In oxygenic photosynthetic organisms, photosystem II (PSII) is a unique membrane protein complex that catalyzes light-driven oxidation of water. PSII undergoes frequent damage due to its demanding photochemistry. It must undergo a repair and reassembly process following photodamage, many facets of which remain unknown. We have discovered a PSII subcomplex that lacks 5 key PSII core reaction center polypeptides: D1, D2, PsbE, PsbF, and PsbI. This pigment-protein complex does contain the PSII core antenna proteins CP47 and CP43, as well as most of their associated low molecular mass subunits, and the assembly factor Psb27. Immunoblotting, mass spectrometry, and ultrafast spectroscopic results support the absence of a functional reaction center in this complex, which we call the "no reaction center" complex (NRC). Analytical ultracentrifugation and clear native PAGE analysis show that NRC is a stable pigment-protein complex and not a mixture of free CP47 and CP43 proteins. NRC appears in higher abundance in cells exposed to high light and impaired protein synthesis, and genetic deletion of PsbO on the PSII luminal side results in an increased NRC population, indicative that NRC forms in response to photodamage as part of the PSII repair process. Our finding challenges the current model of the PSII repair cycle and implies an alternative PSII repair strategy. Formation of this complex may maximize PSII repair economy by preserving intact PSII core antennas in a single complex available for PSII reassembly, minimizing the risk of randomly diluting multiple recycling components in the thylakoid membrane following a photodamage event.
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http://dx.doi.org/10.1073/pnas.1909644116 | DOI Listing |
Plant Cell
December 2024
Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences (CEMPS), Chinese Academy of Sciences, Shanghai 200032, China.
Plant Commun
December 2024
Department of Biochemistry and Center for Plant Biology, Purdue University, West Lafayette, IN 47907, USA. Electronic address:
The light-driven water-splitting reaction of photosystem II exposes its key reaction center core protein subunits to irreversible oxidative photodamage. A rapid repair cycle replaces the photodamaged core subunits in plants, but how the large antenna-core supercomplex structures of plant photosystem II disassemble for repair is not currently understood. Here, we report the specific involvement of phosphorylation in removal of the peripheral antenna from the core and monomerization of the dimeric cores.
View Article and Find Full Text PDFFront Plant Sci
November 2024
College of Grassland Agriculture, Northwest A&F University, Yangling, Shaanxi, China.
Physiol Plant
December 2024
Division of Life Sciences, Korea Polar Research Institute, Incheon, Republic of Korea.
Antarctic plants face significant challenges due to exposure to freeze-thaw stress throughout their life cycle. The ability to recover from freeze-thaw injuries during post-thaw recovery (PTR) periods is a crucial skill for their survival and growth. However, no research, to the best our knowledge, has explored their recovery mechanisms at the cellular and molecular levels.
View Article and Find Full Text PDFThylakoid membranes in chloroplasts and cyanobacteria harbor the multisubunit protein complexes that catalyze the light reactions of photosynthesis. In plant chloroplasts, the thylakoid membrane system comprises a highly organized network with several subcompartments that differ in composition and morphology: grana stacks, unstacked stromal lamellae, and grana margins at the interface between stacked and unstacked regions. The localization of components of the photosynthetic apparatus among these subcompartments has been well characterized.
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