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Submitted on December 19, 2003
Department of Bichemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm SE-10691
Corresponding Author: birgitta.norling{at}dbb.su.se
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 MALDI-TOF 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 which 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.
Revised on February 26, 2004
Accepted on February 26, 2004
Isolation of outer membrane of Synechocystis sp. PCC 6803 and its proteomic characterization
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