Effects of salicylic acid on protein kinase activity and chloroplast D1 protein degradation in wheat leaves subjected to heat and high light stress

2011 ◽  
Vol 31 (5) ◽  
pp. 259-263 ◽  
Author(s):  
Hui-Jie Zhao ◽  
Xue-Juan Zhao ◽  
Pei-Fang Ma ◽  
Yue-Xia Wang ◽  
Wei-Wei Hu ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Protein Kinase ◽  
Protein Degradation ◽  
Kinase Activity ◽  
Light Stress ◽  
D1 Protein ◽  
High Light ◽  
Protein Kinase Activity ◽  
High Light Stress ◽  
Wheat Leaves

scholarly journals Papain-like cysteine proteases are required for the regulation of photosynthetic gene expression and acclimation to high light stress

2021 ◽  
Vol 72 (9) ◽  
pp. 3441-3454
Author(s):  
Sarah Alomrani ◽  
Karl J Kunert ◽  
Christine H Foyer
Keyword(s):  
Gene Expression ◽  
Large Subunit ◽  
Light Stress ◽  
D1 Protein ◽  
Carbon Assimilation ◽  
Cysteine Proteases ◽  
High Light ◽  
High Light Stress ◽  
Photosynthetic Gene ◽  
Transgenic Lines

AbstractChloroplasts are considered to be devoid of cysteine proteases. Using transgenic Arabidopsis lines expressing the rice cystatin, oryzacystatin I (OC-I), in the chloroplasts (PC lines) or cytosol (CYS lines), we explored the hypothesis that cysteine proteases regulate photosynthesis. The CYS and PC lines flowered later than the wild type (WT) and accumulated more biomass after flowering. In contrast to the PC rosettes, which accumulated more leaf chlorophyll and carotenoid pigments than the WT, the CYS lines had lower amounts of leaf pigments. High-light-dependent decreases in photosynthetic carbon assimilation and the abundance of the Rubisco large subunit protein, the D1 protein, and the phosphorylated form of D1 proteins were attenuated in the CYS lines and reversed in the PC lines relative to the WT. However, the transgenic lines had higher amounts of LHC, rbcs, pasbA, and pasbD transcripts than the WT, and also showed modified chloroplast to nucleus signalling. We conclude that cysteine proteases accelerate the reconfiguration of the chloroplast proteome after flowering and in response to high-light stress. Inhibition of cysteine proteases, such as AtCEP1, slows chloroplast protein degradation and stimulates photosynthetic gene expression and chloroplast to nucleus signalling, enhancing stress tolerance traits.

Regulatory effects of salicylic acid on protease Deg5 and PSⅡfunction of wheat chloroplasts under heat and high light stress

2014 ◽  
Vol 34 (24) ◽  
Author(s):  
郑静静 ZHENG Jingjing ◽  
杨丽 YANG Li ◽  
苏小雨 SU Xiaoyu ◽  
赵会杰 ZHAO Huijie ◽  
袁祖丽 YUAN Zuli ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Light Stress ◽  
High Light ◽  
High Light Stress ◽  
Regulatory Effects

scholarly journals Enzymes degraded under high light maintain proteostasis by transcriptional regulation in Arabidopsis

2021 ◽  
Author(s):  
Lei Li ◽  
Owen Duncan ◽  
Diep R Ganguly ◽  
Chun Pong Lee ◽  
Peter A Crisp ◽  
...  
Keyword(s):  
Protein Degradation ◽  
Light Stress ◽  
High Light ◽  
Coupled Analysis ◽  
Protein Abundance ◽  
Mrna Levels ◽  
Transcriptional Responses ◽  
High Light Stress ◽  
Degradation Rates

Photo-inhibitory high light stress in Arabidopsis leads to increases in markers of protein degradation and transcriptional upregulation of proteases and proteolytic machinery, but proteostasis is largely maintained. We find significant increases in the in vivo degradation rate for specific molecular chaperones, nitrate reductase, glyceraldehyde-3 phosphate dehydrogenase, and phosphoglycerate kinase and other plastid, mitochondrial, peroxisomal, and cytosolic enzymes involved in redox shuttles. Coupled analysis of protein degradation rates, mRNA levels, and protein abundance reveal that 57% of the nuclear-encoded enzymes with higher degradation rates also had high light-induced transcriptional responses to maintain proteostasis. In contrast, plastid-encoded proteins with enhanced degradation rates showed decreased transcript abundances and must maintain protein abundance by other processes. This analysis reveals a light-induced transcriptional program for nuclear-encoded genes, beyond the regulation of PSII D1 subunit and the function of PSII, to replace key protein degradation targets in plants and ensure proteostasis under high light stress.  

Effect of Thrombin on Phosphorylation of Platelet Membrane Proteins

1976 ◽  
Vol 35 (03) ◽  
pp. 635-642 ◽  
Author(s):  
M Steiner
Keyword(s):  
Protein Kinase ◽  
Kinase Activity ◽  
Qualitative Change ◽  
Protein Kinase Activity ◽  
Protein Substrates ◽  
Phosphoprotein Phosphatase ◽  
Progressive Loss ◽  
Platelet Membranes ◽  
Endogenous Protein ◽  
Considerable Loss

SummaryThe effect of thrombin on the phosphorylating activity of platelet membranes was compared to that of trypsin. Preincubation of non-32P phosphorylated platelet membranes with or without either of these two enzymes resulted in a considerable loss of membrane protein kinase activity which was most severe when trypsin was used. Protein kinase activity and endogenous protein acceptors decreased in parallel. 32P-phosphorylated membranes showed a slow but progressive loss of label which was accelerated by trypsin. Thrombin under these conditions prevented the loss of 32P-phosphate. These results are interpreted to indicate a thrombin-induced destruction of a phosphoprotein phosphatase. The protein kinase activity of phosphorylated platelet membranes using endogenous or exogenous protein substrates showed a significant reduction compared to non-phosphorylated membranes suggesting a deactivation of protein kinase by phosphorylation of platelet membranes. Neither thrombin nor trypsin caused a qualitative change in the membrane polypeptides accepting 32P-phosphate but resulted in quantitative alterations of their ability to become phosphorylated.

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