S-Space College of Agriculture and Life Sciences (농업생명과학대학) Dept. of Plant Science (식물생산과학부) Theses (Ph.D. / Sc.D._식물생산과학부)
Protein Disulfide Isomerase PDIL1-1 Has a Regulatory Role in Endosperm Development in Rice
- 농업생명과학대학 식물생산과학부(작물생명과학전공)
- Issue Date
- 서울대학교 대학원
- Protein disulfide isomerase-like protein; PDIL1-1; endosperm; chalky phenotype; protein body; aleurone layer; free sugar; cysteine protease; seed protein
- 학위논문 (박사)-- 서울대학교 대학원 : 식물생산과학부 작물생명과학전공, 2013. 2. 서학수.
- Protein disulfide isomerase (PDI) is a chaperone protein involved in oxidative protein folding by acting as a catalyst and assisting folding in the endoplasmic reticulum (ER). A genome database search showed that rice contains 19 PDI-like genes. However, their functions are not clearly identified. Possible functions of rice PDI-like protein 1-1 (PDIL1-1) during seed development were identified in this study. Seeds of the T-DNA insertion PDIL1-1 mutant, PDIL1-1∆ , identified by genomic DNA PCR and western blot analysis, displayed a chalky phenotype and a thick aleurone layer. Protein content per seed was significantly lower and free sugar content higher in PDIL1-1∆ mutant seeds than in the wild type. Proteomic analysis of PDIL1-1∆ mutant seeds showed that PDIL1-1 is post-translationally regulated, and its loss causes accumulation of many types of seed proteins related to glucose/starch metabolism and ROS (reactive oxygen species) scavenging. In addition, PDIL1-1 strongly interacts with the cysteine protease OsCP1. Our data indicate that the opaque phenotype of PDIL1-1∆ mutant seeds results from production of irregular starch granules and protein body through loss of regulatory activity for various proteins involved in the synthesis of seed components.