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Mutagenic analysis of Potato Virus X movement protein (TGBp1) and the coat protein (CP): in vitro TGBp1-CP binding and viral RNA translation activation

Molecular plant pathology, 2008-01, Vol.9 (1), p.37-44 [Peer Reviewed Journal]

2008 INIST-CNRS ;ISSN: 1464-6722 ;EISSN: 1364-3703 ;DOI: 10.1111/j.1364-3703.2007.00445.x ;PMID: 18705882

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  • Title:
    Mutagenic analysis of Potato Virus X movement protein (TGBp1) and the coat protein (CP): in vitro TGBp1-CP binding and viral RNA translation activation
  • Author: ZAYAKINA, OLGA ; ARKHIPENKO, MARINA ; KOZLOVSKY, STANISLAV ; NIKITIN, NIKOLAI ; SMIRNOV, ALEXANDER ; SUSI, PETRI ; RODIONOVA, NINA ; KARPOVA, OLGA ; ATABEKOV, JOSEPH
  • Subjects: Amino Acid Motifs ; Capsid Proteins - genetics ; Mutagenesis ; Original ; Phosphorylation ; Plant Viral Movement Proteins - genetics ; Potexvirus - genetics ; Potexvirus - physiology ; Protein Binding ; Protein Biosynthesis ; Recombinant Proteins - genetics ; RNA, Viral - genetics ; RNA-Binding Proteins - genetics ; Sequence Deletion ; Virus Assembly
  • Is Part Of: Molecular plant pathology, 2008-01, Vol.9 (1), p.37-44
  • Description: Previously, we have shown that encapsidated Potato virus X (PVX) RNA was non-translatable in vitro, but could be converted into a translatable form by binding of the PVX movement protein TGBp1 to one end of the virion or by coat protein (CP) phosphorylation. Here, a mutagenic analysis of PVX CP and TGBp1 was used to identify the regions involved in TGBp1-CP binding and translational activation of PVX RNA by TGBp1. It was found that the C-terminal (C-ter) 10/18 amino acids region was not essential for virus-like particle (VP) assembly from CP and RNA. However, the VPs assembled from the CP lacking C-ter 10/18 amino acids were incapable of TGBp1 binding and being translationally activated. It was suggested that the 10-amino-acid C-ter regions of protein subunits located at one end of a polar helical PVX particle contain a domain accessible to TGBp1 binding and PVX remodelling. The non-translatable particles assembled from the C-ter mutant CP could be converted into a translatable form by CP phosphorylation. The TGBp1-CP binding activity was preserved unless a conservative motif IV was removed from TGBp1. By contrast, TGBp1-dependent activation of PVX RNA translation was abolished by deletions of various NTPase/helicase conservative motifs and their combinations. The motif IV might be essential for TGBp1-CP binding, but insufficient for PVX RNA translation activation. The evidence to discriminate between these two events, i.e. TGBp1 binding to the CP-helix and TGBp1-dependent RNA translation activation, is discussed.
  • Publisher: Oxford, UK: Oxford, UK : Blackwell Publishing Ltd
  • Language: English;Russian
  • Identifier: ISSN: 1464-6722
    EISSN: 1364-3703
    DOI: 10.1111/j.1364-3703.2007.00445.x
    PMID: 18705882
  • Source: MEDLINE
    PubMed Central
    Alma/SFX Local Collection
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