Proteome-wide characterization of seed aging in Arabidopsis: a comparison between artificial and natural aging protocols

Plant Physiol. 2008 Sep;148(1):620-41. doi: 10.1104/pp.108.123141. Epub 2008 Jul 3.

Abstract

A variety of mechanisms have been proposed to account for the extension of life span in seeds (seed longevity). In this work, we used Arabidopsis (Arabidopsis thaliana) seeds as a model and carried out differential proteomics to investigate this trait, which is of both ecological and agricultural importance. In our system based on a controlled deterioration treatment (CDT), we compared seed samples treated for different periods of time up to 7 d. Germination tests showed a progressive decrease of germination vigor depending on the duration of CDT. Proteomic analyses revealed that this loss in seed vigor can be accounted for by protein changes in the dry seeds and by an inability of the low-vigor seeds to display a normal proteome during germination. Furthermore, CDT strongly increased the extent of protein oxidation (carbonylation), which might induce a loss of functional properties of seed proteins and enzymes and/or enhance their susceptibility toward proteolysis. These results revealed essential mechanisms for seed vigor, such as translational capacity, mobilization of seed storage reserves, and detoxification efficiency. Finally, this work shows that similar molecular events accompany artificial and natural seed aging.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acids / metabolism
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / metabolism*
  • Germination*
  • Glycolysis
  • Oxidation-Reduction
  • Plant Proteins / metabolism
  • Protein Biosynthesis
  • Protein Carbonylation
  • Proteome*
  • RNA, Messenger / metabolism
  • Seeds / metabolism*
  • Sulfurtransferases / metabolism
  • Time Factors

Substances

  • Amino Acids
  • Arabidopsis Proteins
  • Plant Proteins
  • Proteome
  • RNA, Messenger
  • dehydrin proteins, plant
  • Sulfurtransferases
  • 3-mercaptopyruvate sulphurtransferase