2010 Fiscal Year Final Research Report
Physiological role of a novel protein disulfide isomerase present in rice endosperm tissue
| Project/Area Number |
19580110
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Applied biochemistry
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| Research Institution | Yamaguchi Prefectural University |
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Principal Investigator |
OGAWA MASAHIRO Yamaguchi Prefectural University, 共通教育機構, 教授 (10160772)
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| Co-Investigator(Kenkyū-buntansha) |
KUMAMARU Toshihiro 九州大学, 大学院・農学研究科, 准教授 (00284555)
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| Project Period (FY) |
2007 – 2010
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| Keywords | イネ / 胚乳 / PDI / 突然変異 / MNU / 分子シャペロン / RNAi組換体 / プロテインボデイ |
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| Research Abstract |
It was elucidated that a nobel PDI2;3 with 40 kDa apparent molecular size plays a physiological role for inter-molecular S-S bond formation in rice endosperm tissue. Generally 11S globulin has intramolecular S-S bonding which is catalysed by PDI1;1. with 60 kDa apparent molecular size. However PDI2;3with small 40 kDa apparent molecular size does not function as intramolecular S-S bond forming enzyme. In rice endosperm tissue there are two types of storage proteins such as acid-soluble glutelin and alcohol-soluble prolamin. It has been well known that an intramolecular S-S bonding of proglutelin is formed before being transporting into vacuole. However it has not been known how prolamin aggregate are formed and are accumulated in ER lumen to form PBI. Finally PDI2;3 functions as an enzyme to form intermolecular S-S bond between prolamin polypeptides and which become prolamin aggregate to form PBI.
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