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  • Title: Tritium planigraphy study of structural alterations in the coat protein of Potato virus X induced by binding of its triple gene block 1 protein to virions.
    Author: Lukashina E, Badun G, Fedorova N, Ksenofontov A, Nemykh M, Serebryakova M, Mukhamedzhanova A, Karpova O, Rodionova N, Baratova L, Dobrov E.
    Journal: FEBS J; 2009 Dec; 276(23):7006-15. PubMed ID: 19860836.
    Abstract:
    Alterations in Potato virus X (PVX) coat protein structure after binding of the protein, encoded by the first gene of PVX triple gene block (triple gene block 1 protein, TGBp1), to the virions were studied using tritium planigraphy. Previously, it has been shown that TGBp1 molecules interact with the PVX particle end, containing the 5'-terminus of PVX RNA, and that this interaction results in a strong decrease in virion stability and its transformation to a translationally active state. In this work, it has been shown that the interaction of TGBp1 with PVX virions leads to an increase of approximately 50% in tritium label incorporation into the 176-198 segment of the 236-residue-long PVX coat protein subunit, with some decrease in label incorporation into the N-terminal coat protein region. According to the new 'sandwich' variant of our recently proposed model of the three-dimensional structure of the intravirus PVX coat protein, the 176-198 segment is assigned to the beta-sheet region located at the subunit surface, presumably participating in coat protein interactions with the intravirus RNA and/or in protein-protein interactions, whereas the N-terminal coat protein region corresponds to the other part of the same beta-sheet. For the remaining segments of the PVX coat protein subunit, no significant difference between tritium incorporation into untreated and TGBp1-treated PVX was observed. A detailed description of the 'sandwich' version of the intravirus PVX coat protein model is presented.
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