WANG Yi-ying
College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004YUAN Jun
College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004TAN Xiao-feng
College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004LU Meng-qi
College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004ZHOU Ao
College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004ZHOU Jun-qin
College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004College of Forestry, Central South University of Forestry and Technology / Key Laboratory of Cultivation and Protection for Non-wood Forest Trees, Ministry of Education, Changsha 410004
Foundation projects: National Natural Science Foundation of China (31730016);Hunan Provincial Department of Education Scientific Research Project Youth Project(21B0274);Hunan Provincial Enterprise Science and Technology Innovation and Entrepreneurship Team Support Program (Xiang ren cai fa [2022]No.9)
In order to investigate the role of superoxide dismutase (SOD) gene family members in the self-incompatibility response of Camellia oleifera Abel, three family members CoCSD, CoFSD and CoMSD were isolated by RT-PCR. The CDS sequences of CoCSD, CoFSD and CoMSD were 660, 813 and 693 bp in length, encoding for 219, 270 and 230 amino acids, with a molecular weight of 22.49, 31.18 and 25.51 kDa, respectively. Structural analysis revealed that three proteins were hydrophilic without transmembrane domain and signal peptide (non-secretory proteins), and all contained 21 phosphorylation sites. Both CoCSD and CoMSD are stable, while CoFSD is an unstable protein. The secondary structure of CoCSD is mainly composed of irregularly coiled and extended chains, while the secondary structure of CoFSD and CoMSD is mainly composed of α-helices and irregular coils. The three proteins were assigned to three categories in the phylogenetic tree, whereas all were clustered on the same branchlet with the corresponding proteins of tea tree and had high sequence homology. The SOD enzyme activity in self-pollinated pistils was overall higher than that in cross-pollinated pistils, but the expression of CoCSD, CoFSD and CoMSD was highest before pollination and was inhibited by both self and cross-pollination treatments. The results of this study provide a basis for the subsequent in-depth investigation of the biological functions of C. oleifera Abel SOD genes, and also provide a reference for revealing the mechanism of self-incompatibility in C. oleifera Abel.