Proteomic study of the soluble proteins from the unicellular cyanobacterium Synechocystis sp. PCC6803 using automated matrix-assisted laser desorption/ionization-time of flight peptide mass fingerprinting

Proteomics. 2002 Dec;2(12):1735-42. doi: 10.1002/1615-9861(200212)2:12<1735::AID-PROT1735>3.0.CO;2-K.


The unicellular cyanobacteria Synechocystis sp. (PCC6803) has become a model organism for a range of biochemical and molecular biology studies aimed at investigating environmental stress responses. In this study the soluble proteins of Synechocystis were analysed using narrow pH range (pH 4.5-5.5) zoom gels, automated matrix-assisted laser desorption/ionization mass spectrometry acquisition, spectral processing and database searching. The work sets the foundation for investigations of proteomic changes following stress treatment. One hundred and ninety-two protein spots were analysed and 105 proteins identified, of these 37 were novel proteins not previously seen on two-dimensional gels. Proteins involved in amino acid biosynthesis, energy metabolism and protein modification were identified using this fully automated procedure demonstrating that automated acquisition and processing will be a useful tool for proteomic analyses on this organism.

MeSH terms

  • Bacterial Proteins / analysis*
  • Cyanobacteria / chemistry*
  • Databases, Protein
  • Electrophoresis, Gel, Two-Dimensional
  • Hydrogen-Ion Concentration
  • Peptide Mapping
  • Proteome / analysis*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods*


  • Bacterial Proteins
  • Proteome