The C-terminal domain of the virulence factor MgtC is a divergent ACT domain
| Autor: | Martin Cohen-Gonsaud, Anne-Béatrice Blanc-Potard, Laurent Kremer, Kevin Esteves, Séverine Carrère-Kremer, Gilles Labesse, Yinshan Yang |
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| Přispěvatelé: | Centre de Biochimie Structurale [Montpellier] (CBS), Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Institut National de la Santé et de la Recherche Médicale (INSERM), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), This work was supported by Vaincre La Mucoviscidose (IC0902), and S.C.-K. was supported by ANR-06-MIME-027-01., We thank Daniel Ladant (Paris, France) for providing plasmids and W. R. Jacobs for the generous gift of the M. tuberculosis mc27000 strain, which has been approved for use in biosafety level 2 by the Institutional Biosafety Committees of the Albert Einstein College of Medicine and the University of Montpellier 2., Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1) |
| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Protein family Protein Conformation Virulence Factors [SDV]Life Sciences [q-bio] MESH: Virulence Factors/chemistry Molecular Sequence Data MESH: Magnesium/metabolism MESH: Amino Acid Sequence Microbiology Virulence factor MESH: Gene Expression Regulation Bacterial/physiology Mycobacterium tuberculosis 03 medical and health sciences MESH: Protein Structure Tertiary MESH: Mycobacterium tuberculosis/genetics MESH: Protein Conformation MESH: Reverse Transcriptase Polymerase Chain Reaction Hydrolase MESH: Virulence Factors/metabolism MESH: Virulence Factors/genetics MESH: Protein Binding Magnesium Amino Acid Sequence Molecular Biology 030304 developmental biology 0303 health sciences MESH: Molecular Sequence Data biology 030306 microbiology MESH: Magnetic Resonance Spectroscopy MESH: Mycobacterium tuberculosis/metabolism Reverse Transcriptase Polymerase Chain Reaction C-terminus Gene Expression Regulation Bacterial Articles biology.organism_classification Protein Structure Tertiary [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology Biochemistry Cytoplasm Small molecule binding ACT domain MESH: Models Molecular Protein Binding |
| Zdroj: | Journal of Bacteriology Journal of Bacteriology, American Society for Microbiology, 2012, 194 (22), pp.6255-6263. ⟨10.1128/JB.01424-12⟩ |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/JB.01424-12⟩ |
| Popis: | MgtC is a virulence factor of unknown function important for survival inside macrophages in several intracellular bacterial pathogens, including Mycobacterium tuberculosis . It is also involved in adaptation to Mg 2+ deprivation, but previous work suggested that MgtC is not a Mg 2+ transporter. In this study, we demonstrated that the amount of the M. tuberculosis MgtC protein is not significantly increased by Mg 2+ deprivation. Members of the MgtC protein family share a conserved membrane N-terminal domain and a more divergent cytoplasmic C-terminal domain. To get insights into MgtC functional and structural organization, we have determined the nuclear magnetic resonance (NMR) structure of the C-terminal domain of M. tuberculosis MgtC. This structure is not affected by the Mg 2+ concentration, indicating that it does not bind Mg 2+ . The structure of the C-terminal domain forms a βαββαβ fold found in small molecule binding domains called ACT domains. However, the M. tuberculosis MgtC ACT domain differs from canonical ACT domains because it appears to lack the ability to dimerize and to bind small molecules. We have shown, using a bacterial two-hybrid system, that the M. tuberculosis MgtC protein can dimerize and that the C-terminal domain somehow facilitates this dimerization. Taken together, these results indicate that M. tuberculosis MgtC does not have an intrinsic function related to Mg 2+ uptake or binding but could act as a regulatory factor based on protein-protein interaction that could be facilitated by its ACT domain. |
| Databáze: | OpenAIRE |
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