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

Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review

Autorschaft

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

Organisationseinheiten

Externe Organisationen

  • Lomonosov Moscow State University
  • University of Turku
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Details

OriginalspracheEnglisch
Seiten (von - bis)75-78
Seitenumfang4
FachzeitschriftFEBS letters
Jahrgang397
Ausgabenummer1
PublikationsstatusVeröffentlicht - 2 Dez. 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.

ASJC Scopus Sachgebiete

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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, Jahrgang 397, Nr. 1, 02.12.1999, S. 75-78.

Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › 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, Jg. 397, Nr. 1, S. 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 Dez 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 ; Jahrgang 397, Nr. 1. S. 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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T1 - Expression and biochemical analyses of the recombinant potato virus X 25K movement protein

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.

PY - 1999/12/2

Y1 - 1999/12/2

N2 - 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.

AB - 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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