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Search Results: 1 - 10 of 51063 matches for " D1 protein "
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Eucalyptus ESTs corresponding to the enzyme glutamine synthetase and the protein D1, sites of action of herbicides that cause oxidative stress
Velini, Edivaldo Domingues;Trindade, Maria Lúcia Bueno;Alves, Elza;Cataneo, Ana Catarina;Marino, Celso Luis;Maia, Ivan de Godoy;Mori, Edson Seizo;Furtado, Edson Luiz;Guerrini, Iraê Amaral;Wilcken, Carlos Frederico;
Genetics and Molecular Biology , 2005, DOI: 10.1590/S1415-47572005000400010
Abstract: this work was aimed at locating eucalyptus ests corresponding to the gs enzyme (glutamine synthetase, ec = 6.3.1.2) and to the d1 protein, which are directly related to resistance to herbicides that promote oxidative stress. glutamine synthetase corresponds to the site of action of the herbicide glufosinate. herbicides that belong to groups such as ureas, uracils, triazines and triazinones act on the d1-qb complex (receptor of electrons from the photosystem ii) by inactivating it. the clusters egeqrt3302e01.g, egeqrt3001f12.b; egezlv1203b04.g; egbgfb1211h06.g and egezlv1205f09.g enclosed complete sequences (with 356 amino acids) of the glutamine synthetase enzyme. the cluster egeqsl1054g06.g is a consensus of four reads and enclosed a complete sequence of d1 protein (with 353 amino acids). the comparison of the sequences of protein d1 from different species showed that the substitutions of serine (s) by glycine (g) or serine (s) by threonine (t) at the position 264 could produce plants resistant to herbicides that act on electron flow on photosystem ii. the sequence of amino acids corresponding to the cluster egeqsl1054g06.g had a serine in position 264 indicating sensitivity of the eucalyptus plants to herbicides that act on this site.
Specific degradation of photosystem II D1 protein by a protease (Alr3815) in heterocysts of the cyanobacterium Anabaena sp. PCC7120
GuoHua Yang,Bin Hu,JinDong Zhao
Chinese Science Bulletin , 2011, DOI: 10.1007/s11434-010-4329-3
Abstract: Some filamentous cyanobacteria form heterocysts under conditions lacking combined nitrogen for nitrogen fixation. Photosystem II is removed from heterocyst during the process of cell differentiation. Here, we demonstrate that Alr3815 is a protease that is capable of degrading D1 protein of photosystem II. Strain-322, which lacks alr3815, is impaired in nitrogen fixation in air because some oxygen evolving activity is retained in its heterocysts. Our results also suggest that calcium may play a regulatory role in D1 degradation during heterocyst differentiation.
Effects of salicylic acid on protein kinase activity and chloroplast D1 protein degradation in wheat leaves subjected to heat and high light stress

Hui-Jie Zhao,Xue-Juan Zhao,Pei-Fang M,Yue-Xia Wang,Wei-Wei Hu,Li-Hong Li,Yi-Dan Zhao,

生态学报 , 2011,
Abstract: In the north of China, wheat plants are often stressed by heat and high light during grain-filling stage, which leads to injury in photosynthetic apparatus and decline in photosynthetic rate. In order to develop a method to protect photosynthetic apparatus in wheat leaves subjected to heat and high light stress, the effects of SA (salicylic acid) and FSBA (5′-p-fluorosulfonylbenzoyl adenosine) on PK (protein kinase) activity, D1 protein degradation and the performance of PSII were investigated in present work. Our results showed that PK activity enhanced under heat and high light stress and declined when stress was removed. FSBA pretreatment resulted in marked decreases in PK activity and D1 protein level, suggesting a correlationship between degradation of D1 protein and phosphorylation. After 2 h of stress, D1 protein level in water-pretreated leaves decreased to 79% of control and then recovered to 81% after 3 h of recovery. This clearly indicated that the damage of D1 protein induced by heat and high light stress was reversible. Compared to the control, SA pretreatment could not only increase PK activity, retard the degradation of D1 protein during heat and high light stress, but also accelerate the recovery of D1 protein level when the stress was removed. Correspondingly, Fv/Fm (maximum photochemical efficiency of PSII), ΦPSII (actual photochemical efficiency of PSII), ETR (electron transfer rate) and Pn (net photosynthetic rate) in SA-treated leaves were higher than that in leaves of control under both stress and non-stress conditions. Taken together, our results revealed that SA pretreatment could significantly alleviate damages of heat and high light stress on D1 protein and PSII of wheat leaves, and accelerate restoration of photosynthetic function.
