Bacteriophage SPP1 tail tube protein self-assembles into β-structure-rich tubes
| Autor: | Langlois, Chantal, Ramboarina, Stéphanie, Cukkemane, Abhishek, Auzat, Isabelle, Chagot, Benjamin, Gilquin, Bernard, Ignatiou, Athanasios, Petitpas, Isabelle, Kasotakis, Emmanouil, Paternostre, Maïté, White, Helen E., Orlova, Elena V., Baldus, Marc, Tavares, Paulo, Zinn-Justin, Sophie, Sub NMR Spectroscopy, NMR Spectroscopy |
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| Přispěvatelé: | Institut de Biologie et de Technologies de Saclay (IBITECS), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Laboratoire de Biologie Structurale et Radiobiologie (LBSR), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Department of Chemistry, Faculty of Science, Utrecht University, 3584 CH Utrecht, The Netherlands, Laboratoire de Virologie Moléculaire et Structurale, Centre National de la Recherche Scientifique (CNRS), Institute of Structural & Molecular Biology, Birkbeck College, University College of London [London] (UCL), Interactions et mécanismes d’assemblage des protéines et des peptides (IMAPP), Département Biochimie, Biophysique et Biologie Structurale (B3S), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut de Biologie et de Technologies de Saclay ( IBITECS ), Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Laboratoire de Biologie Structurale et Radiobiologie ( LBSR ), Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ), Centre National de la Recherche Scientifique ( CNRS ), University College of London [London] ( UCL ), Interactions et mécanismes d’assemblage des protéines et des peptides ( IMAPP ), Département Biochimie, Biophysique et Biologie Structurale ( B3S ), Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Institut de Biologie Intégrative de la Cellule ( I2BC ), Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ) -Université Paris-Sud - Paris 11 ( UP11 ) -Commissariat à l'énergie atomique et aux énergies alternatives ( CEA ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Sub NMR Spectroscopy, NMR Spectroscopy |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Protein Folding
[SDV]Life Sciences [q-bio] Molecular Sequence Data Fourier Transform IR (FTIR) Biology Biochemistry Bacteriophage Viral Proteins Tube (fluid conveyance) Bacteriophages Electron Microscopy cardiovascular diseases Amino Acid Sequence Peptide sequence Molecular Biology [ SDV ] Life Sciences [q-bio] Tertiary Structure Virus Assembly Virion Computational Biology Nuclear magnetic resonance spectroscopy Cell Biology biology.organism_classification Solid State NMR Protein tertiary structure In vitro Protein Structure Tertiary Crystallography Capsid Tail Tube cardiovascular system Protein folding |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (6), pp.3836-49. ⟨10.1074/jbc.M114.613166⟩ Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2015, 290 (6), pp.3836-49. 〈10.1074/jbc.M114.613166〉 Journal of Biological Chemistry, 2015, 290 (6), pp.3836-49. ⟨10.1074/jbc.M114.613166⟩ Journal of Biological Chemistry, 290(6), 3836. American Society for Biochemistry and Molecular Biology Inc. |
| ISSN: | 0021-9258 1083-351X |
| Popis: | International audience; The majority of known bacteriophages have long tails that serve for bacterial target recognition and viral DNA delivery into the host. These structures form a tube from the viral capsid to the bacterial cell. The tube is formed primarily by a helical array of tail tube protein (TTP) subunits. In phages with a contractile tail, the TTP tube is surrounded by a sheath structure. Here, we report the first evidence that a phage TTP, gp17.1 of siphophage SPP1, self-assembles into long tubes in the absence of other viral proteins. gp17.1 does not exhibit a stable globular structure when monomeric in solution, even if it was confidently predicted to adopt the β-sandwich fold of phage λ TTP. However, Fourier transform infrared and nuclear magnetic resonance spectroscopy analyses showed that its β-sheet content increases significantly during tube assembly, suggesting that gp17.1 acquires a stable β-sandwich fold only after self-assembly. EM analyses revealed that the tube is formed by hexameric rings stacked helicoidally with the same organization and helical parameters found for the tail of SPP1 virions. These parameters were used to build a pseudo-atomic model of the TTP tube. The large loop spanning residues 40-56 is located on the inner surface of the tube, at the interface between adjacent monomers and hexamers. In line with our structural predictions, deletion of this loop hinders gp17.1 tube assembly in vitro and interferes with SPP1 tail assembly during phage particle morphogenesis in bacteria. |
| Databáze: | OpenAIRE |
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