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Biomedical subjects

G Russev

Publications and source records attributed to G Russev.

At least 73 records · Page 4Linked to original sources
PubMed1980

Histone exchange in chromatin of hydroxyurea-blocked Ehrlich ascites tumour cells.

It is well established that DNA and histone synthesis are tightly coupled. Nevertheless, these two processes can be partially uncoupled by drugs specifically inhibiting protein or DNA synthesis, and also during n-butyrate-induced differentiation of Friend cells. The fate of the histones synthesized in the absence of DNA synthesis is unknown; they could be: (1) degraded without joining chromatin; (2) deposited on chromatin as extra histones; or (3) replace original chromatin histones. The only data concerning this problem are a recent report supporting the second possibility. We present evidence here in favour of the third possibility by showing that the histones synthesized in the absence of DNA synthesis enter chromatin and become organized in nucleosomes.

Animals↗
PubMed1980

Salt-induced structural changes in nucleosomes.

Ehrlich ascites tumor (EAT) nucleosomes treated with increasing NaCl concentrations were analyzed by sucrose density gradient centrifugation. Two events were found to take place in the course of the salt treatment: a) increasing amounts of nucleosomes dissociated into free DNA and protein in the interval 0.6M-1.5M NaCl, and b) the sedimentation coefficient of the nucleosomes decreased from 11S to 8S in the interval 0.6M - 1M NaCl. This decrease was not caused by loss of protein and was fully reversible upon slow and gradual lowering of the ionic strength. This shows that before dissociation of the protein core from DNA, nucleosomes undergo a structural transition. The electron microscopic observations revealed that it consisted in detachment of the ends of nucleosomal DNA from the protein core. It is suggested that an arginine-rich domain in the protein core exists, which holds more tightly the central part of the nucleosomal DNA, while its ends are relatively loosely bound to lysine-rish domains.

Animals↗
PubMed1977

Endogenous proteolytic activity of chromatin.

Chromatin from rat liver and Ehrlich ascites tumor (EAT) was isolated by two different procedures and the chromatin preparations were incubated at 37 degrees C. To follow the proteolysis at 0, 4, 8, and 24 hrs, aliquots were taken and analysed by SDS polyacrylamide gel electrophoresis. Although there were some differences in the proteolytic activity of the different chromatins, in general they were found to sustain a several hours incubation without appreciable degradation to occur. However, when prior to incubation the chromatins were dissociated, a rapid proteolysis took place. This shows that there are specific, chromatin bound proteinases that are inactive while immobilized in the chromatin structure and become activated on dissociation.

Animals↗
PubMed1976

Distribution of histones in alkali-denatured chromatin studied by isopycnic centrifugation in alkaline metrizamide density gradients.

Three types of density gradients - neutral metrizamide, alkaline NaOH-metrizamide and alkaline triethanolamine-metrizamide - were used for studying the distribution of histones between the two DNA strands in alkali-denatured chromatin. It was found possible to avoid both protein redistribution and dissociation by using triethanolamine-metrizamide density gradients at pH 10.5. Under these conditions an alkali-denatured mixture of DNA and chromatin was well separated into the original DNA and DNP. When native or sonicated chromatin was denatured at pH 12.2 and centrifuged in a triethanolamine-metrizamide density gradient at pH 10.5 no peak of free DNA appeared. These results show that both DNA strands remain associated with histone molecules upon alkaline denaturation of chromatin.

Animals↗
PubMed1975

Fractionation of rat-liver-chromatin nonhistone proteins into two groups with different metabolic rates.

In the pH interval 10.5-11.8, 70% of the nonhistone proteins normally present in rat liver chromatin were dissociated. The rest remained complexed with DNA even at pH 13. Dodecylsulfate-polyacrylamide gel electrophoresis revealed that the majority of the high-molecular-weight nonhistone proteins together with a few characteristic fractions with molecular weights of 40 000-60 000 remained in the alkali-resistant group. L-[14C]Leucine pulse-labelling experiments showed that the specific radioactivity of the alkali-labile nonhistone proteins was 2-3 times higher than that of the alkali-resistant nonhistone proteins, which, in turn, had the same specific radioactivity as that of the histones. The same held true for chromatin from regenerating rat liver. In the course of a 21-day chase the specific radioactivity of the alkali-labile nonhistone proteins gradually decreased and finally became 3 times lower than that of the alkali-resistant nonhistone proteins. On the contrary, the ratio of the specific radioactivities of the alkali-resistant nonhistone proteins and of the histones to the specific radioactivity of DNA remained constant during the chase. A conclusion can be drawn that a fraction of liver nonhistone proteins exists which is alkali-resistant and is conserved in chromatin like histones.

Animals↗