Proteomic analysis of embryo development in rice (Oryza sativa)

Abstract

Although embryo development is a major subject in plant growth and development research, a number of aspects of the mechanism of this development process remain unknown. Rice (Oryza sativa) is an excellent monocot plant model for studying embryogenesis with a known genome sequence. Here, we conducted proteomic analysis of embryo development in rice (O. sativa L. ssp. indica cv. 9311). The aim was to investigate and characterize the changes in the protein expression profile during embryo development. For this purpose, the proteome of developing embryos was characterized by two-dimensional gel electrophoresis and nano liquid chromatography/mass spectrometry/mass spectrometry. Proteomic analyses identified 275 differentially expressed proteins throughout the 5 sequential developmental stages from 5 to 30 days after pollination. Most of these proteins were classified into eight functional categories: metabolism, protein synthesis/destination, disease and defense, transporter, transcription, signal transduction, cell growth/division, and storage proteins, which were involved in different cellular and metabolic processes. Hierarchical clustering analyses of protein expression profiles showed that highly expressed proteins in early stages were involved in metabolism, protein synthesis/destination, and most of the other cellular functions, whereas the proteins highly expressed in later stages functioned in the desiccation and dormancy of the embryo.

Proteomic analysis of maize grain development using iTRAQ reveals temporal programs of diverse metabolic processes

“…The increased expression of LEA proteins during the grain maturation stage has also been observed in rice [19] and wheat [31]. The presence and increased level of LEA proteins is correlated with desiccation tolerance [58, 59], and their expression is also induced in response to diverse abiotic or biotic stresses [59].…”

“…Such studies have been performed in many species, including rice [15, 18, 19], wheat [20], Arabidopsis [17], barley [21], castor [22], Medicago truncatula [23], and soybean [24, 25]. However, some types of protein can’t be analyzed by 2-DE as it has the inherent restrictions of being unable to separate hydrophobic proteins, low identification rate, and lack of accurate quantitative information [26, 27].…”

Proteomic Analysis of Embryogenesis and the Acquisition of Seed Dormancy in Norway Maple (Acer platanoides L.)

“…Three dehydrins (group 2 LEA proteins) in seeds of three Acer species, including A. platanoides , exhibited a classic response to dehydrative stress and are presumed to ameliorate the injury associated with desiccation [52]. Xu et al [53] identified eight LEA proteins, including LEA D-34, in developing rice embryos. LEA D-34 belongs to group 5 LEA proteins, whose corresponding transcripts accumulate during the late stage of seed development and in response to drought [54].…”

Evaluation of Extraction Solutions for Biochemical Analyses of the Proteins in Rice Grains

“…17) Rice allergens in the salt-soluble proteins of a transgenic rice and its non-transgenic counterpart have also been compared by 1D and 2D immunoblotting analyses. 18) Analyses of rice total proteins have also been widely used in rice composition studies; 16,[19][20][21][22][23] however, possibly because most reported rice allergens have been included in salt-soluble proteins, rice salt-soluble proteins have always been used for allergen analyses. [24][25][26][27][28] Even so, among the available reports, the composition of solutions for extracting both salt-soluble and total proteins varies from laboratory to laboratory (Table 1).…”