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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
Author(s) -
Simon William J.,
Hall John J.,
Suzuki Iwane,
Murata Norio,
Slabas Antoni R.
Publication year - 2002
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/1615-9861(200212)2:12<1735::aid-prot1735>3.0.co;2-k
Subject(s) - proteomics , mass spectrometry , peptide mass fingerprinting , matrix assisted laser desorption/ionization , peptide , cyanobacteria , chemistry , proteome , isobaric labeling , time of flight mass spectrometry , desorption , matrix (chemical analysis) , biochemistry , chromatography , biology , ionization , quantitative proteomics , bacteria , adsorption , ion , genetics , gene , organic chemistry
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.