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853 results on '"Ruysschaert, Jean-Marie"'

3. Spontaneous Nanotube Formation of a Very Asymmetric Glycolipid

Author

Losada Pérez, Patricia, primary, Villanueva, Martin Eduardo, additional, Bar, Laure, additional, Redondo-Morata, Lorena, additional, Namdar, Peter, additional, Ruysschaert, Jean Marie, additional, Pabst, George, additional, Vandier, Christophe, additional, and Bouchet, Ana Maria, additional

Published
2024
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8. Phospholipid acyl tail affects lipid headgroup orientation and membrane hydration.

Author

Maltseva, Daria, Gonella, Grazia, Ruysschaert, Jean-Marie, and Bonn, Mischa

Subjects
BIOLOGICAL interfaces, BREWSTER'S angle, CHEMICAL chains, HYDRATION, SURFACE pressure
Abstract

Biomembrane hydration is crucial for understanding processes at biological interfaces. While the effect of the lipid headgroup has been studied extensively, the effect (if any) of the acyl chain chemical structure on lipid-bound interfacial water has remained elusive. We study model membranes composed of phosphatidylethanolamine (PE) and phosphatidylcholine (PC) lipids, the most abundant lipids in biomembranes. We explore the extent to which the lipid headgroup packing and associated water organization are affected by the lipid acyl tail unsaturation and chain length. To this end, we employ a combination of surface-sensitive techniques, including sum-frequency generation spectroscopy, surface pressure measurements, and Brewster angle microscopy imaging. Our results reveal that the acyl tail structure critically affects the headgroup phosphate orientational distribution and lipid-associated water molecules, for both PE and PC lipid monolayers at the air/water interface. These insights reveal the importance of acyl chain chemistry in determining not only membrane fluidity but also membrane hydration. [ABSTRACT FROM AUTHOR]

Published
2022
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11. Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems

Author

De Angelis, Fabien, Lee, John K, O'Connell, Joseph D, Miercke, Larry JW, Verschueren, Koen H, Srinivasan, Vasundara, Bauvois, Cédric, Govaerts, Cédric, Robbins, Rebecca A, Ruysschaert, Jean-Marie, Stroud, Robert M, and Vandenbussche, Guy

Subjects
Biochemistry and Cell Biology, Biological Sciences, Prevention, Emerging Infectious Diseases, Antimicrobial Resistance, Infectious Diseases, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Amino Acid Sequence, Amino Acid Substitution, Bacterial Proteins, Binding Sites, Carrier Proteins, Cation Transport Proteins, Crystallography, X-Ray, Cupriavidus, Drug Resistance, Bacterial, Membrane Fusion Proteins, Metals, Heavy, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutant Proteins, Phylogeny, Protein Conformation, Protein Structure, Tertiary, Recombinant Proteins, Sequence Homology, Amino Acid, Spectroscopy, Fourier Transform Infrared, Zinc, Cupriavidus metallidurans CH34, heavy-metal resistance, resistance nodulation cell division, periplasmic adaptor protein
Abstract

Resistance nodulation cell division (RND)-based efflux complexes mediate multidrug and heavy-metal resistance in many Gram-negative bacteria. Efflux of toxic compounds is driven by membrane proton/substrate antiporters (RND protein) in the plasma membrane, linked by a membrane fusion protein (MFP) to an outer-membrane protein. The three-component complex forms an efflux system that spans the entire cell envelope. The MFP is required for the assembly of this complex and is proposed to play an important active role in substrate efflux. To better understand the role of MFPs in RND-driven efflux systems, we chose ZneB, the MFP component of the ZneCAB heavy-metal efflux system from Cupriavidus metallidurans CH34. ZneB is shown to be highly specific for Zn(2+) alone. The crystal structure of ZneB to 2.8 A resolution defines the basis for metal ion binding in the coordination site at a flexible interface between the beta-barrel and membrane proximal domains. The conformational differences observed between the crystal structures of metal-bound and apo forms are monitored in solution by spectroscopy and chromatography. The structural rearrangements between the two states suggest an active role in substrate efflux through metal binding and release.

Published
2010

38. Calcium-triggered membrane interaction of the alpha-synuclein Acidic tail

Author

Tamamizu-Kato, Shiori, Kosaraju, Malathi G., Kato, Hiroyuki, Raussens, Vincent, Ruysschaert, Jean-Marie, and Narayanaswami, Vasanthy

Subjects
Lewy body disease -- Research, Calcium, Dietary -- Structure, Calcium, Dietary -- Chemical properties, Oxidative stress -- Research, Proteins -- Conformation, Proteins -- Analysis, Biological sciences, Chemistry
Abstract

The effect of Ca(super 2+) on the acidic tail conformation in lipid-bound alpha-Synuclein is examined. The results provide structural details towards understanding the complex interplay between membranes, alpha-Synuclein, and Ca(super 2+) and events leading to pathogenesis of Parkinson disease.

