Apple aminopropyl transferase, MdACL5 interacts with putative elongation factor 1-α and S-adenosylmethionine synthase revealed

Lixiong He, Yusuke Ban, Shin ichi Miyata, Hiroyasu Kitashiba, Takaya Moriguchi

    Research output: Contribution to journalArticlepeer-review

    5 Citations (Scopus)

    Abstract

    Several lines of evidence suggest different allocations of the physiological roles of aminopropyl transferase genes, SPMS and ACL5 in plants. To get deeper insights into the physiological role of apple ACL5 (MdACL5), we performed yeast two-hybrid (Y2H) assay to identify proteins which interact with MdACL5. After intense screening processes, including the swapping of the bait and prey vectors and in vitro coimmunoprecipitation, we identified three MdACL5-interacting proteins: putative translation elongation factor 1A (eEF-1A), putative S-adenosyl-l-methionine synthetase (SAMS) and an unknown protein. Results from Y2H and RNA gel blot analysis suggested the involvement of MdACL5 and eEF-1A or SAMS complexes in the plant growth and development of the organized tissues and/or organs.

    Original languageEnglish
    Pages (from-to)162-167
    Number of pages6
    JournalBiochemical and biophysical research communications
    Volume366
    Issue number1
    DOIs
    Publication statusPublished - 2008 Feb 1

    Keywords

    • ACL5
    • Apple (Malus sylvestris var. domestica)
    • Polyamine
    • Yeast two-hybrid

    ASJC Scopus subject areas

    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Cell Biology

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