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Start Over Author "Carlier, L.P.A." Topic adp ribose transferases
2 results on '"Carlier, L.P.A."'

1. NMR resonance assignments of NarE, a putative ADP-ribosylating toxin from Neisseria meningitidis

Author

Carlier, L.P.A., Köhler, Christian, Veggi, D., Pizza, M., Soriani, M., Boelens, R., Bonvin, A.M.J.J., NMR Spectroscopy, Sub NMR Spectroscopy, Equipe de Chimie Organique et Biologie Structurale (ECOBS), Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Normandie Université (NU), Université Pierre et Marie Curie - Paris 6 (UPMC), NMR Spectroscopy, and Sub NMR Spectroscopy

Subjects
030303 biophysics, Bacterial Toxins, Molecular Sequence Data, ADP Ribose Transferases, Biology, Neisseria meningitidis, medicine.disease_cause, Biochemistry, Protein Structure, Secondary, Article, 03 medical and health sciences, chemistry.chemical_compound, Structural Biology, medicine, NarE, Meningitis, Amino Acid Sequence, Peptide sequence, Nuclear Magnetic Resonance, Biomolecular, 030304 developmental biology, 0303 health sciences, Adenosine Diphosphate Ribose, Adenosine diphosphate ribose, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Nuclear magnetic resonance spectroscopy, NMR, Heteronuclear molecule, chemistry, ADP ribosylation, ADP-ribosylation, Pathogenic bacteria, Target protein
Abstract

International audience; NarE is a 16 kDa protein identified from Neisseria meningitidis, one of the bacterial pathogens responsible for meningitis. NarE belongs to the ADP-ribosyltransferase family and catalyses the transfer of ADP-ribose moieties to arginine residues in target protein acceptors. Many pathogenic bacteria utilize ADP-ribosylating toxins to modify and alter essential functions of eukaryotic cells. NarE was proposed to bind iron through a Fe-S center which is supposed to be implied in catalysis. We have produced and purified uniformly labeled (15)N- and (15)N/(13)C-NarE and assigned backbone and side-chain resonances using multidimensional heteronuclear NMR spectroscopy. These assignments provide the starting point for the three-dimensional structure determination of NarE and the characterization of the role of the Fe-S center in the catalytic mechanism.

Published
2011
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2. Structural and Biochemical Characterization of NarE, an Iron-containing ADP-ribosyltransferase from Neisseria meningitidis*

Author

Koehler, Christian, Carlier, L.P.A., Veggi, Daniele, Balducci, Enrico, Di Marcello, Federica, Ferrer-Navarro, Mario, Pizza, Mariagrazia, Daura, Xavier, Soriani, Marco, Boelens, Rolf, Bonvin, Alexandre M. J. J., Sub NMR Spectroscopy, NMR Spectroscopy, Sub NMR Spectroscopy, and NMR Spectroscopy

Subjects
Iron-Sulfur Proteins, Magnetic Resonance Spectroscopy, Protein Conformation, Neisseria meningitidis, 01 natural sciences, Biochemistry, nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase, proton nuclear magnetic resonance, Protein structure, iron, antibody, Catalytic Domain, Site-directed mutagenesis, cysteine, mass spectrometry, ADP Ribose Transferases, 0303 health sciences, biology, Chemistry, zinc, Proteolytic enzymes, article, titrimetry, unclassified drug, Solutions, protein NarE, priority journal, consensus sequence, protein protein interaction, Protein Structure and Folding, protein degradation, enzyme active site, Target protein, Iron, Protein degradation, 010402 general chemistry, 03 medical and health sciences, site directed mutagenesis, Consensus sequence, controlled study, Binding site, Molecular Biology, enzyme analysis, 030304 developmental biology, enzyme immobilization, structural homology, nonhuman, Binding Sites, binding site, Active site, Cell Biology, histidine, NAD, 0104 chemical sciences, biology.protein
Abstract

NarE is a 16 kDa protein identified from Neisseria meningitidis, one of the bacterial pathogens responsible for meningitis. NarE belongs to the family of ADP-ribosyltransferases (ADPRT) and catalyzes the transfer of ADP-ribose moieties to arginine residues in target protein acceptors. Many pathogenic bacteria utilize ADP-ribosylating toxins to modify and alter essential functions of eukaryotic cells. NarE is further the first ADPRT which could be shown to bind iron through a Fe-S center, which is crucial for the catalytic activity. Here we present the NMR solution structure of NarE, which shows structural homology to other ADPRTs. Using NMR titration experiments we could identify from Chemical Shift Perturbation data both the NAD binding site, which is in perfect agreement with a consensus sequence analysis between different ADPRTs, as well as the iron coordination site, which consists of 2 cysteines and 2 histidines. This atypical iron coordination is also capable to bind zinc. These results could be fortified by site-directed mutagenesis of the catalytic region, which identified two functionally crucial residues. We could further identify a main interaction region of NarE with antibodies using two complementary methods based on antibody immobilization, proteolytic digestion, and mass spectrometry. This study combines structural and functional features of NarE providing for the first timeacharacterization of an iron-dependent ADPRT. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

Published
2011

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