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. 1980 Jun 25;8(12):2577–2590. doi: 10.1093/nar/8.12.2577

HMG proteins (1 + 2) form beaded structures when complexed with closed circular DNA.

D J Mathis, A Kindelis, C Spadafora
PMCID: PMC324107  PMID: 6253884

Abstract

Structures bearing a resemblance to nucleosomes can be assembled by incubating calf thymus High Mobility Group proteins (1 + 2) with closed circular DNA. These HMG proteins are capable of forming beads and inducing superhelicity when bound to DNA. However, they do not protect from nuclease digestion the discrete DNA fragments characteristic of nucleosomes. The relationship between HMGs (1 + 2) and the "primitive" histone-like DNA-packaging proteins from prokaryotes and mitochondria is discussed.

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