Apple aminopropyl transferase, MdACL5 interacts with putative elongation factor 1-alpha and S-adenosylmethionine synthase [corrected].

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.

• Authors: Lixiong He, Yusuke Ban, Shin-Ichi Miyata, Hiroyasu Kitashiba, Takaya Moriguchi
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 366 Issue 1 Pg. 162-7 (Feb 01 2008) ISSN: 1090-2104 [Electronic] United States
• PMID: 18053797 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Multienzyme Complexes
• Peptide Elongation Factor 1
• Spermidine Synthase
• Methionine Adenosyltransferase

Topics

• Binding Sites
• Malus (enzymology)
• Methionine Adenosyltransferase (metabolism)
• Multienzyme Complexes (metabolism)
• Peptide Elongation Factor 1 (metabolism)
• Protein Binding
• Protein Interaction Mapping
• Spermidine Synthase (metabolism)