Abundance of Cnidaria and Ctenophora taxa in the North Atlantic sampled during the G. O. Sars Cruise in May 2013

In recent years a global increase in jellyfish (i.e. Cnidarians and Ctenophores) abundance and a rise in the recurrence of jellyfish outbreak events have been largely debated, but a general consensus on this matter has not been achieved yet. Within this debate, it has been generally recognized that there is a lack of reliable data that could be analyzed and compared to clarify whether indeed jellyfish are increasing throughout the world ocean as a consequence of anthropogenic impact and hydroclimatic variability. During the G.O. Sars cruise jellyfish were collected at different depths in the 0-1000m layer using a standard 1 m**2 Multiple Opening/Closing Net and Environmental Sensing System (MOCNESS) (quantitative data), Harstad and macroplankton trawls (qualitative data). The comparison of records collected with different nets during the G.O. Sars transatlantic cruise shows that different sampling gears might provide very different information on jellyfish diversity. Indeed, the big trawls mostly collect relatively large scyphozoan and hydrozoan species such as Atolla, Pelagia, Praya, Vogtia, while small hydrozoans (e.g. Clytia, Gilia, Muggiaea) and early stages of ctenophora are only caught by the smaller nets.

The 2.1 angstrom crystal structure of copGFP, a representative member of the copepod clade within the green fluorescent protein superfamily

The green fluorescent protein (avGFP), its variants, and the closely related GFP-like proteins are characterized structurally by a cyclic tri-peptide chromophore located centrally within a conserved beta-can fold. Traditionally, these GFP family members have been isolated from the Cnidaria although recently, distantly related GFP-like proteins from the Bilateria, a sister group of the Cnidaria have been described, although no representative structure from this phylum has been reported to date. We have determined to 2.1 angstrom resolution the crystal structure of copGFP, a representative GFP-like protein from a copepod, a member of the Bilateria. The structure of copGFP revealed that, despite sharing only 19% sequence identity with GFP, the tri-peptide chromophore (Gly57-Tyr58-Gly59) of copGFP adopted a cis coplanar conformation within the conserved beta-can fold. However, the immediate environment surrounding the chromophore of copGFP was markedly atypical when compared to other members of the GFP-superfamily, with a large network of bulky residues observed to surround the chromophore. Arg87 and Glu222 (GFP numbering 96 and 222), the only two residues conserved between copGFP, GFP and GFP-like proteins are involved in autocatalytic genesis of the chromophore. Accordingly, the copGFP structure provides an alternative platform for the development of a new suite of fluorescent protein tools. Moreover, the structure suggests that the autocatalytic genesis of the chromophore is remarkably tolerant to a high degree of sequence and structural variation within the beta-can fold of the GFP superfamily. (c) 2006 Elsevier Ltd . All rights reserved.

Clonage moléculaire, caractérisation et localisation de deux récepteurs couplés à la protéine G chez le cnidaire Renilla koellikeri (Anthozoa)

Thèse numérisée par la Direction des bibliothèques de l'Université de Montréal.

Clonage moléculaire, caractérisation et localisation de deux récepteurs couplés à la protéine G chez le cnidaire Renilla koellikeri (Anthozoa)

Thèse numérisée par la Direction des bibliothèques de l'Université de Montréal.