Proteomics of Synechocystis sp strain PCC 6803 -: Identification of plasma membrane proteins

被引:144
作者
Huang, F
Parmryd, I
Nilsson, F
Persson, AL
Pakrasi, HB
Andersson, B
Norling, B [1 ]
机构
[1] Stockholm Univ, Arrhenius Labs Nat Sci, Dept Biochem & Biophys, SE-10691 Stockholm, Sweden
[2] AstraZeneca R&D, SE-43183 Molndal, Sweden
[3] Stockholm Univ, Wenner Gren Inst, Dept Zool Cell Biol, SE-10691 Stockholm, Sweden
[4] Washington Univ, Dept Biol, St Louis, MO 63130 USA
[5] Linkoping Univ, Div Cell Biol, SE-58185 Linkoping, Sweden
关键词
D O I
10.1074/mcp.M200043-MCP200
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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.
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收藏
页码:956 / 966
页数:11
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