Interaction of high mobility group proteins HMG 1 and HMG 2 with nucleosomes studied by gel electrophoresis |
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Authors: | M. Štros V. V. Shick A. V. Belyavsky A. D. Mirzabekov |
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Affiliation: | (1) Institute of Biophysics, Czechoslovak Academy of Sciences, Královopolská 135, 612 65 Brno, Czechoslovakia;(2) Institute of Molecular Biology, Academy of Sciences of the USSR, 32 Vavilov Str., GSP-1, V-344 Moscow, USSR |
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Abstract: | The binding of isolated high mobility group proteins HMG (1+2) with nucleosomes was studied using gel electrophoresis. The interaction of HMG (1+2) with mononucleosomes could be detected as a new discrete electrophoretic band with a decreased mobility only after cross-linking of HMG (1+2)-nucleosome complex by formaldehyde. Approximately two molecules of the large HMG proteins were bound per nucleosomal particle of a DNA length of 185 base pairs, lacking histones H1 and H5. Using the same techniques, no binding was observed with core particles of a DNA length of 145 base pairs. |
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