Marie‐France Giraud

ORCID: 0000-0002-6238-667X
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About
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Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • Enzyme Structure and Function
  • Photosynthetic Processes and Mechanisms
  • Amino Acid Enzymes and Metabolism
  • Mechanisms of cancer metastasis
  • Biochemical and Molecular Research
  • Diet, Metabolism, and Disease
  • Metalloenzymes and iron-sulfur proteins
  • MXene and MAX Phase Materials
  • Cancer, Hypoxia, and Metabolism
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Polyamine Metabolism and Applications
  • Ferrocene Chemistry and Applications
  • RNA and protein synthesis mechanisms
  • Cell death mechanisms and regulation
  • Protein Structure and Dynamics
  • RNA Interference and Gene Delivery
  • Microbial Metabolic Engineering and Bioproduction
  • Photodynamic Therapy Research Studies
  • Lipid Membrane Structure and Behavior
  • Fungal and yeast genetics research
  • Metabolism and Genetic Disorders
  • RNA modifications and cancer

Chimie et Biologie des Membranes et des Nanoobjects
2024

Institut Européen de Chimie et Biologie
2003-2024

Université de Bordeaux
2008-2022

Centre National de la Recherche Scientifique
2010-2022

Centre National pour la Recherche Scientifique et Technique (CNRST)
2022

Université Paris-Saclay
2022

Institut Polytechnique de Bordeaux
2022

Institut de Biochimie et Génétique Cellulaires
2008-2020

National Academy of Sciences
2011

University of St Andrews
1998-2006

Subunits e and g of Saccharomyces cerevisiae ATP synthase are required to maintain dimeric forms. Mutants devoid these subunits display anomalous mitochondrial morphologies. An expression system regulated by doxycycline was used modulate the genes encoding g. A decrease in amount subunit induces a g, but does not affect e. The loss or leads supramolecular structures synthase, which is fully reversible upon removal doxycycline. In absence doxycycline, mitochondria present poorly defined...

10.1074/jbc.m404316200 article EN cc-by Journal of Biological Chemistry 2004-07-16

A conserved putative dimerization GxxxG motif located in the unique membrane‐spanning segment of ATP synthase subunit e was altered yeast both by insertion an alanine residue and replacement glycine leucine residues. These alterations led to loss g dimeric oligomeric forms synthase. Furthermore, as null mutants devoid either or g, mitochondria displayed anomalous morphologies with onion‐like structures. By taking advantage presence endogenous cysteine 28 wild‐type e, disulfide bond formation...

10.1046/j.1432-1033.2003.03557.x article EN European Journal of Biochemistry 2003-03-28

The yeast mitochondrial F(1)F(o)-ATP synthase is a large complex of 600 kDa that uses the proton electrochemical gradient generated by respiratory chain to catalyse ATP synthesis from ADP and P(i). For range organisms, it has been shown adopts oligomeric structures. Moreover, several studies have suggested link exists between morphology.In order understand oligomerization morphology, more information needed on supramolecular organization this enzyme within inner membrane. We conducted an...

10.1042/bc20080022 article EN Biology of the Cell 2008-09-18

Only a few genes remain in the mitochondrial genome retained by every eukaryotic organism that carry out essential functions and are implicated severe diseases. Experimentally relocating these to nucleus therefore has both therapeutic evolutionary implications. Numerous unproductive attempts have been made do so, with total of only 5 successes across all organisms. We taken novel approach utilizes naturally nuclear versions from other demonstrate this on subunit 9/c ATP synthase,...

10.1371/journal.pgen.1002876 article EN cc-by PLoS Genetics 2012-08-16

In the yeast Saccharomyces cerevisiae, inactivation of gene encoding delta subunit ATP synthase led to a lack assembly catalytic sector. addition slow-growth phenotype was observed on fermentable medium. This alteration appears in strains lacking intact mitochondrial DNA and showing defect sector, such as strain inactivated epsilon subunit. rho mitochondria having an F1, ion movement resulting from exchange ADP formed organelle entering compartment transmembranous potential psi that...

10.1111/j.1432-1033.1997.00813.x article EN European Journal of Biochemistry 1997-05-01

The three-dimensional structure of ubiquitin-conjugating enzyme 9 (Ubc9) has been obtained to a resolution 2.8 Å by molecular replacement followed combination automated refinement and graphical intervention. Diffraction data were recorded on single crystal in space group P43 with cell dimensions = b 73.9, c 42.9 Å. final model an R factor 21.3% for all Only the N-terminal methionine, two-residue extension four-residue loop are not located electron-density map. Ubc9 is now known be first...

10.1107/s0907444998002480 article EN Acta Crystallographica Section D Biological Crystallography 1998-09-01

Abstract Here we elucidated the pathogenesis of a 14-year-old Chinese female who initially developed an isolated nephropathy followed by complex clinical presentation with brain and muscle problems, which indicated that disease process was possibly due to mitochondrial dysfunction. Careful evaluation renal biopsy samples revealed decreased staining cells induced COX NADH dehydrogenase activities, strong fragmentation network. These anomalies were presence mutation in ATP6 gene, G8969>A....

10.1038/srep36313 article EN cc-by Scientific Reports 2016-11-04

Inhibition of the yeast F(0)F(1)-ATP synthase by regulatory peptides IF1 and STF1 was studied using intact mitochondria submitochondrial particles from wild-type cells or mutants lacking one both peptides. In mitochondria, endogenous only inhibited uncoupled ATP hydrolysis had no effect. Addition alamethicin to readily made mitochondrial membranes permeable nucleotides, bypassed kinetic control exerted on substrate carriers. addition, able cross membranes. At pH 7.3, F(0)F(1)-ATPase,...

10.1021/bi034394t article EN Biochemistry 2003-05-24

The mitochondrial ATP synthase is made of a membrane-integrated F 0 component that forms proton-permeable pore through the inner membrane and globular peripheral 1 domain where synthesized. catalytic mechanism thought to involve rotation 10-12 c subunit ring in together with γ . An important not yet resolved question define precisely how connected -ring. In this study, using doxycycline-regulatable expression system, we provide direct evidence rest enzyme can assemble without δ , show δ-less...

10.1073/pnas.2135169100 article EN Proceedings of the National Academy of Sciences 2003-10-27

l-Rhamnose is an essential component of the cell wall many pathogenic bacteria. Its precursor, dTDP-l-rhamnose, synthesized from α-d-glucose-1-phosphate and dTTP via a pathway requiring four distinct enzymes: RmlA, RmlB, RmlC RmlD. RmlD catalyses terminal step this by converting dTDP-6-deoxy-l-lyxo-4-hexulose to dTDP-l-rhamnose. ­Salmonella enterica serovar Typhimurium has been overexpressed in Escherichia coli. The recombinant protein was purified two-­step protocol involving anion-exchange...

10.1107/s0907444999012251 article EN Acta Crystallographica Section D Biological Crystallography 1999-12-01

Summary Mutant strains of yeast Saccharomyces cerevisiae lacking a functional F 1 ‐ATPase were found to grow very poorly under anaerobic conditions. A single amino acid replacement (K222 > E222) that locally disrupts the adenine nucleotide catalytic site in β‐ subunit was sufficient compromise growth. This mutation also affected growth aerated conditions when ethidium bromide (an intercalating agent impairing mtDNA propagation) or antimycin inhibitor respiration) included medium....

10.1046/j.1365-2958.2003.03371.x article EN Molecular Microbiology 2003-02-19
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