable C-terminal regions of the pheromones.TheNMRstructures ofEn-1 and En-2 provide novel insights into the cold-adaptive modifications that distinguish the E. nobilii pheromone family from the closely related E. raikovi pheromone family isolated from temperate waters. |
author2 |
Placzek, Wj ETEZADY ESFARJANI, T Herrmann, T Pedrini, B Peti, W Alimenti, Claudio Luporini, Pierangelo Wuethrich, K. |
format |
Article in Journal/Newspaper |
author |
PLACZEK WJ ETEZADY ESFARJANI T HERRMANN T PEDRINI B PETI W WUETHRICH K. ALIMENTI, Claudio LUPORINI, Pierangelo |
spellingShingle |
PLACZEK WJ ETEZADY ESFARJANI T HERRMANN T PEDRINI B PETI W WUETHRICH K. ALIMENTI, Claudio LUPORINI, Pierangelo Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii |
author_facet |
PLACZEK WJ ETEZADY ESFARJANI T HERRMANN T PEDRINI B PETI W WUETHRICH K. ALIMENTI, Claudio LUPORINI, Pierangelo |
author_sort |
PLACZEK WJ |
title |
Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii |
title_short |
Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii |
title_full |
Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii |
title_fullStr |
Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii |
title_full_unstemmed |
Cold-Adapted Signal Proteins: NMR Structures of Pheromones from the Antarctic Ciliate Euplotes nobilii |
title_sort |
cold-adapted signal proteins: nmr structures of pheromones from the antarctic ciliate euplotes nobilii |
publishDate |
2007 |
url |
http://hdl.handle.net/11581/116083 https://doi.org/10.1080/15216540701258165 |
genre |
Antarc* Antarctic Antarctica |
genre_facet |
Antarc* Antarctic Antarctica |
op_relation |
volume:59 issue:8-9 firstpage:578 lastpage:585 numberofpages:8 journal:IUBMB LIFE http://hdl.handle.net/11581/116083 doi:10.1080/15216540701258165 |
op_doi |
https://doi.org/10.1080/15216540701258165 |
container_title |
IUBMB Life |
container_volume |
59 |
container_issue |
8 |
container_start_page |
578 |
op_container_end_page |
585 |
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1810490953755000832 |