Published
2006

42. Phospholipid species act as modulators in p97/p47-mediated fusion of Golgi membranes

Author

Pecheur, Eve-Isabelle, Martin, Isabelle, Maier, Olaf, Bakowsky, Udo, Ruysschaert, Jean-Marie, and Hoekstra, Dick

Subjects
Golgi apparatus -- Physiological aspects, Membrane fusion -- Physiological aspects, Cephalin -- Physiological aspects, Proteins -- Conformation, Biological sciences, Chemistry
Abstract

Research demonstrates fusion between mitotic Golgi membranes mediated by cytosol or p97/p47 complex is modulated by phosphatidyl ethanolamine but not by phosphatidyl choline. Data show that the complex is recruited to the membrane by the phospholipid causing conformational rearrangements, which lead to protein-lipid interactions.

Published
2002

43. Structure and dynamics of the membrane-embedded domain of LmrA investigated by coupling polarized ATR-FTIR spectroscopy and (super)1 H/ (super)2 H exchange

Author

Grimard, Vinciane, Vigano, Catherine, Margolles, Abelardo, Wattiez, Ruddy, Veen, Hendrik W. van, Konings, Wil N., Ruysschaert, Jean-Marie, and Goormaghtigh, Erik

Subjects
Biochemistry -- Research, Hydrogen -- Physiological aspects, Fourier transform infrared spectroscopy -- Usage, Membrane proteins -- Analysis, Infrared spectroscopy -- Usage, Lactococcus -- Physiological aspects, Proteolysis -- Analysis, Biological sciences, Chemistry
Abstract

Research has been conducted on the bacterial LmrA, Lactococcus lactis's integral membrane protein. The secondary structure and the orientation of the LmrA's transmembrane segments have been investigated via the polarized attenuated total reflection infrared spectroscopy and limited proteolysis.

Published
2001

44. Membrane interactions of mutated forms of the influenza fusion peptide

Author

Epand, Richard M., Epand, Raquel F., Martin, Isabelle, and Ruysschaert, Jean-Marie

Subjects
Biochemistry -- Research, Influenza -- Causes of, Peptides -- Research, Gene mutations -- Physiological aspects, Membranes (Biology) -- Genetic aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the group of fusion peptides of influenza hemagglutinin. The substitution of the N-terminal amino acid found in the wild-type peptide with Ala, Ser, Val and Glu has been investigated and the results are presented.

Published
2001

46. A Transmembrane Histidine Kinase Functions as a pH Sensor

Author

Bortolotti, Ana, primary, Vazquez, Daniela Belén, additional, Almada, Juan Cruz, additional, Inda, Maria Eugenia, additional, Drusin, Salvador Iván, additional, Villalba, Juan Manuel, additional, Moreno, Diego M., additional, Ruysschaert, Jean Marie, additional, and Cybulski, Larisa Estefania, additional

Published
2020
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49. Role of the carboxy terminus of Escherichia coli FtsA in self-interaction and cell division

Author

Yim, Lucia, Vandenbussche, Guy, Mingorance, Jesus, Rueda, Sonsoles, Casanova, Mercedes, Ruysschaert, Jean-Marie, and Vicente, Miguel

Subjects
Escherichia coli -- Physiological aspects, Cell division -- Physiological aspects, Proteins -- Structure, Amino acids -- Structure-activity relationships, Gene mutations -- Analysis, Biological sciences
Abstract

Results point out that the biological function of FtsA protein is regulated by the carboxy-terminal amino acid residues in a way not related to its overall structure but is related to some modification in its interacting properties. Data indicate that FtsA molecule interacts with itself in manifesting its biological role in cell division.

Published
2000

50. Multidrug resistance protein MRP1 reconstituted into lipid vesicles: secondary structure and nucleotide-induced tertiary structure changes

Author

Manciu, Liliana, Chang, Xiu-Bao, Riordan, John R., and Ruysschaert, Jean-Marie

Subjects
Cytochemistry -- Research, Cancer, Catalysis -- Physiological aspects, Chemotherapy -- Physiological aspects, Adenosine triphosphate -- Physiological aspects, Biological sciences, Chemistry
Abstract

Multidrug resistance protein MRP1 has been reconstituted in lipid vesicles.The reconstitudes protein conserves ATPase dna drug transport activity. Secondary structure and nucleotide-induced tertiary structure changes are discussed. It was found that the secondary strucutre of MRP1 is not affected upon binding of different nucleotides. The tertiary strucuter of MRP1 changes in the catalytic cycle. In chemotherapy, resistance of cells to cytotoxic agents is a major problem.

Published
2000

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