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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