Expression and biochemical analyses of the recombinant potato virus X 25K movement protein

Research output: Contribution to journal › Article › Research › peer review

Authors

  • N. O. Kalinina
  • O. N. Fedorkin
  • O. V. Samuilova
  • E. Maiss
  • T. Korpela
  • S. Yu Morozov
  • J. G. Atabekov

Research Organisations

External Research Organisations

  • Lomonosov Moscow State University
  • University of Turku
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Details

Original languageEnglish
Pages (from-to)75-78
Number of pages4
JournalFEBS letters
Volume397
Issue number1
Publication statusPublished - 2 Dec 1999

Abstract

The 25K movement protein (MP) of potato virus X (PVX) is encoded by the 5'-proximal gene of three overlapping MP genes forming a 'triple gene block'. The PVX 25K MP (putative NTPase-helicase) has been synthesized in Escherichia coli as a recombinant containing a six-histidine tag at the amino terminus. The His-tagged 25K protein was purified in a one-column Ni-chelate affinity chromatography procedure. In the absence of any other viral factors, this protein had obvious Mg2+-dependent ATPase activity, which was stimulated slightly (1.7-1.9-fold) by various polynucleotides. Like other viral proteins possessing ATPase-helicase motifs and many plant viral movement proteins, the PVX 25K MP was able to bind nucleic acids in vitro. The RNA binding activity of the 25K MP was pronounced only at very low salt concentrations and was independent of its ATPase activity.

Keywords

    ATPase, Movement protein, Plant RNA virus, RNA binding

ASJC Scopus subject areas

Cite this

Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. / Kalinina, N. O.; Fedorkin, O. N.; Samuilova, O. V. et al.
In: FEBS letters, Vol. 397, No. 1, 02.12.1999, p. 75-78.

Research output: Contribution to journal › Article › Research › peer review

Kalinina, NO, Fedorkin, ON, Samuilova, OV, Maiss, E, Korpela, T, Morozov, SY & Atabekov, JG 1999, 'Expression and biochemical analyses of the recombinant potato virus X 25K movement protein', FEBS letters, vol. 397, no. 1, pp. 75-78. https://doi.org/10.1016/S0014-5793(96)01138-6
Kalinina, N. O., Fedorkin, O. N., Samuilova, O. V., Maiss, E., Korpela, T., Morozov, S. Y., & Atabekov, J. G. (1999). Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. FEBS letters, 397(1), 75-78. https://doi.org/10.1016/S0014-5793(96)01138-6
Kalinina NO, Fedorkin ON, Samuilova OV, Maiss E, Korpela T, Morozov SY et al. Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. FEBS letters. 1999 Dec 2;397(1):75-78. doi: 10.1016/S0014-5793(96)01138-6
Kalinina, N. O. ; Fedorkin, O. N. ; Samuilova, O. V. et al. / Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. In: FEBS letters. 1999 ; Vol. 397, No. 1. pp. 75-78.
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abstract = "The 25K movement protein (MP) of potato virus X (PVX) is encoded by the 5'-proximal gene of three overlapping MP genes forming a 'triple gene block'. The PVX 25K MP (putative NTPase-helicase) has been synthesized in Escherichia coli as a recombinant containing a six-histidine tag at the amino terminus. The His-tagged 25K protein was purified in a one-column Ni-chelate affinity chromatography procedure. In the absence of any other viral factors, this protein had obvious Mg2+-dependent ATPase activity, which was stimulated slightly (1.7-1.9-fold) by various polynucleotides. Like other viral proteins possessing ATPase-helicase motifs and many plant viral movement proteins, the PVX 25K MP was able to bind nucleic acids in vitro. The RNA binding activity of the 25K MP was pronounced only at very low salt concentrations and was independent of its ATPase activity.",
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AU - Kalinina, N. O.

AU - Fedorkin, O. N.

AU - Samuilova, O. V.

AU - Maiss, E.

AU - Korpela, T.

AU - Morozov, S. Yu

AU - Atabekov, J. G.

N1 - Funding Information: Acknowledgements." We wish to thank D.A. Zelenina for labeled transcripts. The work was funded in part by the Russian Foundation for Basic Research and the German Ministry of Agriculture.

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Y1 - 1999/12/2

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