The degradation of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase into the 44-kDa fragment in the lysates of chloroplasts incubated in darkness

Norimoto Kokubun, Hiroyuki Ishida, Amane Makino, Tadahiko Mae

    Research output: Contribution to journalArticlepeer-review

    30 Citations (Scopus)

    Abstract

    Lysates of chloroplasts isolated from naturally senescing wheat leaves were incubated in darkness. The 44-kDa fragment, lacking the N-terminal-side portion of the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase (LSU), was found by immunoblotting with the LSU site-specific antibodies. Analysis of its N-terminal amino acid sequence indicated that the LSU was specifically cleaved at the peptide bond between Phe-40 and Arg-41. The site was located on the surface of the molecule and faced outward. Such cleavage of the LSU has not been previously reported. It is indicated that the cleavage was triggered by an unknown protease existing in chloroplasts.

    Original languageEnglish
    Pages (from-to)1390-1394
    Number of pages5
    JournalPlant and Cell Physiology
    Volume43
    Issue number11
    DOIs
    Publication statusPublished - 2002 Nov 1

    Keywords

    • Chloroplast
    • Protease
    • Protein degradation
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco, EC 4.1.1.39)
    • Wheat (Triticum aestivum)

    ASJC Scopus subject areas

    • Physiology
    • Plant Science
    • Cell Biology

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