Journal of Integrative Agriculture ›› 2023, Vol. 22 ›› Issue (3): 752-761.DOI: 10.1016/j.jia.2022.08.069

• • 上一篇    下一篇

StOFP20通过和TONNEAU1 Recruiting Motif 蛋白互作来调控块茎形状

  

  • 收稿日期:2020-10-22 接受日期:2021-12-27 出版日期:2023-03-20 发布日期:2021-12-27

StOFP20 regulates tuber shape and interacts with TONNEAU1 Recruiting Motif proteins in potato

AI Ju*, WANG Ye*, YAN Ya-wen, LI Chen-xiao, LUO Wei, MA Ling, SHANG Yi, GAO Dong-li#    

  1. Yunnan Key Laboratory of Potato Biology, the CAAS-YNNU-YINMORE Joint Academy of Potato Science, Yunnan Normal University, Kunming 650500, P.R.China

  • Received:2020-10-22 Accepted:2021-12-27 Online:2023-03-20 Published:2021-12-27
  • About author:AI Ju, E-mail: 1605664871@qq.com; WANG Ye, E-mail: 1442724630@qq.com; #Correspondence GAO Dong-li, Tel/Fax: +86-871-65941383, E-mail: gdongli@126.com * These authors contributed equally to this study.
  • Supported by:
    This work was supported by the National Natural Science Foundation of China (32060684) and the Academician Workstation of Yunnan, China (202105AF150028).

摘要:

OFP蛋白是植物特有的蛋白家族,参与植物生长发育的多个过程。在番茄中,OFP20通过和TRM蛋白互作来调控果实形状。本研究发现敲除StOFP20使二倍体马铃薯C151的薯形由圆形变为椭圆形,从而证实了StOFP20调控薯形的功能。StOFP20的表达在块茎起始期表达最高,随着薯块发育,其表达逐渐降低。为了揭示StOFP20的调控机制,我们在马铃薯中找到了23个TRM基因,其中23个基因在C151中成功扩增。酵母双杂交和荧光素酶互补实验结果表明StOFP203个TRM蛋白互作。缺失StOFP20中的OVATE结构域使蛋白间不能互作,缺失TRM蛋白中的M8结构域则对蛋白互作产生不同的影响。总之,StOFP20和SlOFP20均能和TRM蛋白互作,但是互作蛋白并不完全相同,暗示着它们的调控机制也可能不尽相同。

Abstract:

The OVATE family proteins (OFPs) are plant-specific proteins that modulate diverse aspects of plant growth and development.  In tomato, OFP20 has been shown to interact with TONNEAU1 Recruiting Motif (TRM) proteins to regulate fruit shape.  In this study, we demonstrated that the mutation of StOFP20 caused a shift from round to oval shaped tubers in a diploid accession C151, supporting the role of StOFP20 in controlling tuber shape.  Its expression reached a maximum in the tuber initiation stage and then decreased as the tuber develops.  To help elucidate the mechanism of tuber shape regulation by StOFP20, 27 TONNEAU1 Recruiting Motif (TRM) proteins were identified and 23 of them were successfully amplified in C151.  A yeast two-hybrid assay identified three TRM proteins that interacted with StOFP20, which was confirmed by firefly luciferase complementation in tobacco leaves.  The OVATE domain was indispensable for the interactions, while the necessity of the M10 motif in TRM proteins varied among the interactions between StOFP20 and the three TRMs.  In summary, both StOFP20 and SlOFP20 directed interactions with TRM proteins, but the corresponding interactants were not completely consistent, implying that they exert regulatory roles through mechanisms that are only partially overlapping.  

Key words: potato , tuber shape , OFP20 , TRM