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Protein Disulfide Isomerase PDIL1-1 Has a Regulatory Role in Endosperm Development in Rice
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- Authors
- Advisor
- 서학수
- Major
- 농업생명과학대학 식물생산과학부(작물생명과학전공)
- Issue Date
- 2013-02
- Publisher
- 서울대학교 대학원
- Keywords
- Protein disulfide isomerase-like protein ; PDIL1-1 ; endosperm ; chalky phenotype ; protein body ; aleurone layer ; free sugar ; cysteine protease ; seed protein
- Description
- 학위논문 (박사)-- 서울대학교 대학원 : 식물생산과학부 작물생명과학전공, 2013. 2. 서학수.
- Abstract
- 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.
- Language
- English
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