Isolation of outer membrane of Synechocystis sp PCC 6803 and its proteomic characterization. Huang, F., Hedman, E., Funk, C., Kieselbach, T., Schroder, W. P., & Norling, B. Molecular & Cellular Proteomics, 3(6):586–595, June, 2004. Place: Rockville Publisher: Amer Soc Biochemistry Molecular Biology Inc WOS:000222029100007doi abstract bibtex 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.
@article{huang_isolation_2004,
title = {Isolation of outer membrane of {Synechocystis} sp {PCC} 6803 and its proteomic characterization},
volume = {3},
issn = {1535-9476},
doi = {10/dxr94c},
abstract = {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.},
language = {English},
number = {6},
journal = {Molecular \& Cellular Proteomics},
author = {Huang, F. and Hedman, E. and Funk, C. and Kieselbach, T. and Schroder, W. P. and Norling, B.},
month = jun,
year = {2004},
note = {Place: Rockville
Publisher: Amer Soc Biochemistry Molecular Biology Inc
WOS:000222029100007},
keywords = {crystal-structure, escherichia-coli, genetic-analysis, htra family, multidrug efflux, photosystem-ii, plasma-membranes, protein, pseudomonas-aeruginosa, thylakoid membranes},
pages = {586--595},
}
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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. 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