- Point mutation in calcium-binding domain of mouse polyomavirus VP1 pr…
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Point mutation in calcium-binding domain of mouse polyomavirus VP1 protein does not prevent virus-like particle formation, but changes VP1 interactions with Saccharomyces cerevisiae cell structures

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    SYSNO ASEP0027836
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JOstatní články
    TitlePoint mutation in calcium-binding domain of mouse polyomavirus VP1 protein does not prevent virus-like particle formation, but changes VP1 interactions with Saccharomyces cerevisiae cell structures
    TitleBodová mutace ve vápník-vážící doméně VP1 proteinu myšího polyomaviru nebrání tvorbě viru podobných částic ale pozměňuje interakce VP1 s buněčnými strukturami Saccharomyces cerevisiae
    Author(s) Adamec, T. (CZ)
    Palková, Zdena (CZ)
    Velková, K. (CZ)
    Štokrová, Jitka (UMG-J)
    Forstová, J. (CZ)
    Source TitleFEMS Yeast Research. - : Oxford University Press - ISSN 1567-1356
    Roč. 5, 4-5 (2005), s. 331-340
    Number of pages10 s.
    Languageeng - English
    CountryNL - Netherlands
    Keywordspolyomavirus VP1 ; Saccharomyces cerevisiae ; heterologous expression
    Subject RIVEB - Genetics ; Molecular Biology
    R&D ProjectsGA204/03/0593 GA ČR - Czech Science Foundation (CSF)
    CEZAV0Z5052915 - UMG-J
    AnnotationThe mouse polyomavirus gene for the major structural protein, VP1, with point mutation in the calcium-binding pocket (VP1Ala), was expressed in Saccharomyces cerevisiae and in baculovirus expression systém. Surprisingly, VP1Ala forms virus-like particles (VLPs) in nuclei of both yeast and insect cells. VP1Ala – VLPs produced in S. cerevisiae are unstable and, unlike wild type VP1 (VP1wt)- VLPs, they dissasemble during the purification procedure and storage. In contrast to VP1wt , VP1Ala does not interact with the yeast mitotic spindle. Nevertheless, both wild type and mutated VP1 inhibit yeast cell growth and this inhibition is c-AMP dependent. The production of VP1Ala and VP1Ala -VLPs in insect cells also revealed differences in their interactions with cellular proteins(s). Thus, the mutation in the VP1 calcium pocket alters the stability and surface conformation of VLPs rather than the ability of VP1 to self-assemble.
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2006
Number of the records: 1  

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