Selected article for: "acute severe and long functional"

Author: Zúñiga, Sonia; Sola, Isabel; Moreno, Jose L.; Sabella, Patricia; Plana-Durán, Juan; Enjuanes, Luis
Title: Coronavirus nucleocapsid protein is an RNA chaperone
  • Cord-id: abriptpb
  • Document date: 2007_1_20
  • ID: abriptpb
    Snippet: RNA chaperones are nonspecific nucleic acid binding proteins with long disordered regions that help RNA molecules to adopt its functional conformation. Coronavirus nucleoproteins (N) are nonspecific RNA-binding proteins with long disordered regions. Therefore, we investigated whether transmissible gastroenteritis coronavirus (TGEV) N protein was an RNA chaperone. Purified N protein enhanced hammerhead ribozyme self-cleavage and nucleic acids annealing, which are properties that define RNA chaper
    Document: RNA chaperones are nonspecific nucleic acid binding proteins with long disordered regions that help RNA molecules to adopt its functional conformation. Coronavirus nucleoproteins (N) are nonspecific RNA-binding proteins with long disordered regions. Therefore, we investigated whether transmissible gastroenteritis coronavirus (TGEV) N protein was an RNA chaperone. Purified N protein enhanced hammerhead ribozyme self-cleavage and nucleic acids annealing, which are properties that define RNA chaperones. In contrast, another RNA-binding protein, PTB, did not show these activities. N protein chaperone activity was blocked by specific monoclonal antibodies. Therefore, it was concluded that TGEV N protein is an RNA chaperone. In addition, we have shown that purified severe acute respiratory syndrome (SARS)-CoV N protein also has RNA chaperone activity. In silico predictions of disordered domains showed a similar pattern for all coronavirus N proteins evaluated. Altogether, these data led us to suggest that all coronavirus N proteins might be RNA chaperones.

    Search related documents:
    Co phrase search for related documents
    • accurate rapid and acute respiratory syndrome: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25
    • acid bind protein and acute respiratory syndrome: 1, 2
    • acid chaperone and acute respiratory syndrome: 1, 2, 3
    • acidic domain and acute respiratory syndrome: 1, 2
    • activity result and acute respiratory syndrome: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12
    • acute respiratory syndrome and local folding: 1