Relationships between D1 protein, xanthophyll cycle and photodamage-resistant capacity in rice (Orysa sativa L.)
Benhua Ji,Demao Jiao
Chinese Science Bulletin , 2000, DOI: 10.1007/BF02886214
Abstract: Relationships between D1 protein, xanthophyll cycle and subspecific difference of photodamage-resistant capacity have been studied inO. japonica rice varieties 02428 and 029 (photoinhibition-tolerance) andO. indica rice varieties 3037 and Palghar (photoinhibition-sensitivity) and their reciprocal cross F1 hybrids after photoinhibitory treatment. It was shown that PS II photochemical efficiency (F v /F m) decreased, and xanthophyll cycle from violaxanthin (V), via anaxanthin (A), to zeaxanthin (Z) was enhanced and non-photochemical quenching (qN) increased accordingly in SM-pretreated leaves of rice when the synthesis of D1 protein was inhibited, and that there was a decrease inqN and, as a result, more loss of D1 protein and a big decrease inF v/F m in DTT-pretreated leaves when xanthophyll cycle was inhibited.O. japonica subspecies had a higher maintaining capacity of D1 protein and a decrease ofF v/F m in a more narrow range, and exhibited more resistance against photodamage, as compared withO. indica subspecies. The above physiological indexes in reciprocal cross F1 hybrids, though between the values of their parents, were closer to maternal lines than to paternal lines. Experimental results support the concept that the turnover capacity for D1 protein is an important physiological basis of photoinhibition-tolerance, and will provide the physiological basis for selection of the photoinhibition-tolerant parents and develop a new approach to breed hybrids with high photosynthetic efficiency.
Involvement of DEG5 and DEG8 proteases in the turnover of the photosystem II reaction center D1 protein under heat stress in Arabidopsis thaliana
XuWu Sun,LiYuan Wang,LiXin Zhang
Chinese Science Bulletin , 2007, DOI: 10.1007/s11434-007-0275-0
Abstract: Deg5, deg8 and the double mutant, deg5deg8 of Arabidopsis thaliana were used to study the physiological role of the DEG proteases in the repair cycle of photosystem II (PSII) under heat stress. PSII activity in deg mutants showed increased sensitivity to heat stress, and the extent of this effect was greater in the double mutant, deg5deg8, than in the single mutants, deg5 and deg8. Degradation of the D1 protein was slower in the mutants than in the WT plants. Furthermore, the levels of other PSII reaction center proteins tested remained relatively stable in the mutant and WT plants following high-temperature treatment. Thus, our results indicate that DEG5 and DEG8 may have synergistic function in degradation of D1 protein under heat stress.
Trans-activation of the human SOX3 promoter by MAZ in NT2/D1 cells
Kova?evi?-Gruji?i? Nata?a,Yokoyama Kazunari K.,Stevanovi? Milena
Archives of Biological Sciences , 2008, DOI: 10.2298/abs0803379k
Abstract: In this study, we examine the role of three highly conserved putative binding sites for Myc-associated zinc finger protein (MAZ) in regulation of the human SOX3 gene expression. Electrophoretic mobility shift and supershift assays indicate that complexes formed at two out of three MAZ sites of the human SOX3 promoter involve ubiquitously expressed MAZ protein. Furthermore, in cotransfection experiments we demonstrate that MAZ acts as a positive regulator of SOX3 gene transcription in both undifferentiated and RA-differentiated NT2/D1 cells. Although MAZ increased both basal and RA-induced promoter activity, our results suggest that MAZ does not contribute to RA inducibility of the SOX3 promoter during neuronal differentiation of NT2/D1 cells.
