Abstract
The high mobility group (HMG) proteins1 are a small set of nonhistone chromatin proteins which exhibit preferential affinity for single-stranded DNA2–4. Large portions of the amino acid sequences of calf thymus HMG-1 and HMG-2 have recently been published5. We have analysed that information and describe here an internal sequence homology in the proteins which, coupled with a prediction of secondary structure, strongly suggests that all the high molecular weight HMG proteins (HMG-1, HMG-2 and HMG-E) exist in three domains of comparable lengths. The N-terminal and central domains have homologous sequences and are probably similar in conformation. The C-terminal domain is nonhomologous and highly acidic. We also present results of trypsin digestion experiments which are consistent with the postulated domain structure. We propose that the N-terminal and central domains of the proteins are DNA-binding regions and that the highly acidic C-terminal domain interacts with histones.
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Reeck, G., Isackson, P. & Teller, D. Domain structure in high molecular weight high mobility group nonhistone chromatin proteins. Nature 300, 76–78 (1982). https://doi.org/10.1038/300076a0
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DOI: https://doi.org/10.1038/300076a0
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