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18 results on '"Tilleman, Lesley"'

1. Ever Surprising Nematode Globins

Author

Hoogewijs, David, Geuens, Eva, Tilleman, Lesley, Vanfleteren, Jacques R., Moens, Luc, Dewilde, Sylvia, Zouhair Atassi, M., editor, Berliner, Lawrence J., editor, Chang, Rowen Jui-Yoa, editor, Jörnvall, Hans, editor, Kenyon, George L., editor, Wittman-Liebold, Brigitte, editor, Bolognesi, Martino, editor, di Prisco, Guido, editor, and Verde, Cinzia, editor

Published
2008
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4. A globin domain in a neuronal transmembrane receptor of caenorhabditis elegans and ascaris suum : molecular modeling and functional properties

Author

Tilleman, Lesley, Germani, Francesca, De Henau, Sasha, Helbo, Signe, Desmet, Filip, Berghmans, Herald, Van Doorslaer, Sabine, Hoogewijs, David, Schoofs, Liliane, Braeckman, Bart P, Moens, Luc, Fago, Angela, Dewilde, Sylvia, Tilleman, Lesley, Germani, Francesca, De Henau, Sasha, Helbo, Signe, Desmet, Filip, Berghmans, Herald, Van Doorslaer, Sabine, Hoogewijs, David, Schoofs, Liliane, Braeckman, Bart P, Moens, Luc, Fago, Angela, and Dewilde, Sylvia

Abstract

We report the structural and biochemical characterization of GLB-33, a putative neuropeptide receptor that is exclusively expressed in the nervous system of the nematode Caenorhabditis elegans. This unique chimeric protein is composed of a 7-transmembrane domain (7TM), GLB-33 7TM, typical of a G-protein-coupled receptor, and of a globin domain (GD), GLB-33 GD. Comprehensive sequence similarity searches in the genome of the parasitic nematode, Ascaris suum, revealed a chimeric protein that is similar to a Phe-Met-Arg-Phe-amide neuropeptide receptor. The three-dimensional structures of the separate domains of both species and of the full-length proteins were modeled. The 7TM domains of both proteins appeared very similar, but the globin domain of the A. suum receptor surprisingly seemed to lack several helices, suggesting a novel truncated globin fold. The globin domain of C. elegans GLB-33, however, was very similar to a genuine “myoglobin”-type molecule. Spectroscopic analysis of the recombinant GLB-33 GD showed that the heme is pentacoordinate when ferrous and in the hydroxide-ligated formwhenferric, even at neutral pH. Flash-photolysis experiments showed overall fast biphasic CO rebinding kinetics. In its ferrous deoxy form, GLB-33GDis capable of reversibly binding O2 with a very high affinity and of reducing nitrite to nitric oxide faster than other globins. Collectively, these properties suggest that the globin domain of GLB-33 may serve as a highly sensitive oxygen sensor and/or as a nitrite reductase. Both properties are potentially able to modulate the neuropeptide sensitivity of the neuronal transmembrane receptor.

Published
2015

5. A redox signalling globin is essential for reproduction in Caenorhabditis elegans

Author

De Henau, Sasha, primary, Tilleman, Lesley, additional, Vangheel, Matthew, additional, Luyckx, Evi, additional, Trashin, Stanislav, additional, Pauwels, Martje, additional, Germani, Francesca, additional, Vlaeminck, Caroline, additional, Vanfleteren, Jacques R., additional, Bert, Wim, additional, Pesce, Alessandra, additional, Nardini, Marco, additional, Bolognesi, Martino, additional, De Wael, Karolien, additional, Moens, Luc, additional, Dewilde, Sylvia, additional, and Braeckman, Bart P., additional

Published
2015
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7. Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans

Author

Tilleman, Lesley, primary, Abbruzzetti, Stefania, additional, Ciaccio, Chiara, additional, De Sanctis, Giampiero, additional, Nardini, Marco, additional, Pesce, Alessandra, additional, Desmet, Filip, additional, Moens, Luc, additional, Van Doorslaer, Sabine, additional, Bruno, Stefano, additional, Bolognesi, Martino, additional, Ascenzi, Paolo, additional, Coletta, Massimo, additional, Viappiani, Cristiano, additional, and Dewilde, Sylvia, additional

Published
2015
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8. A Globin Domain in a Neuronal Transmembrane Receptor of Caenorhabditis elegans and Ascaris suum

Author

Tilleman, Lesley, primary, Germani, Francesca, additional, De Henau, Sasha, additional, Helbo, Signe, additional, Desmet, Filip, additional, Berghmans, Herald, additional, Van Doorslaer, Sabine, additional, Hoogewijs, David, additional, Schoofs, Liliane, additional, Braeckman, Bart P., additional, Moens, Luc, additional, Fago, Angela, additional, and Dewilde, Sylvia, additional

