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Investigating the early stages of Photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexe
- 1.0362744 - MBÚ 2012 RIV US eng J - Journal Article
Boehm, M. - Romero, E. - Reisinger, V. - Yu, J. - Komenda, Josef - Eichacker, L. A. - Dekker, J. P. - Nixon, P. J.
Investigating the early stages of Photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexe.
Journal of Biological Chemistry. Roč. 286, č. 17 (2011), 14812-14819. ISSN 0021-9258. E-ISSN 1083-351X
R&D Projects: GA AV ČR IAA400200801
Institutional research plan: CEZ:AV0Z50200510
Keywords : ENERGY CHLOROPHYLL STATES * ANTENNA PROTEIN COMPLEX * OXYGEN-EVOLVING CENTER
Subject RIV: EE - Microbiology, Virology
Impact factor: 4.773, year: 2011
Using the cyanobacterium Synechocystis sp. PCC 6803, we describe here the isolation of the CP47 and CP43 subunits, which, during biogenesis, attach to a reaction center assembly complex containing D1, D2, and cytochrome b559, with CP47 binding first. Absorption spectroscopy and pigment analyses revealed that both CP47-His and CP43-His bind chlorophyll a and âcarotene. A comparison of the low temperature absorption and fluorescence spectra in theQY region for CP47-His and CP43-His with those for CP47 and CP43 isolated by fragmentation of spinach PSII core complexes confirmed that the spectroscopic properties are similar but not identical. Immunoblotting and mass spectrometry revealed the co-purification of PsbH, PsbL, and PsbT with CP47-His and of PsbK and Psb30/Ycf12 with CP43-His. Overall, our data support the view that CP47 and CP43 form preassembled pigment-protein complexes in vivo before their incorporation into the PSII complex
Permanent Link: http://hdl.handle.net/11104/0198982
Number of the records: 1