tailieunhanh - Báo cáo khoa học: Tritium planigraphy study of structural alterations in the coat protein ofPotato virus Xinduced by binding of its triple gene block 1 protein to virions

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 Elena Lukashina1, Gennady Badun2, Natalia Fedorova1, Alexander Ksenofontov1, Maria Nemykh1, Marina Serebryakova3, Anna Mukhamedzhanova4, Olga Karpova4, Nina Rodionova4, Lyudmila Baratova1 and Evgeny Dobrov1 1 2 3 4 . Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russia Department of Chemistry, Moscow State University, Russia Institute of Physico-Chemical Medicine, Federal Agency for Health Care and Social Development, Moscow, Russia Department of Biology, Moscow State University, Russia Keywords coat protein; Potato virus X; structural alterations; triple gene block 1. | 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 Elena Lukashina1 Gennady Badun2 Natalia Fedorova1 Alexander Ksenofontov1 Maria Nemykh1 Marina Serebryakova3 Anna Mukhamedzhanova4 Olga Karpova4 Nina Rodionova4 Lyudmila Baratova1 and Evgeny Dobrov1 1 . Belozersky Institute of Physico-ChemicalBiology Moscow State University Russia 2 Department of Chemistry Moscow State University Russia 3 Institute of Physico-ChemicalMedicine FederalAgency for Health Care and SocialDevelopment Moscow Russia 4 Department of Biology Moscow State University Russia Keywords coat protein Potato virus X structural alterations triple gene block 1 protein tritium planigraphy Correspondence E. Dobrov Department of Biochemistry of Plant Viruses . Belozersky Institute of Physico-ChemicalBiology Moscow State University Leninskie Gory Moscow 119991 Russia Fax 7 495 9393181 Tel 7 495 9393360 E-mail dobrov@ Received 25 July 2009 revised 16 September 2009 accepted 28 September 2009 doi 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 threedimensional .

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