中文摘要：

为阐明开花负调因子BjSVP（源于种子春化型作物芥菜）与BoFLC（源于绿体春化作物甘蓝）异源聚合后在开花调控路径中的互作机制，从芥菜酵母重组质粒pGADT7．SjSVP分别亚克隆含MI、MIK、K、IKC、KC、IK、IKlLlK2L2、IKlLlK2、IKlLl、IKl、I结构域的11个SVP截短体（sjsve,al～BjSVPAll），构建猎物质粒pGADT7—13jSVPAl～pGADT7一BjSVPAll并转化酵母Y187菌；从甘蓝中克隆了BoFLC和BoFLCzq基因，构建诱饵质粒pGBKT7．BoFLC、pGBKT7．BoFLCzq并转化酵母Y2HGold菌。酵母双杂交表明：芥菜BjSVP能与甘蓝BoFLC相互作用，在QDO／X／A培养基上长出蓝色菌落，激活酵母报告基因AURl-C、HIS3、ADE2、MELl。截短体BjSVPA2～BjSVPA5也能与BoFLC相互作用，而BjSVPA7～BiSVPAll不能与BoFLC互作。由此表明BjSVP完整的K域（BjSVP3）可独立作用于BoFLC，但K域亚域（K1、K2、K3）或者连接区（L1、L2）缺失突变后不能介导该作用。作用强度分析表明：BjSVP的I域能增强该蛋白互作，但M域和C域可能会干扰该作用；芥菜BiFLC被甘蓝BoFLC或BoFLCzq替换后，可明显增加作用强度；甘蓝FLC的I域第20位、K域第65位和C域第32位氨基酸的变异很可能与作用强度相关。

英文摘要：

The transcription factors Flowering Locus C （FLC） and SHORT VEGETATIVE PHASE （SVP） regulate the flowering time via protein interactions in the homologous plants of Brassicajuncea or Brassica oleracea, respectively. However, the heterologous protein-protein interactions between BoFLC of Brassica oleracea and BjSVP of Brassica juncea have not been thoroughly undersltood. In an effort to unravel the mechanisms involved in the heterologous interactions, we cloned BjSVPA 1 - BjSVPA 11 （MI, MIK, K, IKC, KC, IK, IK1L1K2L2, IK1L1K2, IK1L1, IK1 or I domains）inBrassicajuncea, BoFLC and BoFLCzq in Brassica oleracea, respectively. Then we tested the interactions between BoFLC and BjSVP, using the Gal4 yeast two-hybrid system and the [3-galactosidase activity assay. Results showed that BjSVP or BjSVPA2- BjSVPA5 interact with BoFLC. And the fused strains were incubated on QDO/X-~t-Gal/AbA plate and blue colonies were found, suggesting that the yeast fusion reporter genes HIS3, AUR1-C, ADE2, and MEL1 were activated. It also indicated that the full length of K domain （BjSVPA3） was the key amino acid region to independently mediate the protein interactions. However, BjSVPA7 - BjSVPAll truncated forms without K1, K2, K3, L1 or L2 in K domain failed to act with BoFLC. Furthermore, the heterologous interaction was enhanced by I domain of BjSVP, but weakened by its M domain and C domain. The interaction also enhanced by BoFLC or BoFLCzq, compared with the interaction of BjFLC protein. The three amino acid variations （site 20 of I domain, site 65 of K domain and site 32 of C domain） were probably related to the protein interaction strength.