Light stress photodynamics of chlorophyll-binding proteins in Arabidopsis thaliana thylakoid membranes revealed by high-resolution mass spectrometric studies

Bioorg Khim. 2011 Jan-Feb;37(1):119-31. doi: 10.1134/s1068162011010079.

Abstract

In higher plants the light energy is captured by the photosynthetic pigments that are bound to photosystem I and II and their light-harvesting complex (LHC) subunits. In this study, we examined the photodynamic changes within chlorophyll-protein complexes in the thylakoid membrane of Arabidopsis thaliana leaves adapted to low light and subsequently exposed to light stress. Chlorophyll-protein complexes were isolated using sucrose density gradient centrifugation and blue-native polyacrylamid gel electrophoresis (BN-PAGE). Proteome analysis was performed using SDS-PAGE, HPLC and high resolution mass spectrometry. We identified several rarely expressed and stress-induced chlorophyll-binding proteins, showed changes in localization of early light-induced protein family and LHC protein family members between different photosynthetic complexes and assembled/disassembled subcomplexes under light stress conditions and discuss their role in a variety of light stress-related processes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / metabolism
  • Arabidopsis / radiation effects*
  • Arabidopsis Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Light*
  • Light-Harvesting Protein Complexes / metabolism*
  • Molecular Sequence Data
  • Photosystem I Protein Complex / metabolism
  • Photosystem II Protein Complex / metabolism
  • Proteome / metabolism
  • Stress, Physiological
  • Tandem Mass Spectrometry
  • Thylakoids / metabolism
  • Thylakoids / radiation effects*

Substances

  • Arabidopsis Proteins
  • Light-Harvesting Protein Complexes
  • Photosystem I Protein Complex
  • Photosystem II Protein Complex
  • Proteome