Formation and deformation of hyperextended rift systems: Insights from rift domain mapping in the Bay of Biscay-Pyrenees

International audienceThe Bay of Biscay and the Pyrenees correspond to a Lower Cretaceous rift system including both oceanic and hyperextended rift domains. The transition from preserved oceanic and rift domains in the West to their complete inversion in the East enables us to study the progressive reactivation of a hyperextended rift system. We use seismic interpretation, gravity inversion, and field mapping to identify and map former rift domains and their subsequent reactivation. We propose a new map and sections across the system illustrating the progressive integration of the rift domains into the orogen. This study aims to provide insights on the formation of hyperextended rift systems and discuss their role during reactivation. Two spatially and temporally distinct rift systems can be distinguished: the Bay of Biscay-Parentis and the Pyrenean-Basque-Cantabrian rifts. While the offshore Bay of Biscay represent a former mature oceanic domain, the fossil remnants of hyperextended domains preserved onshore in the Pyrenean-Cantabrian orogen record distributed extensional deformation partitioned between strongly segmented rift basins. Reactivation initiated in the exhumed mantle domain before it affected the hyperthinned domain. Both domains accommodated most of the shortening. The final architecture of the orogen is acquired once the conjugate necking domains became involved in collisional processes. The complex 3-D architecture of the initial rift system may partly explain the heterogeneous reactivation of the overall system. These results have important implications for the formation and reactivation of hyperextended rift systems and for the restoration of the Bay of Biscay and Pyrenean domain

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ESSAI DE SUPPLÉMENTATION EN LYSINE D'UN RÉGIME A BASE DE CÉRÉALES CHEZ LA TRUIE EN GESTATION ET EN LACTATION

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Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.

Beta-lactamases are involved in bacterial resistance. Members of the metallo-enzyme class are now found in many pathogenic bacteria and are becoming thus of major clinical importance. Despite the availability of Zn-beta-lactamase X-ray structures their mechanism of action is still unclear. One puzzling observation is the presence of one or two zincs in the active site. To aid in assessing the role of zinc content in beta-lactam hydrolysis, the replacement by Ser of the zinc-liganding residue Cys168 in the Zn-beta-lactamase from Bacillus cereus strain 569/H/9 was carried out: the mutant enzyme (C168S) is inactive in the mono-Zn form, but active in the di-Zn form. The structure of the mono-Zn form of the C168S mutant has been determined at 1.85 A resolution. Ser168 occupies the same position as Cys168 in the wild-type enzyme. The protein residues mostly affected by the mutation are Asp90-Arg91 and His210. A critical factor for the activity of the mono-Zn species is the distance between Asp90 and the Zn ion, which is controlled by Arg91: a slight movement of Asp90 impairs catalysis. The evolution of a large superfamily including Zn-beta-lactamases suggests that they may not all share the same mechanism

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold.

The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC 3.5.2.6), which catalyses the hydrolysis of nearly all beta-lactams, has been solved at 2.5 A resolution by the multiple isomorphous replacement method, with density modification and phase combination, from crystals of the native protein and of a specially designed mutant (T97C). The current model includes 212 of the 227 amino acid residues, the zinc ion and 10 water molecules. The protein is folded into a beta beta sandwich with helices on each external face. To our knowledge, this fold has never been observed. An approximate internal molecular symmetry is found, with a 2-fold axis passing roughly through the zinc ion and suggesting a possible gene duplication. The active site is located at one edge of the beta beta sandwich and near the N-terminal end of a helix. The zinc ion is coordinated by three histidine residues (86, 88 and 149) and a water molecule. A sequence comparison of the relevant metallo-beta-lactamases, based on this protein structure, highlights a few well-conserved amino acid residues. The structure shows that most of these residues are in the active site. Among these, aspartic acid 90 and histidine 210 participate in a proposed catalytic mechanism for beta-lactam hydrolysis

Supplementation of pig diet with algal fibre changes the chemical and physicochemical characteristics of digesta

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