Table 2.
List of starch biosynthesis proteins of rice endosperm based on proteomics in response to different developmental stages.
Sample | Aim of Study | Technique | Identified Proteins | Details of Results |
---|---|---|---|---|
Taichung Native 1 (TN 1, Indica) and Tainung 67, (TNG 67, Japonica) [13] | To investigate the changes in protein expression patterns during rice caryopsis development (6, 9, 12, 15, and 32 DAF). | 2-DE LC-MS/MS |
GBSS (Waxy) | The expression of GBSS increased after 6 DAF was coincident with the increase in amylose content. GBSS protein was highly expressed in kernels of rice with high amylose content (TN1). |
Nipponbare (Japonica) [22] | To study the protein expression profiles related to grain filling during 6–20 DAF. | 2-DE MALDI-TOF/TOF |
ISA I, AMY, Pho, PGM, AGPaseL2, AGPaseL3, AGPaseS2a/b | All identified proteins were continuously increased from 6 to 20 DAF. Some AGPase isoforms had the highest peak of protein expression at 16 DAF and decrease thereafter. |
ISA3 | ISA3 increased at 6 DAF, showed the highest expression at 10 DAF, and decreased thereafter. | |||
SSI | No result of expression pattern. | |||
Zhonghua 10 (Japonica) [24] | To study the cellular features and proteomics of rice endosperm from 12, 15, and 18 DAF. | 2D-DIGE MALDI-TOF/ TOF-MS |
PUL Pho1 AGPase L AGPase S2 |
Most of the protein expression patterns showed increase in abundance from 12 to 18 DAF. Some isoforms of PUL and AGPase S2 had the highest peak of expression at 15 DAF. Pho1 decreased the expression level form 12–18 DAF. AGPase L showed the highest variation of expression patterns including the expression levels continuously decreased and increased from 12–18 DAF, showed the highest peak and lowest peak at 15 DAF. The completion of starch granule packing was firstly observed in the inner part of endosperm at 15 DAF and showed entire endosperm at 18 DAF. AGPase L and Pho1 were significantly coexpressed with proteins in redox regulation (SOD and APX, respectively) |
Ilpumbyeo (Japonica) [25] |
To identify the differentially expressed proteins of rice grains at 10, 20, 30 DAF and the fully mature grain (45 DAF). | MudPIT | Pho1 PUL AMY SS 2–3 GWD SBE |
All identified 6 starch biosynthesis proteins were reproducibly identified and differentially expressed during four stages (10, 20, 30, and 45 DAF). All of these proteins had the highest expression levels at the fully mature grain except SS 2–3 in which its abundance increased until 20 DAF after that decreased at 30 DAF and increased at fully mature grain. The authors suggested that the expression profile of starch biosynthesis proteins was similar to previous research of Xu et al. [22] |
Jinhui No. 809 (Indica) [87] | To identify the differentially expressed proteins between superior (SS) and inferior spikelet (IS) at the early (EGS), mid (MGS), and late (LGS) grain-filling stages. | 2-DE MALDI-TOF/MS LC-ESI-MS/MS |
AGPase GBSS PUL |
AGPase, GBSS, and PUL isoforms were downregulated in inferior spikelets at EGS. |
AGPase S | AGPase S showed downregulation in both MGS and LGS. | |||
Jinhui No. 809 (Indica) [88] | To identify the differentially expressed proteins of 10 DAF superior spikelet (SS) and 10 and 20 DAF inferior spikelet (IS). | 2-DE MALDI-TOF/MS LC-ESI-MS/MS |
AGPase GBSS SBE 1 SBE 3 PUL |
AGPase had lower expression level in 10 DAF IS compared with both 10 DAF SS and 20 DAF IS. SBE 3, AGPase, PUL, and SBE 1 were detected as the 14-3-3 interacting proteins. AGPase and GBSS might be involved in the developmental stagnancy stage (DSS) of IS especially at the early grain-filling stage. |
Zhonghua 10 (Japonica) [26] | To identify the SGAPs of rice at 10, 15, and 20 DAF. | 2D-DIGE MALDI-TOF/ TOF-MS |
Pho1 PUL SSI AGPase L2 GBSSI AGPase S2a |
Protein abundance of Pho1, PUL, SSI, and AGPase S2a slowly increased from 10 to 15 DAF and then drastically increased from 15 to 20 DAF. GBSSI showed linearly decreased abundance levels from 10 to 20 DAF. GBSSI and SSI were found only in starch granule-associated (SGA) form. AGPase, Pho1, and PUL were observed in both soluble and SGA forms. |