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Induction of an ATP-polymerizing enzyme in TMV-infected tobacco and its homology to the human 2′–5′ a synthetase

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Abstract

Several reports have indicated that tobacco carries an enzyme (APE) that, in the presence of poly (rI):(rC), polymerizes ATP to oligoadenylates. This paper demonstrates that the tobacco APE system comprises several proteins (estimated sizes: 32, 42, 67, and 84±10% kD). Only one of these proteins (the “67-kD” form) binds to poly (rI):(rC). This APE form has been purified by affinity chromatography on a synthetic ds-RNA column. Four tobacco proteins, including the purified one, crossreact with antibodies against the human enzyme, 2′–5′ A synthetase. The ATP-binding capacity of some of these proteins has also been demonstrated. The amount of plant oligoadenylates obtained by polymerizing ATP with the purified APE form allows, for the first time, their direct analysis by TLC. The TLC analysis indicated that the oligomer produced by APE is not identical to the 2′–5′ oligoadenylate.

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Authors and Affiliations

  1. Virus Laboratory and the Otto Warburg Center for Biotechnology in Argiculture, The Hebrew University of Jerusalem, Faculty of Agriculture, 76100, Rehovot, Israel

    Naamit Sher, Orit Edelbaum, Zehava Barak, Gideon Grafi, Yehuda Stram & Ilan Sela

  2. Department of Virology, The Weizmann Institute of Science, Rehovot, Israel

    J. Raber

Authors
  1. Naamit Sher
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  2. Orit Edelbaum
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  3. Zehava Barak
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  4. Gideon Grafi
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  5. Yehuda Stram
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  6. J. Raber
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  7. Ilan Sela
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Sher, N., Edelbaum, O., Barak, Z. et al. Induction of an ATP-polymerizing enzyme in TMV-infected tobacco and its homology to the human 2′–5′ a synthetase. Virus Genes 4, 27–39 (1990). https://doi.org/10.1007/BF00308563

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  • DOI: https://doi.org/10.1007/BF00308563

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