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Biochemistry (Moscow)

, Volume 73, Issue 1, pp 50–55 | Cite as

Oligomerization of the potato virus X 25-kD movement protein

  • A. D. Leshchiner
  • E. A. Minina
  • D. V. Rakitina
  • V. K. Vishnichenko
  • A. G. Solovyev
  • S. Yu. Morozov
  • N. O. KalininaEmail author
Article

Abstract

A 25-kD movement protein (25K protein) encoded by the first gene of the potexvirus Potato virus X triple gene block of transport genes is essential for the viral movement in infected plants. The 25K protein belongs to superfamily 1 of NTPase/helicases and exhibits in vitro RNA helicase, Mg2+-dependent NTPase, and RNA-binding activities. In the present work, the ability of 25K protein for homologous interactions was studied using the yeast two-hybrid system, protein chemical cross-linking in the presence of glutaraldehyde, far-Western blotting, and ultracentrifugation in sucrose density gradients. The 25K protein was shown to form homodimers and homooligomers. Sites of homologous protein-protein interactions were found in both the N- and C-terminal portions of the protein.

Key words

potato virus X movement protein oligomerization yeast two-hybrid system glutaraldehyde 

Abbreviations

AD, BD

activator and DNA-binding domains of the yeast Ga14 protein, respectively

GA

glutaraldehyde

PVX

potato virus X

TGB(1–3) proteins

proteins encoded by the genes (1–3) of the triple gene block

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Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  • A. D. Leshchiner
    • 1
    • 2
  • E. A. Minina
    • 3
  • D. V. Rakitina
    • 1
  • V. K. Vishnichenko
    • 2
  • A. G. Solovyev
    • 1
    • 2
  • S. Yu. Morozov
    • 1
  • N. O. Kalinina
    • 1
    Email author
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Institute of Agricultural BiotechnologyRussian Academy of Agricultural SciencesMoscowRussia
  3. 3.Shemyakin and Ovchinnikov Institute of Bioorganic ChemistryRussian Academy of SciencesMoscowRussia

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