Search results for: Thierry Granjon

Items from 1 to 12 out of 12 results

article

Evidence of proteolipid domain formation in an inner mitochondrial membrane mimicking model

Mouhedine Cheniour, Jonathan Brewer, Luis Bagatolli, Olivier Marcillat, more

Biochimica et Biophysica Acta (BBA) - General Subjects > 2017 > 1861 > 5(PA) > 969-976

Mitochondrial creatine kinase (mtCK) is highly abundant in mitochondria; its quantity is equimolecular to the Adenylic Nucleotide Translocator and represents 1% of the mitochondrial proteins. It is a multitask protein localized in the mitochondria intermembrane space where it binds to the specific cardiolipin (CL) phospholipid. If mtCK was initially thought to be exclusively implicated in energy transfer...

article

Acyl chain composition determines cardiolipin clustering induced by mitochondrial creatine kinase binding to monolayers

Ofelia Maniti, Mouhedine Cheniour, Marie-France Lecompte, Olivier Marcillat, more

BBA - Biomembranes > 2011 > 1808 > 4 > 1129-1139

It has been recently shown that mitochondrial creatine kinase (mtCK) organizes mitochondrial model membrane by modulating the state and fluidity of lipids and by promoting the formation of protein–cardiolipin clusters. This report shows, using Brewster angle microscopy, that such clustering is largely dependent on the acyl chain composition of phospholipids. Indeed, mtCK-cardiolipin domains were observed...

article

Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion

Ofelia Maniti, Marie-France Lecompte, Olivier Marcillat, Christian Vial, more

European Biophysics Journal > 2010 > 39 > 12 > 1649-1655

Mitochondrial creatine kinase (mtCK) binding to the mitochondrial inner membrane largely determines its biological functions in cellular energy homeostasis, mitochondrial physiology, and dynamics. The membrane binding mechanism is, however, not completely understood. Recent data suggest that a hydrophobic component is involved in mtCK binding to cardiolipin at the outer face of the inner mitochondrial...

article

Mitochondrial creatine kinase interaction with heterogeneous monolayers: Effect on lipid lateral organization

Nathalie Vernoux, Ofelia Maniti, Olivier Marcillat, Christian Vial, more

Biochimie > 2009 > 91 > 6 > 752-764

Our study highlights the tight relationship between protein binding to monolayers and the phase-state of the phospholipids. Interaction of mitochondrial creatine kinase with phospholipidic membranes was analysed using a two-phase monolayer system containing anionic phospholipids under chain mismatch conditions. Monolayers were made up of mixtures of DMPC/DPPG or DPPC/DMPG containing 40% negatively...

article

Mitochondrial Creatine Kinase Binding to Phospholipid Monolayers Induces Cardiolipin Segregation

Ofelia Maniti, Marie-France Lecompte, Olivier Marcillat, Bernard Desbat, more

Biophysical Journal > 2009 > 96 > 6 > 2428-2438

It is well established that the octameric mitochondrial form of creatine kinase (mtCK) binds to the outer face of the inner mitochondrial membrane mainly via electrostatic interactions with cardiolipin (CL). However, little is known about the consequences of these interactions on membrane and protein levels. Brewster angle microscopy investigations provide, for the first time to our knowledge, images...

article

Mitochondrial creatine kinase adsorption to biomimetic membranes: A Langmuir monolayer study

Nathalie Vernoux, Ofelia Maniti, Françoise Besson, Thierry Granjon, more

Journal of Colloid And Interface Science > 2007 > 310 > 2 > 436-445

Interaction of mitochondrial creatine kinase (mtCK) with either synthetic or natural zwitterionic or acidic phospholipids was monitored by surface pressure measurements. Injection of mtCK beneath a monolayer at very low surface pressure results in a large increase in the apparent area per lipid molecule reflecting the intrinsic surface activity of the protein. This effect is particularly pronounced...

article

Oxaloacetate decarboxylase of Vibrio cholerae: purification, characterization, and expression of the genes in Escherichia coli

Pius Dahinden, Yolanda Auchli, Thierry Granjon, Malgorzata Taralczak, more

Archives of Microbiology > 2005 > 183 > 2 > 121-129

The oxaloacetate decarboxylase (OAD) Na⁺ pump consists of subunits α, β, and γ, which are expressed from an oadGAB gene cluster present in various anaerobic bacteria. Vibrio cholerae has two copies of oad genes, which are termed oad-1 and oad-2. The oad-2 genes are part of the citrate fermentation operon, while the oad-1 genes are flanked by genes encoding products not involved in a catabolic pathway...

article

Oligomeric Properties and Signal Peptide Binding by Escherichia coli Tat Protein Transport Complexes

Erik de Leeuw, Thierry Granjon, Ida Porcelli, Meriem Alami, more

Journal of Molecular Biology > 2002 > 322 > 5 > 1135-1146

The Escherichia coli Tat apparatus is a protein translocation system that serves to export folded proteins across the inner membrane. The integral membrane proteins TatA, TatB and TatC are essential components of this pathway. Substrate proteins are directed to the Tat apparatus by specialized N-terminal signal peptides bearing a consensus twin-arginine sequence motif. Here we have systematically...

article

Mitochondrial Creatine Kinase Binding to Phospholipids Decreases Fluidity of Membranes and Promotes New Lipid-Induced β Structures As Monitored by Red Edge Excitation Shift, Laurdan Fluorescence, and FTIR ^†

Thierry Granjon, Marie-Jeanne Vacheron, Christian Vial, René Buchet

Biochemistry > 2001 > 40 > 20 > 6016 - 6026

article

Structural Changes of Mitochondrial Creatine Kinase upon Binding of ADP, ATP, or Pi, Observed by Reaction-Induced Infrared Difference Spectra ^†

Thierry Granjon, Marie-Jeanne Vacheron, Christian Vial, René Buchet

Biochemistry > 2001 > 40 > 9 > 2988 - 2994

article

Mitochondrial Creatine Kinase Binding to Liposomes and Vesicle Aggregation: Effect of Cleavage by Proteinase K

Thierry Granjon, Christian Vial, René Buchet, Marie-Jeanne Vacheron

The Protein Journal > 2001 > 20 > 8 > 593-599

Mitochondrial creatine kinase and its proteinase K nicked-derivative interaction with liposomes induced slight secondary structure changes evidenced by infrared spectra. In nondenaturing conditions, the N-terminal (K₁) and the C-terminal (K₂) fragments remained associated with each other and bound to liposomes. When the two fragments were separated by denaturation, K₂ was soluble, whereas most of...

article

Cloning, Escherichia coli Expression, and Phase-Transition Chromatography-Based Purification of Recombinant Rabbit Heart Mitochondrial Creatine Kinase

Olivier Marcillat, Catherine Perraut, Thierry Granjon, Christian Vial, more

Protein Expression and Purification > 1999 > 17 > 1 > 163-168

A cDNA clone of the mitochondrial sarcomeric creatine kinase cDNA was obtained by screening a rabbit heart library. This cDNA is characterized by a 1257-nucleotide open reading frame encoding a 419-amino-acid protein with a cleavable 39-amino-acid mitochondrial presequence (Accession No. AJ011334). This new member of the guanidino kinase family shows a high degree of sequence similarity with the other...

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