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Proteomics of Synechocystis sp. strain PCC 6803: identification of plasma membrane proteins
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden.
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden.
AstraZeneca R&D Mölndal, SE-43183 Mölndal, Sweden .
Department of Zoological Cell Biology, The Wenner-Gren Institute, Stockholm University, SE-10691 Stockholm, Sweden.
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2002 (English)In: Molecular & Cellular Proteomics, ISSN 1535-9476, E-ISSN 1535-9484, Vol. 1, no 12, 956-966 p.Article in journal (Refereed) Published
Abstract [en]

Cyanobacteria are unique prokaryotes since they in addition to outer and plasma membranes contain the photosynthetic membranes (thylakoids). The plasma membranes of Synechocystis 6803, which can be completely purified by density centrifugation and polymer two-phase partitioning, have been found to be more complex than previously anticipated, i.e. they appear to be essential for assembly of the two photosystems. A proteomic approach for the characterization of cyanobacterial plasma membranes using two-dimensional gel electrophoresis and mass spectrometry analysis revealed a total of 57 different membrane proteins of which 17 are integral membrane spanning proteins. Among the 40 peripheral proteins 20 are located on the periplasmic side of the membrane, while 20 are on the cytoplasmic side. Among the proteins identified are subunits of the two photosystems as well as Vipp1, which has been suggested to be involved in vesicular transport between plasma and thylakoid membranes and is thus relevant to the possibility that plasma membranes are the initial site for photosystem biogenesis. Four subunits of the Pilus complex responsible for cell motility were also identified as well as several subunits of the TolC and TonB transport systems. Several periplasmic and ATP-binding proteins of ATP-binding cassette transporters were also identified as were two subunits of the F(0) membrane part of the ATP synthase.

Place, publisher, year, edition, pages
2002. Vol. 1, no 12, 956-966 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-193098DOI: 10.1074/mcp.M200043-MCP200ISI: 000185314000005PubMedID: 12543932OAI: oai:DiVA.org:uu-193098DiVA: diva2:601319
Available from: 2013-01-29 Created: 2013-01-29 Last updated: 2017-12-06Bibliographically approved

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Parmryd, Ingela

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