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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(s) -
Lukashina Elena,
Badun Gennady,
Fedorova Natalia,
Ksenofontov Alexander,
Nemykh Maria,
Serebryakova Marina,
Mukhamedzhanova Anna,
Karpova Olga,
Rodionova Nina,
Baratova Lyudmila,
Dobrov Evgeny
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07408.x
Subject(s) - potato virus x , microbiology and biotechnology , protein subunit , chemistry , coat protein , gene , virology , biology , rna , biochemistry
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 ∼ 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 β‐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 β‐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.