論文

査読有り
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
  • Lixiong He
  • ,
  • Yusuke Ban
  • ,
  • Shin-ichi Miyata
  • ,
  • Hiroyasu Kitashiba
  • ,
  • Takaya Moriguchi

366
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
DOI
https://doi.org/10.1016/j.bbrc.2007.11.099
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/18053797
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000252392400026&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/j.bbrc.2007.11.099
  • ISSN : 0006-291X
  • PubMed ID : 18053797
  • Web of Science ID : WOS:000252392400026

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