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Nearest-neighbor analysis of higher-plant photosystem I holocomplex
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).ORCID iD: 0000-0002-7906-6891
1996 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 112, no 1, 409-420 p.Article in journal (Refereed) Published
Abstract [en]

Photosystem I (PSI) preparations from barley (Hordeum vulgare) and spinach (Spinacia oleracea) were subjected to chemical crosslinking using the cleavable homobifunctional cross-linkers dithiobis(succinimidylpropionate) and 3,3'-dithiobis(sulfosuccinimidylpropionate). 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 ] 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.

Place, publisher, year, edition, pages
1996. Vol. 112, no 1, 409-420 p.
Identifiers
URN: urn:nbn:se:umu:diva-44614ISI: A1996VJ09300049OAI: oai:DiVA.org:umu-44614DiVA: diva2:434829
Available from: 2011-08-16 Created: 2011-06-09 Last updated: 2017-12-08

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