Engineering sulfur storage in maize seed proteins without apparent yield loss

Proc Natl Acad Sci U S A. 2017 Oct 24;114(43):11386-11391. doi: 10.1073/pnas.1714805114. Epub 2017 Oct 9.

Abstract

Sulfur assimilation may limit the pool of methionine and cysteine available for incorporation into zeins, the major seed storage proteins in maize. This hypothesis was tested by producing transgenic maize with deregulated sulfate reduction capacity achieved through leaf-specific expression of the Escherichia coli enzyme 3'-phosphoadenosine-5'-phosphosulfate reductase (EcPAPR) that resulted in higher methionine accumulation in seeds. The transgenic kernels have higher expression of the methionine-rich 10-kDa δ-zein and total protein sulfur without reduction of other zeins. This overall increase in the expression of the S-rich zeins describes a facet of regulation of these proteins under enhanced sulfur assimilation. Transgenic line PE5 accumulates 57.6% more kernel methionine than the high-methionine inbred line B101. In feeding trials with chicks, PE5 maize promotes significant weight gain compared with nontransgenic kernels. Therefore, increased source strength can improve the nutritional value of maize without apparent yield loss and may significantly reduce the cost of feed supplementation.

Keywords: 10-kDa δ-zein; APS reductase; sulfur assimilation; sulfur-rich zeins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animal Feed / analysis
  • Animal Nutritional Physiological Phenomena
  • Animals
  • Chickens / physiology
  • Cysteine / chemistry
  • Cysteine / metabolism
  • Diet / veterinary
  • Gene Expression Regulation, Plant
  • Methionine / chemistry
  • Methionine / metabolism
  • Plants, Genetically Modified
  • Seeds / genetics*
  • Seeds / physiology
  • Sulfur / chemistry
  • Sulfur / metabolism*
  • Zea mays / genetics*
  • Zea mays / physiology
  • Zein / chemistry
  • Zein / metabolism*

Substances

  • Sulfur
  • Zein
  • Methionine
  • Cysteine