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Proteomics of Synechocystis sp. strain PCC 6803

2000; Wiley; Volume: 267; Issue: 19 Linguagem: Inglês

10.1046/j.1432-1327.2000.01642.x

1432-1033

Simone Fulda, Fang Huang, Fredrik Nilsson, Martin Hagemann, Birgitta Norling,

Protist diversity and phylogeny

Periplasmic proteins isolated by cold osmotic shock of Synechocystis sp. PCC 6803 cells were identified using 2D PAGE, MS and genome analysis. Most of the periplasmic proteins represent ‘hypothetical proteins’ with unknown function. A number of proteases of different specificity, and several enzymes involved in cell wall biosynthesis were also found. In salt‐adapted cells, six proteins were greatly enhanced and three proteins were newly induced. Most of the salt‐enhanced proteins are involved in the alteration of cell wall structure of salt‐adapted cells. The precursors of all 57 periplasmic proteins identified have a signal peptide; 47 of them contain a typical Sec‐dependent signal peptide, whereas 10 contain a putative twin‐arginine signal peptide.