Journal
FEBS JOURNAL
Volume 276, Issue 23, Pages 7006-7015Publisher
WILEY
DOI: 10.1111/j.1742-4658.2009.07408.x
Keywords
coat protein; Potato virus X; structural alterations; triple gene block 1 protein; tritium planigraphy
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Funding
- Russian Foundation for Basic Research [09-04-01373, 06-03-33036]
- Russian Federation [MK-5272.2008.3]
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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 similar to 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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