National Key Laboratory of Crop Genetic Improvement, National Center of Plant Gene Research (Wuhan), Huazhong Agricultural University, Wuhan, 430070, China.
Protein Cell. 2011 Jan;2(1):55-63. doi: 10.1007/s13238-011-1010-9. Epub 2011 Feb 20.
The importance of NAC (named as NAM, ATAF1, 2, and CUC2) proteins in plant development, transcription regulation and regulatory pathways involving protein-protein interactions has been increasingly recognized. We report here the high resolution crystal structure of SNAC1 (stress-responsive NAC) NAC domain at 2.5 Å. Although the structure of the SNAC1 NAC domain shares a structural similarity with the reported structure of the ANAC NAC1 domain, some key features, especially relating to two loop regions which potentially take the responsibility for DNA-binding, distinguish the SNAC1 NAC domain from other reported NAC structures. Moreover, the dimerization of the SNAC1 NAC domain is demonstrated by both soluble and crystalline conditions, suggesting this dimeric state should be conserved in this type of NAC family. Additionally, we discuss the possible NAC-DNA binding model according to the structure and reported biological evidences.
NAC（命名为 NAM、ATAF1、2 和 CUC2）蛋白在植物发育、转录调控以及涉及蛋白-蛋白相互作用的调控途径中的重要性已得到越来越多的认可。我们在此报道了 SNAC1（应激响应 NAC）NAC 结构域的高分辨率晶体结构，分辨率为 2.5Å。尽管 SNAC1 NAC 结构域的结构与已报道的 ANAC NAC1 结构域的结构具有相似性，但一些关键特征，特别是与两个潜在负责 DNA 结合的环区有关的特征，将 SNAC1 NAC 结构域与其他报道的 NAC 结构区分开来。此外，SNAC1 NAC 结构域的二聚化通过可溶性和晶体条件得到证实，表明这种二聚体状态应该在这种类型的 NAC 家族中保守。此外，我们根据结构和已报道的生物学证据讨论了可能的 NAC-DNA 结合模型。
