Structure of a PSII-Pcb supercomplex isolated from Prochloron didemni
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Structure of a photosystem II supercomplex isolated from Prochloron didemni retaining its chlorophyll a/b light-harvesting system |
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| - adapted from: Thomas Bibby, Jon Nield, Min Chen, Anthony Larkum & James Barber. Proceedings of the National Academy of Sciences (USA): 100:9050-9054 | |
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| Prochlorophytes are a class of cyanobacteria that do not use phycobiliproteins
as light-harvesting systems, but contain chlorophyll (Chl) a/b-binding
Pcb proteins. Recently it was shown that Pcb proteins form an 18-subunit
light-harvesting antenna ring around the photosystem I (PSI) trimeric
reaction center complex of the prochlorophyte Prochlorococcus
marinus SS120. Here we have investigated whether the symbiotic
prochlorophyte Prochloron didemni also contains the same supermolecular
complex. Using cells isolated directly from its ascidian host, we
found no evidence for the presence of the Pcb–PSI supercomplex.
Instead we have identified and characterized a supercomplex composed
of photosystem II (PSII) and Pcb proteins. We show that 10-Pcb subunits associate with the PSII dimeric reaction center core to form a giant complex having an estimated Mr of 1,500 kDa with dimensions of 210 x 290 Å. Five-Pcb subunits flank each long side of the dimer and assuming each binds 13 Chl molecules, increase the antenna size of PSII by ~200%. Fluorescence emission studies indicate that energy transfer occurs efficiently from the Pcb antenna. Modeling using the x-ray structure of cyanobacterial PSII suggests that energy transfer to the PSII reaction center is via the Chls bound to the CP47 and CP43 proteins. |
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CONTENTS
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| Straight to Introduction | |
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© Proceedings of
the National Academy of Sciences (USA), 2003