Share This Author
Enzymatic and Structural Similarities between theEscherichia coli ATP-dependent Proteases, ClpXP and ClpAP*
- R. Grimaud, M. Kessel, F. Beuron, A. Steven, M. Maurizi
- Chemistry, BiologyJournal of Biological Chemistry
- 15 May 1998
ClpX and ClpA interactions with ClpP result in structurally analogous complexes and induce similar conformational changes that affect the accessibility and the catalytic efficiency of Clpp active sites.
Repair of Oxidized Proteins
A new methionine sulfoxide reductase is identified, which is referred to as MsrB, the gene of which is present in genomes of eubacteria, archaebacteria, and eucaryotes and is required for cadmium resistance of E. coli.
Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.
- S. Singh, R. Grimaud, J. Hoskins, S. Wickner, M. Maurizi
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 1 August 2000
ClpX can catalyze unfolding of a green fluorescent protein fused to a ClpX recognition motif (GFP-SsrA) and the results suggest a bipartite mode of interaction between Clp X and substrates.
Physiological Adaptation of Desulfitobacterium hafniense Strain TCE1 to Tetrachloroethene Respiration
- Laure Prat, J. Maillard, R. Grimaud, C. Holliger
- BiologyApplied and Environmental Microbiology
- 8 April 2011
Proteomic results suggest that D. hafniense strain TCE1 adapts its physiology to face the relative unfavorable growth conditions during an apparent opportunistic organohalide respiration.
Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli
- B. Ezraty, R. Grimaud, M. Hassouni, Daniéle Moinier, F. Barras
- Biology, ChemistryEMBO Journal
- 21 April 2004
It is concluded that MsrA and MsrB are required to repair Ffh oxidized by reactive oxygen species produced by aerobic metabolism, establishing an as‐yet undescribed link between protein targeting and oxidation.
The marine bacterium Marinobacter hydrocarbonoclasticus SP17 degrades a wide range of lipids and hydrocarbons through the formation of oleolytic biofilms with distinct gene expression profiles.
It is shown that Marinobacter hydrocarbonoclasticus SP17 develops biofilmms, referred to as oleolytic biofilms, on a large variety of hydrophobic substrates, including hydrocarbons, fatty alcohols, fatty acids, triglycerides, and wax esters.
Cytoplasmic wax ester accumulation during biofilm-driven substrate assimilation at the alkane--water interface by Marinobacter hydrocarbonoclasticus SP17.
Degradation of the “Erika” oil
Since March 2001, samples of the remaining oil from the wreck of the "Erika" have been collected along the Atlantic coastline in order to assess the natural degradation rate. Four years after the…
Bacteriophage Mu repressor as a target for the Escherichia coli ATP‐dependent Clp Protease.
The results support the existence of the existence, on the substrate polypeptides, of separate motifs responsible for recognition and cleavage by the protease.
Genome Sequence of the Marine Bacterium Marinobacter hydrocarbonoclasticus SP17, Which Forms Biofilms on Hydrophobic Organic Compounds
The genome sequence of Marinobacter hydrocarbonoclasticus SP17 is presented, which could provide further insights into the mechanisms of enhancement of HOCs assimilation through biofilm formation.