The action spectrum of Photosystem II photoinactivation in visible light

Author(s):  
Alonso Zavafer ◽  
Wah Soon Chow ◽  
Mun Hon Cheah
Small ◽  
2012 ◽  
Vol 9 (1) ◽  
pp. 61-66 ◽  
Author(s):  
Yi-Yeoun Kim ◽  
David Williams ◽  
Fiona C. Meldrum ◽  
Dominic Walsh

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.


1956 ◽  
Vol 39 (5) ◽  
pp. 735-751 ◽  
Author(s):  
C. L. Brandt ◽  
A. C. Giese

1. Irradiation with three short ultraviolet (UV) wave lengths, 226, 233, and 239 mµ rapidly immobilizes Paramecium caudatum, the dosage required being smaller the shorter the wave length. 85 per cent of paramecia immobilized with wave length 226 mµ recover completely. Recovery from immobilizing doses is less the longer the wave length. 2. Irradiation continued after immobilization kills the paramecia in a manner which is markedly different for very short (226, 233, and 239 mµ) and longer (267 mµ) wave lengths. 3. An action spectrum for immobilization in P. caudatum was determined for the wave lengths 226, 233, 239, 248, and 267 mµ, and found to resemble the absorption of protein and lipide in the wave length region below 248 mµ. Addition of these data to those of Giese (1945 b) gives an action spectrum resembling the absorption by albumin-like protein. 4. Division of P. caudatum is delayed by doses of wave lengths 226, 233, and 239 mµ which cause immobilization, the longest wave length being most effective. 5. Immobilization at any of the wave lengths tested (226, 233, 239, 248, 267 mµ) is not photoreversible when UV-treated paramecia are concurrently illuminated. 6. Division delay resulting from immobilizing doses of 226, 233, and 239 mµ is photoreversible by exposure to visible light concurrently with the UV. 7. Division delay induced by exposure to wave length 267 mµ is reduced by exposure to visible light applied concurrently with UV or immediately afterwards. 8. The data suggest that the shortest UV wave length tested (226 mµ) affects the cytoplasm selectively, because it is absorbed superficially as indicated by unilateral fluorescence in UV. Consequently it immobilizes paramecia rapidly but has little effect on the division rate because little radiation reaches the nucleus. 9. The data support the view that nuclear effects of UV are readily photoreversed but cytoplasmic effects are not.


2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Alonso Zavafer ◽  
Mun Hon Cheah ◽  
Warwick Hillier ◽  
Wah Soon Chow ◽  
Shunichi Takahashi

2017 ◽  
Vol 33 (3) ◽  
pp. 172-175 ◽  
Author(s):  
Izumi Kishimoto ◽  
Naoko Uetsu ◽  
Hirotsugu Tanimura ◽  
Hidetaka Fujii ◽  
Hiroyuki Okamoto

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