Published
2015
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11. An N-Myristoylated Globin with a Redox-Sensing Function That Regulates the Defecation Cycle in Caenorhabditis elegans

Author

Tilleman, Lesley, primary, De Henau, Sasha, additional, Pauwels, Martje, additional, Nagy, Nora, additional, Pintelon, Isabel, additional, Braeckman, Bart P., additional, De Wael, Karolien, additional, Van Doorslaer, Sabine, additional, Adriaensen, Dirk, additional, Timmermans, Jean-Pierre, additional, Moens, Luc, additional, and Dewilde, Sylvia, additional

Published
2012
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13. Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin

Author

Abbruzzetti, Stefania, primary, Tilleman, Lesley, additional, Bruno, Stefano, additional, Viappiani, Cristiano, additional, Desmet, Filip, additional, Van Doorslaer, Sabine, additional, Coletta, Massimo, additional, Ciaccio, Chiara, additional, Ascenzi, Paolo, additional, Nardini, Marco, additional, Bolognesi, Martino, additional, Moens, Luc, additional, and Dewilde, Sylvia, additional

Published
2012
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16. Globins in Caenorhabditis elegans

Author

Tilleman, Lesley, primary, Germani, Francesca, additional, De Henau, Sasha, additional, Geuens, Eva, additional, Hoogewijs, David, additional, Braeckman, Bart P., additional, Vanfleteren, Jacques R., additional, Moens, Luc, additional, and Dewilde, Sylvia, additional

Published
2011
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17. Globin-like proteins in Caenorhabditis elegans: in vivo localization, ligand binding and structural properties

Author

Geuens, Eva, primary, Hoogewijs, David, additional, Nardini, Marco, additional, Vinck, Evi, additional, Pesce, Alessandra, additional, Kiger, Laurent, additional, Fago, Angela, additional, Tilleman, Lesley, additional, De Henau, Sasha, additional, Marden, Michael C, additional, Weber, Roy E, additional, Van Doorslaer, Sabine, additional, Vanfleteren, Jacques, additional, Moens, Luc, additional, Bolognesi, Martino, additional, and Dewilde, Sylvia, additional

Published
2010
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18. Structure and Haem-Distal Site Plasticity in Methanosarcina acetivorans Protoglobin.

Author

Pesce, Alessandra, Tilleman, Lesley, Donné, Joke, Aste, Elisa, Ascenzi, Paolo, Ciaccio, Chiara, Coletta, Massimo, Moens, Luc, Viappiani, Cristiano, Dewilde, Sylvia, Bolognesi, Martino, and Nardini, Marco

Subjects
*METHANOSARCINA, *METHANOGENS, *PROTEIN structure, *PROTEIN binding, *PROTEIN stability, *LIGANDS (Biochemistry), *HYDROGEN bonding
Abstract

Protoglobin from Methanosarcina acetivorans C2A (MaPgb), a strictly anaerobic methanogenic Archaea, is a dimeric haem-protein whose biological role is still unknown. As other globins, protoglobin can bind O2, CO and NO reversibly in vitro, but it displays specific functional and structural properties within members of the hemoglobin superfamily. CO binding to and dissociation from the haem occurs through biphasic kinetics, which arise from binding to (and dissociation from) two distinct tertiary states in a ligation-dependent equilibrium. From the structural viewpoint, protoglobin-specific loops and a N-terminal extension of 20 residues completely bury the haem within the protein matrix. Thus, access of small ligand molecules to the haem is granted by two apolar tunnels, not common to other globins, which reach the haem distal site from locations at the B/G and B/E helix interfaces. Here, the roles played by residues Trp(60)B9, Tyr(61)B10 and Phe(93)E11 in ligand recognition and stabilization are analyzed, through crystallographic investigations on the ferric protein and on selected mutants. Specifically, protein structures are reported for protoglobin complexes with cyanide, with azide (also in the presence of Xenon), and with more bulky ligands, such as imidazole and nicotinamide. Values of the rate constant for cyanide dissociation from ferric MaPgb-cyanide complexes have been correlated to hydrogen bonds provided by Trp(60)B9 and Tyr(61)B10 that stabilize the haem-Fe(III)-bound cyanide. We show that protoglobin can strikingly reshape, in a ligand-dependent way, the haem distal site, where Phe(93)E11 acts as ligand sensor and controls accessibility to the haem through the tunnel system by modifying the conformation of Trp(60)B9. [ABSTRACT FROM AUTHOR]

Published
2013
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