Cold‐adapted signal proteins: NMR structures of pheromones from the antarctic ciliate Euplotes nobilii

Abstract 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, Euplo...

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Published in:IUBMB Life
Main Authors: Placzek, William J., Etezady‐Esfarjani, Touraj, Herrmann, Torsten, Pedrini, Bill, Peti, Wolfgang, Alimenti, Claudio, Luporini, Pierangelo, Wüthrich, Kurt
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2007
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Online Access:http://dx.doi.org/10.1080/15216540701258165
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spelling crwiley:10.1080/15216540701258165 2024-06-23T07:47:07+00:00 Cold‐adapted signal proteins: NMR structures of pheromones from the antarctic ciliate Euplotes nobilii Placzek, William J. Etezady‐Esfarjani, Touraj Herrmann, Torsten Pedrini, Bill Peti, Wolfgang Alimenti, Claudio Luporini, Pierangelo Wüthrich, Kurt 2007 http://dx.doi.org/10.1080/15216540701258165 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1080%2F15216540701258165 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1080/15216540701258165 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor IUBMB Life volume 59, issue 8-9, page 578-585 ISSN 1521-6543 1521-6551 journal-article 2007 crwiley https://doi.org/10.1080/15216540701258165 2024-06-13T04:23:58Z Abstract 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‐α‐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. The NMR structures of En‐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 Wiley Online Library Antarctic The Antarctic IUBMB Life 59 8 578 585
institution Open Polar
collection Wiley Online Library
op_collection_id crwiley
language English
description Abstract 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‐α‐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. The NMR structures of En‐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.
format Article in Journal/Newspaper
author Placzek, William J.
Etezady‐Esfarjani, Touraj
Herrmann, Torsten
Pedrini, Bill
Peti, Wolfgang
Alimenti, Claudio
Luporini, Pierangelo
Wüthrich, Kurt
spellingShingle Placzek, William J.
Etezady‐Esfarjani, Touraj
Herrmann, Torsten
Pedrini, Bill
Peti, Wolfgang
Alimenti, Claudio
Luporini, Pierangelo
Wüthrich, Kurt
Cold‐adapted signal proteins: NMR structures of pheromones from the antarctic ciliate Euplotes nobilii
author_facet Placzek, William J.
Etezady‐Esfarjani, Touraj
Herrmann, Torsten
Pedrini, Bill
Peti, Wolfgang
Alimenti, Claudio
Luporini, Pierangelo
Wüthrich, Kurt
author_sort Placzek, William J.
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
publisher Wiley
publishDate 2007
url http://dx.doi.org/10.1080/15216540701258165
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1080%2F15216540701258165
https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1080/15216540701258165
geographic Antarctic
The Antarctic
geographic_facet Antarctic
The Antarctic
genre Antarc*
Antarctic
Antarctica
genre_facet Antarc*
Antarctic
Antarctica
op_source IUBMB Life
volume 59, issue 8-9, page 578-585
ISSN 1521-6543 1521-6551
op_rights http://onlinelibrary.wiley.com/termsAndConditions#vor
op_doi https://doi.org/10.1080/15216540701258165
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