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See detailNd and Pb isotope signatures of the clay-size fraction of Labrador Sea sediments during the Holocene: Implications for the inception of the modern deep circulation pattern
Fagel, Nathalie ULg; Hillaire-Marcel, Claude ULg; Humblet, Marc et al

in Paleoceanography (2004), 19(3),

Nd and Pb isotopes were measured on the fine fraction of one sediment core drilled off southern Greenland. This work aims to reconstruct the evolution of deep circulation patterns in the North Atlantic ... [more ▼]

Nd and Pb isotopes were measured on the fine fraction of one sediment core drilled off southern Greenland. This work aims to reconstruct the evolution of deep circulation patterns in the North Atlantic during the Holocene on the basis of sediment supply variations. For the last 12 kyr, three sources have contributed to the sediment mixture: the North American Shield, the Pan-African and Variscan crusts, and the Mid-Atlantic Ridge. Clay isotope signatures indicate two mixtures of sediment sources. The first mixture (12.2-6.5 ka) is composed of material derived from the North American shield and from a "young'' crustal source. From 6.5 ka onward the mixture is characterized by a young crustal component and by a volcanic component characteristic of the Mid-Atlantic Ridge. Since the significant decrease in proximal deglacial supplies, the evolution of the relative contributions of the sediment sources suggests major changes in the relative contributions of the deep water masses carried by the Western Boundary Undercurrent over the past 8.4 kyr. The progressive intensification of the Western Boundary Undercurrent was initially associated mainly with the transport of the Northeast Atlantic Deep Water mass until 6.5 ka and with the Denmark Strait Overflow Water thereafter. The establishment of the modern circulation at 3 ka suggests a reduced influence of the Denmark Strait Overflow Water, synchronous with the full appearance of the Labrador Seawater mass. Our isotopic data set emphasizes several changes in the relative contribution of the two major components of North Atlantic Deep Water throughout the Holocene. [less ▲]

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See detailDifferential Functionalities of Amphiphilic Peptide Segments of the Cell-Septation Penicillin-Binding Protein 3 of Escherichia Coli
Marrec-Fairley, Monique; Piette, André ULg; Gallet, Xavier et al

in Molecular Microbiology (2000), 37(5), 1019-1031

The class B M1-V577 penicillin-binding protein (PBP) 3 of Escherichia coli consists of a M1-L39 membrane anchor (bearing a cytosolic tail) that is linked via a G40-S70 intervening peptide to an R71-I236 ... [more ▼]

The class B M1-V577 penicillin-binding protein (PBP) 3 of Escherichia coli consists of a M1-L39 membrane anchor (bearing a cytosolic tail) that is linked via a G40-S70 intervening peptide to an R71-I236 non-catalytic module (containing the conserved motifs 1-3) itself linked via motif 4 to a D237-V577 catalytic module (containing the conserved motifs 5-7 of the penicilloyl serine transferases superfamily). It has been proposed that during cell septation the peptidoglycan crosslinking activity of the acyl transferase module of PBP3 is regulated by the associated M1-I236 polypeptide itself in interaction with other components of the divisome. The fold adopted by the R71-V577 polypeptide of PBP3 has been modelled by reference to the corresponding R76-S634 polypeptide of the class B Streptococcus pneumoniae PBP2x. Based on these data and the results of site-directed mutagenesis of motifs 1-3 and of peptide segments of high amphiphilicity (identified from hydrophobic moment plots), the M1-I236 polypeptide of PBP3 appears to be precisely designed to work in the way proposed. The membrane anchor and the G40-S70 sequence (containing the G57-Q66 peptide segment) upstream from the non-catalytic module have the information ensuring that PBP3 undergoes proper insertion within the divisome at the cell septation site. Motif 1 and the I74-L82 overlapping peptide segment, motif 2 and the H160-G172 overlapping peptide segment, and the G188-D197 motif 3 are located at or close to the intermodule junction. They contain the information ensuring that PBP3 folds correctly and the acyl transferase catalytic centre adopts the active configuration. The E206-V217 peptide segment is exposed at the surface of the non-catalytic module. It has the information ensuring that PBP3 fulfils its cell septation activity within the fully complemented divisome. [less ▲]

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