Varying light regimes in naturally growing Jatropha curcus: pigment, proline and photosynthetic performance
Wadhwa R.,N. Kumari,V. Sharma
Journal of Stress Physiology & Biochemistry , 2010,
Abstract: Light stress is a major abiotic stress which adversely affects productivity of the plants. Tolerance to abiotic stresses is very complex, due to the intricate of interactions between stress factors and various molecular, biochemical and physiological phenomena affecting plant growth and development. In many cases, high yield potential can contribute to yield in moderate stress environment. We studied chlorophyll (Chl) a fluorescence parameters and analyzed D1 core protein in one year old plants of Jatropha curcus under different light regimes (10–1200 μmol m–2 s–1) in sun and shade plants. Chl a fluorescence provides insights into the responses of the photosynthetic system to increasing irradiance. Total Chl content was 1.43 and 0.61 mg/g-1 FM for shade and sun exposed plants respectively. The effective quantum yield (ΔF/Fm') of the sun plants was lower as compared to shade plants but the amount of the D1 core protein was higher in plants grown under high light intensity. A decrease in ΔF/Fm' indicates down regulation of photosynthesis or photoinhibition. D1 protein is the membrane protein complex of the PSII reaction centre. The degradation of D1 protein may regulate the functioning of the PSII repair cycle under photoinhibitory conditions. It has been shown that low-light grown or shade plants are more susceptible to photoinhibition than high light or sun plants. This higher susceptibility is accompanied by slow degradation of damaged D1 protein. High light intensity or exposure to photooxidation leads to the irreversible damage in photosynthetic performance and consequently has an overall inhibitory effect on crop productivity.
comment to the article: Upregulation of anti-human ribosomal protein S6-p240, topoisomerase II , cyclin D1, Bcl-2 and anti-corneal antibodies in acute psoriasis
Takashi Hashimoto,Daisuke Tsuruta,Takahiro Hamada,Teruki Dainichi
Our Dermatology Online , 2011,
Abstract:
Upregulation of anti-human ribosomal protein S6-p240, topoisomerase II , cyclin D1, Bcl-2 and anti-corneal antibodies in acute psoriasis
Abreu Velez Ana Maria,Howard William R.,Howard Michael S.
Our Dermatology Online , 2011,
Abstract: Background. The immunopathogenesis of psoriasis is complex, and involves alterations in the innate immunologic system Case Report: A 57-year-old female was evaluated for the presence of rapidly appearing plaques on the knees and elbows. Methods: Skin biopsies for hematoxylin and eosin examination, as well as for direct immunofluorescence and immunohistochemistry analysis were performed. Results: H&E examination demonstrated classic features of psoriasis. Direct immunofluorescence revealed positive anti-corneal antibodies with several immunoglobulins, as well as positivity to upper and deep small dermal blood vessels. Immunohistochemistry revealed an increased expression of survivin, anti-human-ribosomal protein S6-p240, Topoisomerase II , cyclin D1, and Bcl-2 in lesional plaques. Conclusions: The pathobiology of psoriasis seems to involve a series of molecules involved in a complex interaction between the inflammation itself, cell cycle regulation, and ectopic expression of selected molecules.
Epstein-Barr virus-encoded latent membrane protein 1 modulates cyclin D1 by c-Jun/Jun B heterodimers
Xin Song,Yongguang Tao,Liang Zeng,Jing Yang,Faqing Tang,Leo M. Lee,Jianping Gong,Qiao Wu,Ya Cao
Science China Life Sciences , 2005, DOI: 10.1360/03yc0251
Abstract: In our recent studies, we found that LMP1 encoded by Epstein-Barr virus could accelerate the formation of active c-Jun/Jun B heterodimer. We studied the regulation of cyclinD1 by c-Jun/Jun B heterodimers by laser scanning confocal influorescence microscopy, Western blot, luciferase activity assay, super-EMSA and flow cytometry in the Tet-on-LMP1 HNE2 cell line, in which LMP1 expression was regulated by Tet-on system. c-Jun/Jun B heterodimers induced by LMP1 could up regulate cyclin D1 promoter activity and expression. Overexpression of cyclinD1 accelerated the progression of cell cycle.
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