scholarly journals Silencing of a Gene Encoding a Protein Component of the Oxygen-Evolving Complex of Photosystem II Enhances Virus Replication in Plants

Virology ◽  
2002 ◽  
Vol 295 (2) ◽  
pp. 307-319 ◽  
Author(s):  
Truus E.M. Abbink ◽  
Jack R. Peart ◽  
Thera N.M. Mos ◽  
David C. Baulcombe ◽  
John F. Bol ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Virus Replication ◽  
Protein Component ◽  
Oxygen Evolving Complex ◽  
Gene Encoding ◽  
Oxygen Evolving

scholarly journals The Photosystem II Oxygen-Evolving Complex Protein PsbP Interacts With the Coat Protein of Alfalfa mosaic virus and Inhibits Virus Replication

2014 ◽  
Vol 27 (10) ◽  
pp. 1107-1118 ◽  
Author(s):  
Muthukumar Balasubramaniam ◽  
Bong-Suk Kim ◽  
Heather M. Hutchens-Williams ◽  
L. Sue Loesch-Fries
Keyword(s):  
Coat Protein ◽  
Photosystem Ii ◽  
Mosaic Virus ◽  
Virus Replication ◽  
Alfalfa Mosaic Virus ◽  
Bimolecular Fluorescence Complementation ◽  
Oxygen Evolving Complex ◽  
In Planta ◽  
Oxygen Evolving

Alfalfa mosaic virus (AMV) coat protein (CP) is essential for many steps in virus replication from early infection to encapsidation. However, the identity and functional relevance of cellular factors that interact with CP remain unknown. In an unbiased yeast two-hybrid screen for CP-interacting Arabidopsis proteins, we identified several novel protein interactions that could potentially modulate AMV replication. In this report, we focus on one of the novel CP-binding partners, the Arabidopsis PsbP protein, which is a nuclear-encoded component of the oxygen-evolving complex of photosystem II. We validated the protein interaction in vitro with pull-down assays, in planta with bimolecular fluorescence complementation assays, and during virus infection by co-immunoprecipitations. CP interacted with the chloroplast-targeted PsbP in the cytosol and mutations that prevented the dimerization of CP abolished this interaction. Importantly, PsbP overexpression markedly reduced virus accumulation in infected leaves. Taken together, our findings demonstrate that AMV CP dimers interact with the chloroplast protein PsbP, suggesting a potential sequestration strategy that may preempt the generation of any PsbP-mediated antiviral state.

scholarly journals Structural Changes in the Acceptor Site of Photosystem II upon Ca2+/Sr2+ Exchange in the Mn4CaO5 Cluster Site and the Possible Long-Range Interactions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Long Range ◽  
Electron Acceptor ◽  
Structural Changes ◽  
Acceptor Site ◽  
Oxygen Evolving Complex ◽  
Long Range Interactions ◽  
Structural Perturbations ◽  
Oxygen Evolving

The Mn4CaO5 cluster site in the oxygen-evolving complex (OEC) of photosystem II (PSII) undergoes structural perturbations, such as those induced by Ca2+/Sr2+ exchanges or Ca/Mn removal. These changes have been known to induce long-range positive shifts (between +30 and +150 mV) in the redox potential of the primary quinone electron acceptor plastoquinone A (QA), which is located 40 Å from the OEC. To further investigate these effects, we reanalyzed the crystal structure of Sr-PSII resolved at 2.1 Å and compared it with the native Ca-PSII resolved at 1.9 Å. Here, we focus on the acceptor site and report the possible long-range interactions between the donor, Mn4Ca(Sr)O5 cluster, and acceptor sites.

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