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Originally published In Press as doi:10.1074/mcp.M200043-MCP200 on November 17, 2002.
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Molecular & Cellular Proteomics 1:956-966, 2002.
© 2002 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Proteomics of Synechocystis sp. Strain PCC 6803

Identification of Plasma Membrane Proteins*,S

Fang Huang{ddagger}, Ingela Parmryd{ddagger}, Fredrik Nilsson§, Annika L. Persson, Himadri B. Pakrasi||, Bertil Andersson{ddagger},** and Birgitta Norling{ddagger},{ddagger}{ddagger}

{ddagger} 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
|| Department of Biology, Washington University, St. Louis, Missouri 63130
** Division of Cell Biology, Linköping University, SE-58185 Linköping, Sweden

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 F0 membrane part of the ATP synthase.

{ddagger}{ddagger} To whom correspondence should be addressed: Dept. of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden. Tel.: 46-8-162460; Fax: 46-8-153679; E-mail:birgitta.norling{at}dbb.su.se


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