3 results match your criteria: "CEA-Centre de Saclay[Affiliation]"
Biosci Rep
April 2015
*Laboratoire Léon Brillouin, CEA-Centre de Saclay, 91191 Gif-sur-Yvette, France.
Accumulating evidence indicates that RNA metabolism components assemble into supramolecular cellular structures to mediate functional compartmentalization within the cytoplasmic membrane of the bacterial cell. This cellular compartmentalization could play important roles in the processes of RNA degradation and maturation. These components include Hfq, the RNA chaperone protein, which is involved in the post-transcriptional control of protein synthesis mainly by the virtue of its interactions with several small regulatory ncRNAs (sRNA).
View Article and Find Full Text PDFIntegr Biol (Camb)
January 2015
Laboratoire Léon Brillouin, CEA - Centre de Saclay, 91191 Gif-sur-Yvette, France.
The bacterial actin-homolog MreB is a key player in bacterial cell-wall biosynthesis and is required for the maintenance of the rod-like morphology of Escherichia coli. However, how MreB cellular levels are adjusted to growth conditions is poorly understood. Here, we show that DsrA, an E.
View Article and Find Full Text PDFFEBS Lett
October 2006
CEA Centre de Saclay, Département de Biologie Joliot-Curie and URA CNRS 2096, Service de Biophysique des Protéines et des Membranes, Bat 528, 91191 Gif sur Yvette Cedex, France.
Circular dichroism (CD) and NMR spectroscopy were used to study the conformational properties of two synthetic peptides, D82-R101 and D82-I109, encompassing the caveolin scaffolding domain (D82-R101), in the presence of dodecylphosphocholine (DPC) micelles. Our data show that a stable helical conformation of the caveolin scaffolding domain in a membrane mimicking system is only obtained for the peptide including the L102-I109 hydrophobic stretch, a part of the caveolin intra-membrane domain. Through chemical shift variations, an ensemble of six residues of the D82-L109 peptide, mainly located in the V(94)TKYWFYR(101) motif were found to detect the presence of phosphatidylserine solubilized in DPC micelles.
View Article and Find Full Text PDF