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Review
. 2014 May 30:5:240.
doi: 10.3389/fpls.2014.00240. eCollection 2014.

Proteome balancing of the maize seed for higher nutritional value

Yongrui Wu  1 , Joachim Messing  2
Affiliations
Review

Proteome balancing of the maize seed for higher nutritional value

Yongrui Wu et al. Front Plant Sci. .

Abstract

Most flowering plant seeds are composed of the embryo and endosperm, which are surrounded by maternal tissue, in particular the seed coat. Whereas the embryo is the dormant progeny, the endosperm is a terminal organ for storage of sugars and amino acids in proteins and carbohydrates, respectively. Produced in maternal leaves during photosynthesis, sugars, and amino acids are transported to developing seeds after flowering, and during germination they nourish early seedlings growth. Maize endosperm usually contains around 10% protein and 70% starch, and their composition ratio is rather stable, because it is strictly regulated through a pre-set genetic program that is woven by networks of many interacting or counteracting genes and pathways. Endosperm protein, however, is of low nutritional value due mainly to the high expression of the α-zein gene family, which encodes lysine-free proteins. Reduced levels of these proteins in the opaque 2 (o2) mutant and α-zein RNAi (RNA interference) transgenic seed is compensated by an increase of non-zein proteins, leading to the rebalancing of the nitrogen sink and producing more or less constant levels of total proteins in the seed. The same rebalancing of zeins and non-zeins has been observed for maize seeds bred for 30% protein. In contrast to the nitrogen sink, storage of sulfur is controlled through the accumulation of specialized sulfur-rich proteins in maize endosperm. Silencing the synthesis of α-zeins through RNAi fails to raise sulfur-rich proteins. Although overexpression of the methionine-rich δ-zein can increase the methionine level in seeds, it occurs at least in part at the expense of the cysteine-rich β- and γ-zeins, demonstrating a balance between cysteine and methionine in sulfur storage. Therefore, we propose that the throttle for the flow of sulfur is placed before the synthesis of sulfur amino acids when sulfur is taken up and reduced during photosynthesis.

Keywords: RNAi; lysine; nitrogen; storage proteins; sulfur.

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Figures

FIGURE 1
FIGURE 1
Maize storage proteins. Prolamin proteins in maize are called zeins and the others are all classified as non-zeins. Adapted from Wu et al. (2012).
FIGURE 2
FIGURE 2
Proteome rebalancing in o2 mutant and IHP with suppressed α-zeins. Lane 1 and 4, W64A and W64Ao2; lane 2 and 4, two F1 progeny of IHP × α-zeinRNAi/- not inheriting and inheriting the RNAi. Adapted from Wu and Messing (2012).
FIGURE 3
FIGURE 3
Accumulation patterns of zeins in high-methionine transgenic and WT seeds. Hi-Met transgenic seeds in lane 2 and 4 express much higher levels of the 10-kDa δ-zein, but lower levels of β- and γ-zeins than WT in lane 1 and 4. Adapted from Wu et al. (2012).
FIGURE 4
FIGURE 4
Sulfate reduction and synthesis of cysteine and methionine pathways. The flow of sulfur is shown to illustrate sink source relationship. Adapted from Wu et al. (2012).
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