2008年2月
Apple aminopropyl transferase, MdACL5 interacts with putative elongation factor 1-alpha and S-adenosylmethionine synthase revealed
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- 巻
- 366
- 号
- 1
- 開始ページ
- 162
- 終了ページ
- 167
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.bbrc.2007.11.099
- 出版者・発行元
- ACADEMIC PRESS INC ELSEVIER SCIENCE
Several lines of evidence suggest different allocations of the physiological roles of aminopropyl tranferase 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. (c) 2007 Elsevier Inc. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.bbrc.2007.11.099
- ISSN : 0006-291X
- PubMed ID : 18053797
- Web of Science ID : WOS:000252392400026