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Protein Disulfide Isomerase PDIL1-1 Has a Regulatory Role in Endosperm Development in Rice

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Authors

김연정

Advisor
서학수
Major
농업생명과학대학 식물생산과학부(작물생명과학전공)
Issue Date
2013-02
Publisher
서울대학교 대학원
Keywords
Protein disulfide isomerase-like proteinPDIL1-1endospermchalky phenotypeprotein bodyaleurone layerfree sugarcysteine proteaseseed 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
URI
https://hdl.handle.net/10371/121034
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