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A globin domain in a neuronal transmembrane receptor of Caenorhabditis elegans and Ascaris suum: molecular modeling and functional properties

(2015) JOURNAL OF BIOLOGICAL CHEMISTRY. 290(16). p.10336-10352
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Organization
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 form when ferric, even at neutral pH. Flash-photolysis experiments showed overall fast biphasic CO rebinding kinetics. In its ferrous deoxy form, GLB-33 GD is capable of reversibly binding O-2 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.
Keywords
GENE FAMILY, HORSERADISH-PEROXIDASE, HEME OXYGENASE, ELECTRON-PARAMAGNETIC RESONANCE, FMRFAMIDE-RELATED NEUROPEPTIDE, PROTEIN-COUPLED RECEPTORS, CYTOCHROME-C PEROXIDASE, SPERM-WHALE MYOGLOBIN, LIGAND-BINDING, NITRIC-OXIDE, Electron Paramagnetic Resonance (EPR), Hemoglobin, Kinetics, Oxygen Binding, Redox Signaling

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MLA
Tilleman, Lesley et al. “A Globin Domain in a Neuronal Transmembrane Receptor of Caenorhabditis Elegans and Ascaris Suum: Molecular Modeling and Functional Properties.” JOURNAL OF BIOLOGICAL CHEMISTRY 290.16 (2015): 10336–10352. Print.
APA
Tilleman, Lesley, Germani, F., De Henau, S., Helbo, S., Desmet, F., Berghmans, H., Van Doorslaer, S., et al. (2015). A globin domain in a neuronal transmembrane receptor of Caenorhabditis elegans and Ascaris suum: molecular modeling and functional properties. JOURNAL OF BIOLOGICAL CHEMISTRY, 290(16), 10336–10352.
Chicago author-date
Tilleman, Lesley, Francesca Germani, Sasha De Henau, Signe Helbo, Filip Desmet, Herald Berghmans, Sabine Van Doorslaer, et al. 2015. “A Globin Domain in a Neuronal Transmembrane Receptor of Caenorhabditis Elegans and Ascaris Suum: Molecular Modeling and Functional Properties.” Journal of Biological Chemistry 290 (16): 10336–10352.
Chicago author-date (all authors)
Tilleman, Lesley, Francesca Germani, Sasha De Henau, Signe Helbo, Filip Desmet, Herald Berghmans, Sabine Van Doorslaer, David Hoogewijs, Liliane Schoofs, Bart Braeckman, Luc Moens, Angela Fago, and Sylvia Dewilde. 2015. “A Globin Domain in a Neuronal Transmembrane Receptor of Caenorhabditis Elegans and Ascaris Suum: Molecular Modeling and Functional Properties.” Journal of Biological Chemistry 290 (16): 10336–10352.
Vancouver
1.
Tilleman L, Germani F, De Henau S, Helbo S, Desmet F, Berghmans H, et al. A globin domain in a neuronal transmembrane receptor of Caenorhabditis elegans and Ascaris suum: molecular modeling and functional properties. JOURNAL OF BIOLOGICAL CHEMISTRY. 2015;290(16):10336–52.
IEEE
[1]
L. Tilleman et al., “A globin domain in a neuronal transmembrane receptor of Caenorhabditis elegans and Ascaris suum: molecular modeling and functional properties,” JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 290, no. 16, pp. 10336–10352, 2015.
@article{6860885,
  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 form when ferric, even at neutral pH. Flash-photolysis experiments showed overall fast biphasic CO rebinding kinetics. In its ferrous deoxy form, GLB-33 GD is capable of reversibly binding O-2 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.},
  author       = {Tilleman, Lesley and Germani, Francesca and De Henau, Sasha and Helbo, Signe and Desmet, Filip and Berghmans, Herald and Van Doorslaer, Sabine and Hoogewijs, David and Schoofs, Liliane and Braeckman, Bart and Moens, Luc and Fago, Angela and Dewilde, Sylvia},
  issn         = {0021-9258},
  journal      = {JOURNAL OF BIOLOGICAL CHEMISTRY},
  keywords     = {GENE FAMILY,HORSERADISH-PEROXIDASE,HEME OXYGENASE,ELECTRON-PARAMAGNETIC RESONANCE,FMRFAMIDE-RELATED NEUROPEPTIDE,PROTEIN-COUPLED RECEPTORS,CYTOCHROME-C PEROXIDASE,SPERM-WHALE MYOGLOBIN,LIGAND-BINDING,NITRIC-OXIDE,Electron Paramagnetic Resonance (EPR),Hemoglobin,Kinetics,Oxygen Binding,Redox Signaling},
  language     = {eng},
  number       = {16},
  pages        = {10336--10352},
  title        = {A globin domain in a neuronal transmembrane receptor of Caenorhabditis elegans and Ascaris suum: molecular modeling and functional properties},
  url          = {http://dx.doi.org/10.1074/jbc.M114.576520},
  volume       = {290},
  year         = {2015},
}

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