Effects of High Temperature Stress on PSII Function and Its Relation to D1 Protein in Chloroplast Thylakoid in Rice Flag Leaves

2013 ◽  
Vol 39 (6) ◽  
pp. 1060 ◽  
Author(s):  
Wei-Li YANG ◽  
Fu-Deng HUANG ◽  
Zhen-Zhen CAO ◽  
Bing-Ting LEI ◽  
Dong-Wei HU ◽  
...  
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)


2020 ◽  
Vol 53 (2) ◽  
Author(s):  
Khalil Ahmed Laghari ◽  
Abdul Jabbar Pirzada ◽  
Mahboob Ali Sial ◽  
Muhammad Athar Khan ◽  
Jamal Uddin Mangi

2020 ◽  
Vol 52 (5) ◽  
Author(s):  
De-Gong Wu ◽  
Qiu-Wen Zhan ◽  
Hai-Bing Yu ◽  
Bao-Hong Huang ◽  
Xin-Xin Cheng ◽  
...  

Author(s):  
D-J Kim ◽  
I-G Kim ◽  
J-Y Noh ◽  
H-J Lee ◽  
S-H Park ◽  
...  

Abstract As DRAM technology extends into 12-inch diameter wafer processing, plasma-induced wafer charging is a serious problem in DRAM volume manufacture. There are currently no comprehensive reports on the potential impact of plasma damage on high density DRAM reliability. In this paper, the possible effects of floating potential at the source/drain junction of cell transistor during high-field charge injection are reported, and regarded as high-priority issues to further understand charging damage during the metal pad etching. The degradation of block edge dynamic retention time during high temperature stress, not consistent with typical reliability degradation model, is analyzed. Additionally, in order to meet the satisfactory reliability level in volume manufacture of high density DRAM technology, the paper provides the guidelines with respect to plasma damage. Unlike conventional model as gate antenna effect, the cell junction damage by the exposure of dummy BL pad to plasma, was revealed as root cause.


2020 ◽  
Vol 16 (2) ◽  
pp. 18-23
Author(s):  
K. PRAVALLIKA ◽  
C. ARUNKUMAR ◽  
A. VIJAYKUMAR ◽  
R. BEENA ◽  
V. G. JAYALEKSHMI

Plants ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 687
Author(s):  
Chan Seop Ko ◽  
Jin-Baek Kim ◽  
Min Jeong Hong ◽  
Yong Weon Seo

High-temperature stress during the grain filling stage has a deleterious effect on grain yield and end-use quality. Plants undergo various transcriptional events of protein complexity as defensive responses to various stressors. The “Keumgang” wheat cultivar was subjected to high-temperature stress for 6 and 10 days beginning 9 days after anthesis, then two-dimensional gel electrophoresis (2DE) and peptide analyses were performed. Spots showing decreased contents in stressed plants were shown to have strong similarities with a high-molecular glutenin gene, TraesCS1D02G317301 (TaHMW1D). QRT-PCR results confirmed that TaHMW1D was expressed in its full form and in the form of four different transcript variants. These events always occurred between repetitive regions at specific deletion sites (5′-CAA (Glutamine) GG/TG (Glycine) or (Valine)-3′, 5′-GGG (Glycine) CAA (Glutamine) -3′) in an exonic region. Heat stress led to a significant increase in the expression of the transcript variants. This was most evident in the distal parts of the spike. Considering the importance of high-molecular weight glutenin subunits of seed storage proteins, stressed plants might choose shorter polypeptides while retaining glutenin function, thus maintaining the expression of glutenin motifs and conserved sites.


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