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Developmental and hormonal regulation of the arabidopsis CER2 gene that codes for a nuclear-localized protein required for the normal accumulation of cuticular waxes. 总被引:3,自引:1,他引:2
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The previously cloned CER2 gene is required for the normal accumulation of cuticular waxes and encodes a novel protein. Earlier reports suggested that the CER2 protein is either a membrane-bound component of the fatty acid elongase complex or a regulatory protein. Cell fractionation and immunoblot analyses using polyclonal antibodies raised against a chemically synthesized peptide with a sequence based on the predicted CER2 protein sequence have demonstrated that the 47-kD CER2 protein is soluble and nuclear localized. These results are consistent with CER2 being a regulatory protein. Detailed studies of plants harboring a CER2 promoter/GUS transgene (CER2-GUS), in combination with immunoblot analyses, revealed that CER2 is expressed and the CER2 protein accumulates in a variety of organs and cell types. Expression is highest early in the development of these organs and is epidermis specific in most tissues. In agreement with the activity of the CER2 promoter in hypocotyls, cuticular wax accumulates on this organ in a CER2-dependent fashion. In leaves CER2 expression is confined to the guard cells, trichomes, and petioles. However, application of the cytokinin 6-benzylaminopurine induces ectopic expression of CER2-GUS in all cell types of leaves that emerge following treatment. 相似文献
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Grace G. Y. Lim Doreen S. K. Chua Adeline H. Basil Hui-Ying Chan Chou Chai Thiruma Arumugam Kah-Leong Lim 《The Journal of biological chemistry》2015,290(27):16882-16893
The potential cellular function of the 53-kDa cytosolic form of PINK1 (PINK1-53) is often overlooked because of its rapid degradation by the proteasome upon its production. Although a number of recent studies have suggested various roles for PINK1-53, how this labile PINK1 species attains an adequate expression level to fulfil these roles remains unclear. Here we demonstrated that PINK1-53 is stabilized in the presence of enhanced Lys-63-linked ubiquitination and identified TRAF6-related NF-κB activation as a novel pathway involved in this. We further showed that a mimetic of PINK1-53 promotes mitophagy but, curiously, in apparently healthy mitochondria. We speculate that this “non-selective” form of mitophagy may potentially help to counteract the build-up of reactive oxygen species in cells undergoing oxidative stress and, as such, represent a cytoprotective response. 相似文献
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Summary The influence of the asymmetric addition of various divalent cations and protons on the properties of active Ca2+ transport have been examined in intact human red blood cells. Active Ca2+ efflux was determined from the initial rate of45Ca2+ loss after CoCl2 was added to block Ca2+ loading via the ionophore A23187. Ca2+-ATPase activity was measured as phosphate production over 5 min in cells equilibrated with EGTA-buffered free Ca2+ in the presence of A23187. The apparent Ca affinity of active Ca2+ efflux (K
0.5=30–40 mol/liter cells) was significantly lower than that measured by the Ca2+-ATPase assay (K
0.5=0.4 m). Possible reasons for this apparent difference are considered. Both active Ca2+ efflux and Ca2+-ATPase activity were reduced to less than 5% of maximal levels (20 mmol/liter cells · hr) in Mg2+-depleted cells, and completely restored by reintroduction of intracellular Mg2+. Active Ca2+ efflux was inhibited almost completely by raising external CaCl2 (but not MgCl2) to 20mm, probably by interaction of Ca2+ at the externally oriented E2P conformation of the pump. Cd2+ was more potent than Ca2+ in this inhibition, while Mn2+ was less potent and 10mm Ba2+ was without effect. A Ca2+: proton exchange mechanism for active Ca2+ efflux was supported by the results, as external protons (pH 6–6.5) stimulated active Ca2+ efflux at least twofold above the efflux rate at pH 7.8 Ca2+ transport was not affected by decreasing the membrane potential across the red cell. 相似文献