Proteomic analysis of the expression of proteins related to rice quality during caryopsis development and the effect of high temperature on expression.
Proteins are essential to rice caryopsis development and quality formation. High temperature is an important environmental factor, which may decrease grain quality. In the present study rice caryopsis proteins were profiled by two-dimensional polyacrylamide gel electrophoresis, and differentially expressed proteins were analyzed by liquid chromatography/tandem mass spectrometry. Expressions of more than 400 polypeptide spots during caryopsis development, in response to temperature treatments or between varieties were monitored. Among them, more than 70 differentially expressed polypeptides were analyzed by liquid chromatography/tandem mass spectrometry. We identified 54 proteins with known functions. Of these, 21 were involved with carbohydrate metabolism, 14 with protein synthesis and sorting, and 9 with stress responses. Waxy (Wx) proteins and glutelins were the most significant spots, which increased significantly during development. Allergen-like proteins, PPDK and NADH-SDH, also were expressed during development, implying their physiological roles in caryopsis. Expression of large isoforms of Wx proteins was correlated with the amylose content of rice caryopses. One protein with high GC content in its DNA sequence was correlated with the chalky trait of kernels. High temperature (35/30 degrees C) decreased the expression of Wx proteins, allergen-like proteins, and elongation factor 1beta, but increased the expression of small heat shock proteins (sHSP), glyceraldehyde-3-phosphate dehydrogenase, and prolamin. sHSP was positively correlated with the appearance of chalky kernels. During development, glutelins were phosphorylated and glycosylated, indicating that these molecules were post-translationally modified. Possible functions of the expression of candidate proteins on the grain quality are discussed.
Lin
Shao-Kai
SK
Department of Agronomy, National Taiwan University, Taipei, Republic of China.
Chang
Meng-Chi
MC
Tsai
Yeou-Guang
YG
Lur
Huu-Sheng
HS
D002853:Chromatography, Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D005638:Fruit / Q000737:chemistry / Q000254:growth & development*; D006360:Heat-Shock Proteins / Q000378:metabolism; D006358:Hot Temperature; D013058:Mass Spectrometry; D012275:Oryza / Q000254:growth & development*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D040081:Protein Array Analysis; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D040901:Proteomics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017422:Sequence Analysis, DNA
D006360:Heat-Shock Proteins; D010940:Plant Proteins; D020033:Protein Isoforms