NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.

A variety of strains of Euplotes nobilii collected from Antarctic and Arctic waters have been found capable to constitutively secrete cell type-specific signal polypeptides of 50 to 63 amino acids (usually referred to as pheromones) in concentrations high enough (approx 50-150 micrograms of protein/...

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Main Authors: ALIMENTI, Claudio, VALLESI, Adriana, LUPORINI, Pierangelo, B. Pedrini, W. , Wüthrich
Other Authors: Alimenti, Claudio, Vallesi, Adriana, B., Pedrini, W., Wüthrich, Luporini, Pierangelo
Format: Conference Object
Language:English
Published: CIMAR Associate Laboratory & CEQUIMED.UP 2009
Subjects:
Online Access:http://hdl.handle.net/11581/333192
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spelling ftuncamerinoiris:oai:pubblicazioni.unicam.it:11581/333192 2024-01-28T10:01:01+01:00 NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii. ALIMENTI, Claudio VALLESI, Adriana LUPORINI, Pierangelo B. Pedrini W. , Wüthrich Alimenti, Claudio Vallesi, Adriana B., Pedrini W., Wüthrich Luporini, Pierangelo 2009 http://hdl.handle.net/11581/333192 eng eng CIMAR Associate Laboratory & CEQUIMED.UP country:PRT place:Porto info:eu-repo/semantics/altIdentifier/isbn/0000000000 ispartofbook:Proceedings of the 6th European Conference on Marine Natural Products 6th European Conference on Marine Natural Products firstpage:52 lastpage:52 numberofpages:1 http://hdl.handle.net/11581/333192 info:eu-repo/semantics/conferenceObject 2009 ftuncamerinoiris 2024-01-03T17:42:00Z A variety of strains of Euplotes nobilii collected from Antarctic and Arctic waters have been found capable to constitutively secrete cell type-specific signal polypeptides of 50 to 63 amino acids (usually referred to as pheromones) in concentrations high enough (approx 50-150 micrograms of protein/liter of cell culture) to carry out NMR determinations of the relative molecular structures. The four determined pheromone structures all show in common a tight conservation of a three-helix bundle core, that is stabilized by four disulfide bonds and ensures a long-lasting integrity of these molecules in the natural environment. On this conserved scaffold, molecule- and family-specific traits can be distinguished. The individual traits appear to be primarily committed to confer specificity to the autocrine (mitogenic) and paracrine (sexual) signaling activity of each pheromone, and are mainly due to variations in the length and regularity of the three helices, as well as in the shape and orientation of the carboxy-terminal tail. On the other hand, the family-specific traits appear to be evolved in functional correlation with cold-adaptation. Most relevant are: (i) the extension of polypeptide segments devoid of regular secondary structures, (ii) a unique distribution of polar and hydrophobic amino acids, (iii) the presence of solvent-exposed clusters of negatively charged amino acid side chains, and (iv) a central role of aromatic residues in anchoring particular regions of the molecular architecture. Overall these cold-adaptive modifications make the psychrophilic pheromone family of E. nobilii an elegant example of how a high level of global stability of the three-dimensional structures may be combined with sufficient levels of local structural plasticity for efficient functioning of environmental signaling molecules at physiologically low temperatures. Conference Object Antarc* Antarctic Arctic CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino) Arctic Antarctic
institution Open Polar
collection CAMPUS Pubblicazioni Scientifiche Unicam (Università di Camerino)
op_collection_id ftuncamerinoiris
language English
description A variety of strains of Euplotes nobilii collected from Antarctic and Arctic waters have been found capable to constitutively secrete cell type-specific signal polypeptides of 50 to 63 amino acids (usually referred to as pheromones) in concentrations high enough (approx 50-150 micrograms of protein/liter of cell culture) to carry out NMR determinations of the relative molecular structures. The four determined pheromone structures all show in common a tight conservation of a three-helix bundle core, that is stabilized by four disulfide bonds and ensures a long-lasting integrity of these molecules in the natural environment. On this conserved scaffold, molecule- and family-specific traits can be distinguished. The individual traits appear to be primarily committed to confer specificity to the autocrine (mitogenic) and paracrine (sexual) signaling activity of each pheromone, and are mainly due to variations in the length and regularity of the three helices, as well as in the shape and orientation of the carboxy-terminal tail. On the other hand, the family-specific traits appear to be evolved in functional correlation with cold-adaptation. Most relevant are: (i) the extension of polypeptide segments devoid of regular secondary structures, (ii) a unique distribution of polar and hydrophobic amino acids, (iii) the presence of solvent-exposed clusters of negatively charged amino acid side chains, and (iv) a central role of aromatic residues in anchoring particular regions of the molecular architecture. Overall these cold-adaptive modifications make the psychrophilic pheromone family of E. nobilii an elegant example of how a high level of global stability of the three-dimensional structures may be combined with sufficient levels of local structural plasticity for efficient functioning of environmental signaling molecules at physiologically low temperatures.
author2 Alimenti, Claudio
Vallesi, Adriana
B., Pedrini
W., Wüthrich
Luporini, Pierangelo
format Conference Object
author ALIMENTI, Claudio
VALLESI, Adriana
LUPORINI, Pierangelo
B. Pedrini
W. , Wüthrich
spellingShingle ALIMENTI, Claudio
VALLESI, Adriana
LUPORINI, Pierangelo
B. Pedrini
W. , Wüthrich
NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.
author_facet ALIMENTI, Claudio
VALLESI, Adriana
LUPORINI, Pierangelo
B. Pedrini
W. , Wüthrich
author_sort ALIMENTI, Claudio
title NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.
title_short NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.
title_full NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.
title_fullStr NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.
title_full_unstemmed NMR structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, Euplotes nobilii.
title_sort nmr structures of a psychrophilic family of water-borne signal polypeptides isolated from the polar protozoan ciliate, euplotes nobilii.
publisher CIMAR Associate Laboratory & CEQUIMED.UP
publishDate 2009
url http://hdl.handle.net/11581/333192
geographic Arctic
Antarctic
geographic_facet Arctic
Antarctic
genre Antarc*
Antarctic
Arctic
genre_facet Antarc*
Antarctic
Arctic
op_relation info:eu-repo/semantics/altIdentifier/isbn/0000000000
ispartofbook:Proceedings of the 6th European Conference on Marine Natural Products
6th European Conference on Marine Natural Products
firstpage:52
lastpage:52
numberofpages:1
http://hdl.handle.net/11581/333192
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