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Biochemistry (Moscow)

, Volume 77, Issue 9, pp 1072–1081 | Cite as

In vitro phosphorylation of the N-terminal half of hordeivirus movement protein

  • V. V. Makarov
  • A. Y. Iconnikova
  • M. A. Guseinov
  • V. K. Vishnichenko
  • N. O. KalininaEmail author
Article

Abstract

The N-terminal half of TGB1 movement protein of poa semilatent hordeivirus, which forms a ribonucleoprotein complex involved in movement of the viral genome in the plant, and its two domains, NTD and ID, are phosphorylated in vitro by a fraction enriched in cell walls from Nicotiana benthamiana. Using a set of protein kinase inhibitors with different specificities, it was found that enzymes possessing activities of casein kinase 1, protein kinase A, and protein kinase C are involved in phosphorylation. Commercial preparations of protein kinases A and C are able to phosphorylate in vitro recombinant proteins corresponding to the N-terminal half of the protein and its domains NTD and ID. Phosphorylation of the NTD has no effect on the efficiency and character of its binding to RNA. However, phosphorylation of the ID leads to a decrease in its RNA-binding activity and in the ability for homological protein-protein interactions.

Key words

hordeivirus TGB1 movement protein domain phosphorylation RNA-binding activity 

Abbreviations

BaMV

bamboo mosaic virus

CK

casein kinase

DTT

dithiothreitol

ID

internal domain

IPTG

isopropyl-β-D-thiogalactopyranoside

MP

movement protein

NCM

nitrocellulose membrane

Ni-NTA-agarose

Ni2+-nitrilotriacetate agarose

N63K

N-terminal protein half including the NTD and ID

NTD

N-terminal domain

PK

protein kinase

PSLV

poa semilatent virus

PVA

potato virus A

PVX

potato virus X

RNP

ribonucleoprotein

TGB (1–3)

triple gene block encoded proteins (1–3)

TMV

tobacco mosaic virus

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Copyright information

© Pleiades Publishing, Ltd. 2012

Authors and Affiliations

  • V. V. Makarov
    • 1
    • 2
  • A. Y. Iconnikova
    • 1
    • 2
  • M. A. Guseinov
    • 3
  • V. K. Vishnichenko
    • 3
  • N. O. Kalinina
    • 1
    Email author
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Biological FacultyLomonosov Moscow State UniversityMoscowRussia
  3. 3.Institute of Agricultural BiotechnologyRussian Academy of Agricultural SciencesMoscowRussia

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