Abstract:Abstract: SEPALLATA3 (SEP3) protein plays important roles in many aspects of the reproductive growth in dicotyledonous plants, including formation of flower meristems and organs. However, the molecular mechanism of floral organ formation in monocotyledon plants is not very clear yet. To reveal the structural characteristics of SEP3 as well as its relationship between the potential polymer formation and biological functions, a series of experiments using the monocotyledon plant Bambusa oldhami as the material were performed. Different protein domains were constructed and soluble expressions were obtained in prokaryotic E. coil system. The target proteins were purified through one-step nickel-affinity approach. Gelfiltration assay indicated that K domain was involved in the tetrameric formation under the testing conditions. Furthermore, the involvement of the K domain in the polymer formation was verified by yeast two-hybrid system. Thus an effective approach to express and purify Bambusa oldhami SEP3 (BoSEP3) protein was established. Confirmation of BoSEP3 as a tetramer in vitro facilitates a functional and structural analysis in the future.
引用本文:
吴文魁, 周佳平, 林新春, 徐英武, 曹友志. 绿竹SEP3-like蛋白表达纯化以及不同结构域互作研究[J]. 生命科学研究, 2016, 20(5): 389-394.
WU Wen-Kui, ZHOU Jia-Ping, LIN Xin-Chun, XU Ying-Wu, CAO You-Zhi. Expression and Purification of Bambusa oldhami SEP3 Protein in Vitro and the Yeast Two-hybrid Assay Between Different Domains. Life Science Research, 2016, 20(5): 389-394.