Abstract
HMG-like proteins were isolated from nuclei of the acellular slime mold Physarum polycephalum. These proteins represented 0.6 ± 0.2% of nuclear proteins and approx. 6% of DNA by weight. Polyacrylamide gel electrphoresis demonstrated the presence of 3 major proteins, designated HMG-1P, HMG-2P and HMG-14/17P. None of these proteins comigrated with any of the calf thymus HMGs. Physarum HMG-like proteins were found to be preferentially associated with transcriptionally active chromatin fraction, as well as being released from nuclei by light DNase I digestion. In contrast, the content of histone H1 was significantly lower in active than in inactive chromatin fraction.
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