Specific Degradation of D1 Protein during Exposure of Thylakoid Membranes to High Temperature in the Dark

1999 ◽  
Vol 36 (3) ◽  
pp. 433-440 ◽  
Author(s):  
A.K. Singh ◽  
G.S. Singhal
2021 ◽  
Vol 50 (2) ◽  
pp. 433-436
Author(s):  
Yuan Xue Tao ◽  
Li Fu Ping

Photosynthetic capacity and photosystem II (PSII) activity decreased with increasing temperature, whereas antioxidant enzyme activity showed the opposite trend. High temperature stress induced a significant increase in Φf,D, and D1 protein turnover rate. Photosynthetic capacity, PSII activity, and antioxidant enzyme levels in plants treated at 35 and 40°C were restored to control levels upon stress relief, whereas those in plants grown at 45℃ were only partially restored. Therefore, the temperature limit for heat tolerance in Parthenocissus quinquefolia is between 40 and 45℃. Further, it was observed that antioxidant enzymes were crucial for high-temperature stress resistance in P. quinquefolia, with DEGP1 protein playing a major role in the rapid turnover of D1 protein for PSII repair. Bangladesh J. Bot. 50(2): 433-436, 2021 (June)


2001 ◽  
Vol 29 (4) ◽  
pp. 427-430 ◽  
Author(s):  
Z. Adam ◽  
O. Ostersetzer

To study protein degradation in thylakoid membranes we identified, characterized and cloned thylakoid proteases, and then linked them to known proteolytic processes. Several families of chloroplast proteases were identified and characterized to different extents. FtsH, an ATP-dependent metalloprotease that belongs to the AAA-protein family, was found to be integral to the thylakoid membrane, facing the stroma. It is involved in both the degradation of unassembled subunits of membrane complexes, such as the Rieske Fe-S protein of the cytochrome complex, and the degradation of oxidatively damaged proteins such as the D1 protein of the photosystem II (PS II) reaction centre. Plant genomes contain multiple isomers of this protease but the functional significance of this multiplication is not clear yet. A second protease, the serine ATP-independent DegP, was found to be strongly associated with the luminal side of the thylakoid membrane. Although a specific role has not yet assigned for it, its location suggests that it can degrade luminal soluble proteins as well as luminally exposed regions of thylakoid membrane proteins.


2016 ◽  
Vol 81 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Hua Li ◽  
Hailiang Xu ◽  
Pengju Zhang ◽  
Mingquan Gao ◽  
Dan Wang ◽  
...  

1993 ◽  
Vol 16 (4) ◽  
pp. 421-428 ◽  
Author(s):  
D. L. FERGUSON* ◽  
K. AL-KHATIB ◽  
J. A. GUIKEMA ◽  
G. M. PAULSEN

2007 ◽  
Vol 34 (12) ◽  
pp. 1112 ◽  
Author(s):  
Iva Šnyrychová ◽  
Péter B. Kós ◽  
Éva Hideg

The production of reactive oxygen species (ROS) was studied in isolated thylakoid membranes exposed to 312 nm UV-B irradiation. Hydroxyl radicals (•OH) and hydrogen peroxide were measured directly, using a newly developed method based on hydroxylation of terephthalic acid and the homovanillic acid/peroxidase assay, respectively. At the early stage of UV-B stress (doses lower than 2.0 J cm–2), •OH were derived from superoxide radicals via hydrogen peroxide. Production of these ROS was dependent on photosynthetic electron transport and was not exclusive to UV-B. Both ROS were found in samples exposed to the same doses of PAR, suggesting that the observed ROS are by-products of the UV-B-driven electron transport rather than specific initiators of the UV-B-induced damage. After longer exposure of thylakoids to UV-B, leading to the inactivation of PSII centres, a small amount of •OH was still observed in thylakoids, even though no free hydrogen peroxide was detected. At this late stage of UV-B stress, •OH may also be formed by the direct cleavage of organic peroxides by UV-B. Immunodetection showed that the presence of the observed ROS alone was not sufficient to achieve the degradation of the D1 protein of PSII centres.


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