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ABSTRACT: Incubation (1 hour, 37 degrees C) of nuclei and chromatin from guinea pig spleen (but not from thymus or the liver) resulted in a proteolysis of H1 and H2A histones and accumulation of specific hydrolytic products. Sodium dodecyl sulfate gel electrophoresis revealed a decline in H1 and H2A and the appearance of new protein bands under histone H10 and between H2A and H4. ATP (10 mM) (but not cAMP or PPi) added to the incubation mixture prevented the H1 and H2A digestion and accumulation of the aforementioned products. The ATP, which protects the histones in the nucleus and chromatin from proteinases, promoted the cleavage of cytosolic low molecular weight proteins. The mechanisms of ATP-dependent chromatin structural rearrangements determining the resistance of nuclear proteins to proteolysis are discussed.
Biokhimii͡a (Moscow, Russia) 09/1993; 58(8):1206-12.
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ABSTRACT: A simple and fast method for isolation of large amounts of the histone octamer (H2A-H2B-H3-H4)2 is proposed. This method is based on chromatin adsorption by hydroxyapatite with subsequent extraction of the histone octamer with 50 mM sodium-phosphate buffer containing 4 M NaCl pH 8.0. It was shown that the properties of the histone octamer isolated by this extractive procedure are identical with those of the histone octamer obtained by elution on a Sephadex G-100 column. The histone tetramer (H3-H4)2 and dimer (H2A-H2B) were obtained after gel filtration on Sephadex G-100 in 50 mM sodium-acetate (pH 5.6).
Biokhimii͡a (Moscow, Russia) 11/1991; 56(10):1864-9.
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ABSTRACT: It was shown that rRNA and HnRNA synthesis in rat liver nuclei does not change-within 30 min after intraperitoneal injection of acetylcholine (0.005 mg per 100 g of body weight) but decreases after injection of norepinephrine and epinephrine (0.05 mg per 100 g of body weight). The synthesis of rRNA (but not of HnRNA) increases after injection of hydrocortisone (2,5 mg per 100 g of body weight). The synthesis of HnRNA (but not of rRNA) increases after injection of ACTH1-24 (3 ME per 100 g of body weight) and oxytocin (1 ME per 100 g of body weight). The synthesis of rRNA decreases after injection of propranolol and atropine (0.5 mg per 100 g of body weight). At the same time, the synthesis of HnRNA does not change thereby. The inhibitory effect of propranolol and atropine was corrected by electrostimulation of hypothalamus. The content of cAMP and Ca2+ and the phosphorylation degree of nuclear proteins are increased after stimulation of hypothalamus. The phosphorylation of nuclear proteins is increased by 10(-8)-10(-6) M cAMP. The synthesis of RNA in liver nuclei is increased by 10(-6) M cAMP only after addition of cytosol. In this case the activity of RNA-polymerase II increases in a greater degree than that of RNA-polymerase I + III. It is assumed that the regulatory mechanisms of rRNA and HnRNA synthesis are different. The role of hypothalamus electrostimulation, neurotransmitters, hormones, and cAMP in the mechanisms of RNA synthesis in rat liver nuclei is discussed.
Biokhimii͡a (Moscow, Russia) 09/1984; 49(8):1320-6.
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ABSTRACT: The effect of acidic neurospecific protein S-100 on the phosphorylation of brain and liver nuclear proteins with 1 and 10 microM ATP was investigated. It was shown that protein S-100 increases the phosphorylation of brain nuclear proteins, while antigen D, another acidic neurospecific protein half-identical to 14-3-2 protein, inhibits this process. Ca2+ and cAMP at concentration of 10(-6) M do not affect the phosphorylation of brain nuclear proteins. In control assays the tracer 32P is presumably incorporated into high molecular weight nuclear protein fractions (Mr greater than 40000). After addition of protein S-100 the tracer is mainly incorporated into these proteins as well independently of ATP concentration (1 or 10 microM). The phosphorylation of nuclear proteins with molecular weights above 100000 is mostly increased in this case. At ATP concentration of 1 microM protein S-100 decreases histone phosphorylation 2.3 times but does not affect that of non-histone proteins. However, at 10 microM ATP the inhibitory action of this protein on histone phosphorylation is absent. The possible mechanisms of protein S-100 action on nuclear proteins phosphorylation are discussed.
Biokhimii͡a (Moscow, Russia) 06/1983; 48(5):827-32.
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ABSTRACT: It has been shown that the induction of D-RNA synthesis in rat liver nuclei by electrostimulation of hypothalamus is accompanied by a decrease in chromatin protein synthesis and an increase in phosphorylation and acetylation of chromatin proteins. The decrease of the histone synthesis is mainly due to the decrease of [14C]lysine and [14C]alanine incorporation into histones H1 and H4. The relationship between H1, H2b-H3, H2a and H4 histone fractions remains unchanged. Electrostimulation of hypothalamus increases acetylation of H2a and H4 histone fractions and phosphorylation of all histones with the exception of histone H1.
Biokhimii͡a (Moscow, Russia) 10/1980; 45(9):1669-74.
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Fiziologicheskiĭ zhurnal SSSR imeni I. M. Sechenova 09/1979; 65(8):1226-30.
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Doklady Akademii nauk SSSR 02/1979; 247(5):1278-80.
