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Formation of protein complexes containing plant virus movement protein TGBp3 is necessary for its intracellular trafficking
Authors:Shemyakina Elena A  Erokhina Tatiana N  Gorshkova Elena N  Schiemann Joachim  Solovyev Andrey G  Morozov Sergey Yu
Institution:
  • a Department of Virology, Biological Faculty, Moscow State University, Moscow 119992, Russia
  • b M. M. Shemyakin & Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya Str., Moscow 117997, Russia
  • c A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119992 Moscow, Russia
  • d Julius Kühn Institute (JKI), Federal Research Centre for Cultivated Plants, Institute for Biosafety of Genetically Modified Plants, Erwin-Baur-Str. 27, 06484 Quedlinburg, Germany
  • e Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, Timiryazevskaya 42, 127550 Moscow, Russia
  • Abstract:Cell-to-cell movement of Poa semilatent virus (genus Hordeivirus) in infected plants is mediated by three viral ‘triple gene block’ (TGB) proteins. One of those termed TGBp3 is an integral membrane protein essential for intracellular transport of other TGB proteins and viral genomic RNA to plasmodesmata. TGBp3 targeting to plasmodesmata-associated sites is believed to involve an unconventional mechanism which does not employ endoplasmic reticulum-derived transport vesicles. Previously TGBp3 has been shown to contain a composite transport signal consisting of the central hydrophilic protein region which includes a conserved pentapeptide YQDLN and the C-terminal transmembrane segment. This study demonstrates that these TGBp3 structural elements have distinct functions in protein transport. The YQDLN-containing region is essential for TGBp3 incorporation into high-molecular-mass protein complexes. In transient expression assay formation of such complexes is necessary for entering the TGBp3-specific pathway of intracellular transport and protein delivery to plasmodesmata-associated sites. In virus-infected plants TGBp3 is also found predominantly in the form of high-molecular-mass complexes. When the complex-formation function of YQDLN-containing region is disabled by a mutation, targeting to plasmodesmata-associated sites can be complemented by a heterologous peptide capable of formation multimeric complexes. The C-terminal transmembrane segment is found to be an essential signal of TGBp3 intracellular transport to peripheral sites.
    Keywords:Plant virus  Movement protein  Intracellular transport  Protein complex
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