Počet záznamů: 1

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

  1. 1.
    0362744 - MBU-M 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
    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