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Molecular & Cellular Proteomics 3:586-595, 2004.
© 2004 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Isolation of Outer Membrane of Synechocystis sp. PCC 6803 and Its Proteomic Characterization^*

Fang Huang^,, Erik Hedman^¶,, Christiane Funk^||, Thomas Kieselbach^¶, Wolfgang P. Schröder^|| and Birgitta Norling^,**

From the Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden; ^¶ Department of Medical Nutrition and Biosciences, Karolinska Institute, Novum, SE-14186 Huddinge, Sweden; and ^|| Department of Biochemistry, Umeå University, SE-90187 Umeå, Sweden

In this report, we describe a newly developed method for isolating outer membranes from Synechocystis sp. PCC 6803 cells. The purity of the outer membrane fraction was verified by immunoblot analysis using antibodies against membrane-specific marker proteins. We investigated the protein composition of the outer membrane using two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry followed by database identification. Forty-nine proteins were identified corresponding to 29 different gene products. All of the identified proteins have a putative N-terminal signal peptide. About 40% of the proteins identified represent hypothetical proteins with unknown function. Among the proteins identified are a Toc75 homologue, a protein that was initially found in the outer envelope of chloroplasts in pea, as well as TolC, putative porins, and a pilus protein. Other proteins identified include ABC transporters and GumB, which has a suggested function in carbohydrate export. A number of proteases such as HtrA were also found in the outer membrane of Synechocystis sp. PCC 6803.

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