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1.
Photosynth Res ; 133(1-3): 215-223, 2017 Sep.
Article in English | MEDLINE | ID: mdl-28110449

ABSTRACT

Membrane fluidity is the important regulator of cellular responses to changing ambient temperature. Bacteria perceive cold by the transmembrane histidine kinases that sense changes in thickness of the cytoplasmic membrane due to its rigidification. In the cyanobacterium Synechocystis, about a half of cold-responsive genes is controlled by the light-dependent transmembrane histidine kinase Hik33, which also partially controls the responses to osmotic, salt, and oxidative stress. This implies the existence of some universal, but yet unknown signal that triggers adaptive gene expression in response to various stressors. Here we selectively probed the components of photosynthetic machinery and functionally characterized the thermodynamics of cyanobacterial photosynthetic membranes with genetically altered fluidity. We show that the rate of oxidation of the quinone pool (PQ), which interacts with both photosynthetic and respiratory electron transport chains, depends on membrane fluidity. Inhibitor-induced stimulation of redox changes in PQ triggers cold-induced gene expression. Thus, the fluidity-dependent changes in the redox state of PQ may universally trigger cellular responses to stressors that affect membrane properties.


Subject(s)
Cold-Shock Response/physiology , Membrane Fluidity/physiology , Synechocystis/physiology , Anisotropy , Cold Temperature , Fatty Acids/metabolism , Fluorescence , Gene Expression Regulation, Bacterial , Kinetics , Membrane Lipids/metabolism , Oxidation-Reduction , Plastoquinone/metabolism , Spectrum Analysis, Raman , Synechocystis/genetics
2.
Biochim Biophys Acta ; 1848(6): 1277-84, 2015 Jun.
Article in English | MEDLINE | ID: mdl-25753112

ABSTRACT

Conjugation to penetrating cations is a general approach for intramitochondrial delivery of physiologically active compounds, supported by a high membrane potential of mitochondria having negative sign on the matrix side. By using fluorescence correlation spectroscopy, we found here that Atto520-biotin, a conjugate of a fluorescent cationic rhodamine-based dye with the membrane-impermeable vitamin biotin, accumulated in energized mitochondria in contrast to biotin-rhodamine 110. The energy-dependent uptake of Atto520-biotin by mitochondria, being slower than that of the conventional mitochondrial dye tetramethyl-rhodamine ethyl ester, was enhanced by the hydrophobic anion tetraphenylborate (TPB). Atto520-biotin also exhibited accumulation in liposomes driven by membrane potential resulting from potassium ion gradient in the presence valinomycin. The induction of electrical current across planar bilayer lipid membrane by Atto520-biotin proved the ability of the compound to permeate through lipid membrane in a cationic form. Atto520-biotin stained mitochondria in a culture of L929 cells, and the staining was enhanced in the presence of TPB. Therefore, the fluorescent Atto520 moiety can serve as a vehicle for intramitochondrial delivery of hydrophilic drugs. Of importance for biotin-streptavidin technology, binding of Atto520-biotin to streptavidin was found to cause quenching of its fluorescence similar to the case of fluorescein-4-biotin.


Subject(s)
Azo Compounds/metabolism , Biotin/metabolism , Electricity , Lipid Bilayers/metabolism , Mitochondria, Liver/metabolism , Animals , Azo Compounds/chemistry , Biotin/chemistry , Cations , Kinetics , Microscopy, Fluorescence , Mitochondria, Liver/drug effects , Organometallic Compounds/metabolism , Permeability/drug effects , Rats , Spectrometry, Fluorescence , Streptavidin/metabolism , Tetraphenylborate/pharmacology , Time Factors
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