Investigating the early stages of Photosystem II assembly in Synechocystis sp. PCC 6803: isolation of CP47 and CP43 complexe

0362744 - MBÚ 2012 RIV US eng J - Článek v odborném periodiku
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
Grant CEP: GA AV ČR IAA400200801
Výzkumný záměr: CEZ:AV0Z50200510
Klíčová slova: ENERGY CHLOROPHYLL STATES * ANTENNA PROTEIN COMPLEX * OXYGEN-EVOLVING CENTER
Kód oboru RIV: EE - Mikrobiologie, virologie
Impakt faktor: 4.773, rok: 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
Trvalý link: http://hdl.handle.net/11104/0198982