Keeping the Green World Alive: The Repair Cycle of Photosystem II

2011 ◽  
pp. 28-47
2016 ◽  
Vol 11 (9) ◽  
pp. e1218587 ◽  
Author(s):  
Jasmine Theis ◽  
Michael Schroda

2018 ◽  
Vol 178 (2) ◽  
pp. 596-611 ◽  
Author(s):  
Yusuke Kato ◽  
Kiwamu Hyodo ◽  
Wataru Sakamoto

Plant Science ◽  
1996 ◽  
Vol 115 (2) ◽  
pp. 183-190 ◽  
Author(s):  
Douglas Campbell ◽  
Adrian K. Clarke ◽  
Petter Gustafsson ◽  
Gunnar Öquist

2014 ◽  
Vol 1837 (9) ◽  
pp. 1463-1471 ◽  
Author(s):  
Marjaana Suorsa ◽  
Marjaana Rantala ◽  
Ravi Danielsson ◽  
Sari Järvi ◽  
Virpi Paakkarinen ◽  
...  

2006 ◽  
Vol 18 (11) ◽  
pp. 3121-3131 ◽  
Author(s):  
Marc M. Nowaczyk ◽  
Romano Hebeler ◽  
Eberhard Schlodder ◽  
Helmut E. Meyer ◽  
Bettina Warscheid ◽  
...  
Keyword(s):  

2020 ◽  
Vol 117 (35) ◽  
pp. 21775-21784 ◽  
Author(s):  
Prakitchai Chotewutmontri ◽  
Alice Barkan

The D1 reaction center protein of photosystem II (PSII) is subject to light-induced damage. Degradation of damaged D1 and its replacement by nascent D1 are at the heart of a PSII repair cycle, without which photosynthesis is inhibited. In mature plant chloroplasts, light stimulates the recruitment of ribosomes specifically topsbAmRNA to provide nascent D1 for PSII repair and also triggers a global increase in translation elongation rate. The light-induced signals that initiate these responses are unclear. We present action spectrum and genetic data indicating that the light-induced recruitment of ribosomes topsbAmRNA is triggered by D1 photodamage, whereas the global stimulation of translation elongation is triggered by photosynthetic electron transport. Furthermore, mutants lacking HCF136, which mediates an early step in D1 assembly, exhibit constitutively highpsbAribosome occupancy in the dark and differ in this way from mutants lacking PSII for other reasons. These results, together with the recent elucidation of a thylakoid membrane complex that functions in PSII assembly, PSII repair, andpsbAtranslation, suggest an autoregulatory mechanism in which the light-induced degradation of D1 relieves repressive interactions between D1 and translational activators in the complex. We suggest that the presence of D1 in this complex coordinates D1 synthesis with the need for nascent D1 during both PSII biogenesis and PSII repair in plant chloroplasts.


2019 ◽  
Vol 116 (43) ◽  
pp. 21907-21913 ◽  
Author(s):  
Daniel A. Weisz ◽  
Virginia M. Johnson ◽  
Dariusz M. Niedzwiedzki ◽  
Min Kyung Shinn ◽  
Haijun Liu ◽  
...  

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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