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

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成果类型:
期刊论文
作者:
He, Lixiong;Ban, Yusuke;Miyata, Shin-Chi;Kitashiba, Hiroyasu;Moriguchi, Takaya*
通讯作者:
Moriguchi, Takaya
作者机构:
[Miyata, Shin-Chi; Moriguchi, Takaya; He, Lixiong] Natl Inst Fruit Tree Sci, Ibaraki, Japan.
[He, Lixiong] Hunan Agr Univ, Coll Biosci & Biotechnol, Changsha 410128, Hunan Province, Peoples R China.
[Ban, Yusuke; Moriguchi, Takaya] Univ Tsukuba, Grad Sch Life & Environm Sci, Tsukuba 3058572, Japan.
[Kitashiba, Hiroyasu] Tohoku Univ, Grad Sch Agr Sci, Sendai, Miyagi 9818555, Japan.
通讯机构:
[Moriguchi, Takaya] N
Natl Inst Fruit Tree Sci, Ibaraki, Japan.
语种:
英文
关键词:
ACL5;Apple (Malus sylvestris var. domestica);Polyamine;Yeast two-hybrid
期刊:
Biochemical and Biophysical Research Communications
ISSN:
0006-291X
年:
2008
卷:
366
期:
1
页码:
162-167
基金类别:
This work was supported in part by Grants-in-Aid from the Japan Society for the Promotion of Science (JSPS). We thank Drs I. Suzuki, Y. Shiraiwa, H. Ezura, and T. Mizoguchi (University of Tsukuba, Japan) and Dr. K. Sugimoto (National Institute of Agrobiological Sciences) for their technical suggestions. We thank Dr. S. Terakami (University of Tsukuba, Japan) for his technical assistance with the computational analysis.
机构署名:
本校为其他机构
院系归属:
生物科学技术学院
摘要:
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-adenosy...

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