P869
Characters and Subcellular Localization of OsVDAC3 Protein and Its Effects on Rice Growth

Date: Monday, January 13, 2014
Room: Grand Exhibit Hall
Gang Cheng , South-Central University for Nationalities, Wuhan, China
Linpeng Li , South-Central University for Nationalities, Wuhan, China
Yingjian Zhong , South-Central University for Nationalities, Wuhan, China
Yanping Tan , South-Central University for Nationalities, Wuhan, China
Yonghua Qin , South-Central University for Nationalities, Wuhan, China
Xin Xu , South-Central University for Nationalities, Wuhan, China
Jie Zhou , South-Central University for Nationalities, Wuhan, China
Xuequn Liu , South-Central University for Nationalities, Wuhan, China
Chuntai Wang , South-Central University for Nationalities, Wuhan, China
Voltage-dependent anion channel (VDAC) is a kind of ion channel protein, and widely exists in from fungi to the plant and animal organisms. Through bioinformatics analysis, eight complete vdac genes were identified in rice genome early. The full ORF of osvdac3 gene was cloned, and the expression vector CaMV35S∷osvdac3∷rfp was constructed and transformed into rice line YTB. The RT-PCR results of the genetically modified positive materials showed that the plant height and pollen sterility of T0 positive materials were down–regulation than the control. When Treated with NaCl and Mannitol for T1 positive materials, it was found that the plant height and root length of the positive materials grew more slowly than the control YTB rice. So it implied that osvdac3 gene plays a role in the process of abiotic stress for rice. Then the full length,the C- and N-terminal of osvdac3 gene were cloned into the transient expression vector pM999-gfp, respectively. And the plasmids transfect into YTB rice protoplast and the protoplast was observed with organelles dyes under Laser scanning confocal microscopy. Results showed that OsVDAC3 protein, and -N terminal could be located in the membrane system, and -C terminal was located in the cytoplasm. The results of circular dichroism spectrum for OsVDAC3 soluble protein showed that the secondary structure of OsVDAC3 protein was mainly beta protein folding structure as human VDAC protein reported. All of these could give the chance to deeply understand VDAC protein function in rice.