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PLANT PHYSIOLOGY , Vol 112, Issue 1 409-420, Copyright © 1996 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Nearest-Neighbor Analysis of Higher-Plant Photosystem I Holocomplex
S. Jansson, B. Andersen and H. V. Scheller
Plant Biochemistry Laboratory, Department of Plant Biology, Royal Veterinary and Agricultural University, Thorvaldsenvej 40, 1871 Frederiksberg C, Denmark (S.J., B.A., H.V.S.)
Photosystem I (PSI) preparations from barley (Hordeum vulgare) and spinach
(Spinacia oleracea) were subjected to chemical cross-linking using the
cleavable homobifunctional cross-linkers dithiobis(succinimidylpropionate)
and 3,3[prime]-dithiobis(sulfosuccinimidyl-propionate). The overall pattern
of cross-linked products was analyzed by the simple but powerful technique
of diagonal electrophoresis, in which the disulfide bond in the
cross-linker was cleaved between the first and second dimensions of the
gel, and immunoblotting. A large number of cross-linked products were
identified. Together with preexisting data on the structure of PSI, it was
deduced that the subunits PSI-D, PSI-H, PSI-I, and PSI-L occupy one side of
the complex, whereas PSI-E, PSI-F, and PSI-J occupy the other. PSI-K and
PSI-G appear to be adjacent to Lhca3 and Lhca2, respectively, and not close
to the other small subunits. Experiments with isolated light-harvesting
complex I preparations indicate that the subunits are organized as dimers,
which seem to associate to the PSI-A/PSI-B proteins independent of each
other. We suggest which PSI subunit corresponds to each membrane-spanning
helix in the cyanobacterial PSI structure, and present a model for
higher-plant PSI.
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