2007 Fiscal Year Final Research Report Summary
Resolution of accumulation mechanism into protein body of prolamin in rice seed
| Project/Area Number |
16380009
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (B)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
Breeding science
|
|---|
| Research Institution | Kyushu University |
|---|
Principal Investigator |
KUMAMARU Toshihiro Kyushu University, Faculty of Agriculture, Associate professor (00284555)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
SATOH Hikaru Kyushu University, Faculty of Agriculture, Professor (70128031)
OGAWA Masahiro Yamaguchi Prefectural University, Faculty of Life Science, Professor (10160772)
|
|---|
| Project Period (FY) |
2004 – 2007
|
| Keywords | Cell. Tissue / Genetics / Genome / Seed / Rice / Storage Protein |
|---|
| Research Abstract |
Accumulation of prolamin into protein body
In rice cystein rich prolamin, which is composed of three polypeptides, 10 kDa, 15 kDa, and 16 kDa, forms the prolamin protein body with 13 kDa cystein poor prolamin. Immunofluorescent and immunoelectron microscopies indicated that 10 and 13 kDa prolamins localized to central and peripheral regions of the PB. Additionally, immunofluorescent microscopy showed that 10 kDa prolamin was accumulated into ER lumen at 7 day after flowering and after that 13 kDa prolamin was layered over the core of 10 kDa prolamin. In the 13 kDa cystein poor prolamin deficient mutant, esp1, spherical PB with the electron dense core including 10kDa prolamin was observed. In the 10 kDa prolamin deficient mutant, esp3, the core structure of PB was not observed, instead, irregular, electron lucent and hypertrophied PB was observed. These results suggest that the formation of prolamin PB in rice is initiated by accumulation of 10 kDa prolamin in the central core and sequentially 13 kDa prolamin is layered over the core structure. It is concluded that 10 kDa prolamin plays a role to form the core structure to stabilize prolamin PB structure in rice.
Identification and function of Esp1 gene
In esp1 mutation, cystein poor prolamin is reduced. In order to specify the responsible gene of esp1 mutation, the construction of the high-density linkage map of esp1 gene and the complementation test were performed. As results, it became clear that Esp1 gene encode the Eucaryotic Release Factor 1(eRFF1), which is translation termination factor, indicating that the eRF1 is a factor regulating the translation of cystein poor prolamin.
|
Research Products
(31 results)
-
-
-
[Journal Article] Protein body biogenesis2007
Author(s)
Kumamaru, T., et. al.
-
Journal Title
cereal endosperms.In Endosperm-Development and Molecular Biology, O.A.Olsen, ed.Plant Cell Monographs(8), Springer
Pages: 141-158
Description
「研究成果報告書概要(和文)」より
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
