Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves

C. MacKintosh, P. Douglas, C. Lillo

    Research output: Contribution to journalArticle

    111 Citations (Scopus)

    Abstract

    The low-activity, phosphorylated form of nitrate reductase (NR) became activated during purification from spinach (Spinacia oleracea) leaves harvested in the dark. This activation resulted from its separation from an approximately 110-kD nitrate reductase inhibitor protein (NIP). Readdition of NIP inactivated the purified phosphorylated NR, but not the active dephosphorylated form of NR, indicating that the inactivation of NR requires its interaction with NIP as well as phosphorylation. Consistent with this hypothesis, NR that had been inactivated in vitro in the presence of NR kinase, ATP-Mg, and NIP could be reactivated either by dephosphorylation with protein phosphatase 2A or by dissociation of NIP from NR.

    Original languageEnglish
    Pages (from-to)451-457
    Number of pages7
    JournalPlant Physiology
    Volume107
    Issue number2
    DOIs
    Publication statusPublished - 1995

    Cite this

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    title = "Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves",
    abstract = "The low-activity, phosphorylated form of nitrate reductase (NR) became activated during purification from spinach (Spinacia oleracea) leaves harvested in the dark. This activation resulted from its separation from an approximately 110-kD nitrate reductase inhibitor protein (NIP). Readdition of NIP inactivated the purified phosphorylated NR, but not the active dephosphorylated form of NR, indicating that the inactivation of NR requires its interaction with NIP as well as phosphorylation. Consistent with this hypothesis, NR that had been inactivated in vitro in the presence of NR kinase, ATP-Mg, and NIP could be reactivated either by dephosphorylation with protein phosphatase 2A or by dissociation of NIP from NR.",
    author = "C. MacKintosh and P. Douglas and C. Lillo",
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    language = "English",
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    Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves. / MacKintosh, C. ; Douglas, P.; Lillo, C.

    In: Plant Physiology, Vol. 107, No. 2, 1995, p. 451-457.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Identification of a protein that inhibits the phosphorylated form of nitrate reductase from spinach (Spinacia oleracea) leaves

    AU - MacKintosh, C.

    AU - Douglas, P.

    AU - Lillo, C.

    PY - 1995

    Y1 - 1995

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    AB - The low-activity, phosphorylated form of nitrate reductase (NR) became activated during purification from spinach (Spinacia oleracea) leaves harvested in the dark. This activation resulted from its separation from an approximately 110-kD nitrate reductase inhibitor protein (NIP). Readdition of NIP inactivated the purified phosphorylated NR, but not the active dephosphorylated form of NR, indicating that the inactivation of NR requires its interaction with NIP as well as phosphorylation. Consistent with this hypothesis, NR that had been inactivated in vitro in the presence of NR kinase, ATP-Mg, and NIP could be reactivated either by dephosphorylation with protein phosphatase 2A or by dissociation of NIP from NR.

    U2 - 10.1104/pp.107.2.451

    DO - 10.1104/pp.107.2.451

    M3 - Article

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    EP - 457

    JO - Plant Physiology

    JF - Plant Physiology

    SN - 0032-0889

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