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ABSTRACT: The kinetics of histone F2b aggregation in the presenceof NaCl and methanole was investigated. The size of aggregates increases during 20 hours, and in the following 13 hours the size of formed complexes does not change. It was shown that the stable colloid system was formed by the olygomers of histone F2b.
Biofizika 12/1976; 21(6):1114-6. · 0.43 Impact Factor
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Doklady Akademii nauk SSSR 09/1973; 211(4):993-5.
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Ukraïns'kyĭ biokhimichnyĭ zhurnal 02/1967; 39(6):577-83.
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Ukraïns'kyĭ biokhimichnyĭ zhurnal 02/1967; 39(3):231-6.
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Ukraïns'kyĭ biokhimichnyĭ zhurnal 02/1967; 39(4):343-51.
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V I Tiulenev
Ukraïns'kyĭ biokhimichnyĭ zhurnal 02/1967; 39(1):11-7.
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Ukraïns'kyĭ biokhimichnyĭ zhurnal 02/1966; 38(4):343-8.
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ABSTRACT: The liver nuclear proteins of 3- and 6-month old rats were studied by the gel-electrophoresis technique after electrostimulation of hypothalamus. In this case new nuclear proteins with low molecular weight were found. The electrophoretic rate of these proteins is higher than that of histone H4. A decrease in the content of histone H2B in the nuclear liver of 6-month old rats was also found after electrostimulation of hypothalamus. The mechanism of this phenomenon is discussed.
Ukrainskii biokhimicheskii zhurnal 59(6):14-8.
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ABSTRACT: 3-5 hours incubation of calf thymus nuclei at 37 degrees C leads to the proteolysis of histones H1, H3 and H2B; 1-10 mM NiCl2 and ZnSO4 inhibits the proteolysis of the histones H1, H3 and H2B.
Ukrainskii biokhimicheskii zhurnal 72(1):48-50.
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ABSTRACT: Effects of nucleotides on the proteolysis of histones in nuclei incubated at 37 degrees C during 1, 3 and 20 h were studied. It has been shown that the H1 histone is removed first during proteolysis and then the H3 and H2B histones are digested. The H4 histone is not cleaved even after 20 h incubation. PMSF and ATP inhibit the H1 cleavage when its structure was not disturbed before ATP, CTP, ADP, NAD+, AMP and NADH inhibit the partial cleavage of the core histones H3 and H2B. ATP, CTP, AMP and NADH prevent the total digestion of H2B. ATP and, at lower extent, CTP prevent the H3 digestion. ATP, CTP, ADP and NAD+ inhibit the cleavage of the H2A histone in the experiments with 20 h incubation, when H4 is only resistant in the absence of nucleotides. The data obtained suggest an important role of ATP and other nucleotides in maintaining the structure of histones and chromatin.
Ukrainskii biokhimicheskii zhurnal 70(6):43-7.
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ABSTRACT: Data on physico-chemical properties and functional role of protein S-100 have been generalized. An analysis of literary data permits making a conclusion that the protein interaction with Ca2+ ions plays great part in its action mechanisms. Data are presented on the properties of the family of Ca-binding proteins similar to protein S-100 as to their structure. Peculiar attention is paid to the analysis of this protein function in the cellular nucleus, changing the degree of proteins phosphorylation and RNA synthesis.
Ukrainskii biokhimicheskii zhurnal 68(3):3-13.
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ABSTRACT: Proteolysis of histones H1b and H1(0) is observed after the incubation of rat spleen nuclei at 37 degrees C during 1 hour. Adenosine triphosphate, inorganic pyrophosphate and nicotinamide adenine dinucleotide decrease the digestion of histone H1b. ATP, PP1 and NAD+, in the case of 3 hours incubation, do not affect proteolysis of H1 histones in rat spleen nuclei. The incubation of rat liver nuclei at 37 degrees C during 1 hour leads to a decrease of the amount of histone H1b and, to much more extent, H1a. In this case ATP, PP1 and NAD+ increase proteolysis of histone H1a but practically do not affect proteolysis of H1b. After 2-hours incubations histone H1a is completely digested but histone H1b is partially preserved: ATP in this case, as well as in spleen nuclei, decreases proteolysis of histone H1b. During the 3 hours incubation, when histones H H1a and H1b are completely digested, partial digestion of histone H3 being observed, ATP does not prevent from proteolysis of histone H1b. A protein appears between the H2A and H4 histones after heating at 37 degrees C in both spleen and liver rat nuclei. Neither ATP nor PP1 and NAD+ affect the amount of this protein. It is suggested that the location of histones H1a and H1b in different chromatin domains determines the digestion of these histones by ATP-dependent proteinases.
Ukrainskii biokhimicheskii zhurnal 68(6):23-9.
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ABSTRACT: Electric stimulation of paraventricular hypothalamic nucleus results in intensification of RNA synthesis in rat brain. Content of acid proteins and RNA in liver and brain chromatin of geese changes in the period of sexual activity controlled by hypothalamus. With long introduction of hydrocortisone content of non-histone proteins of chromatine and RNA as well as total content of RNA in rat liver cells increases. These and other facts confirm the supposition that the central nervous system has an influence on the function of organs and tissues by means of genetical apparatus of cells.
T͡Sitologii͡a i genetika 9(2):138-41.
