High Glutamic and Aspartic Region in Nonhistone Protein HMG(1+2) Unwinds DNA Double Helical Structure1

1 January 1987

journal article
research article
Published by Oxford University Press (OUP) in The Journal of Biochemistry

Vol. 101 (1) , 175-180
https://doi.org/10.1093/oxfordjournals.jbchem.a121888

Abstract

A high mobility group (HMG) nonhistone protein fraction HMG(1+2) from pig thymus, composed. of HMGI and HMG2, has an activity to unwind the double helical structure of DNA (Yoshida, M. and Shimura, K. (1984) J. Biochem. 95,117–124; Makiguchi, K., Chida, .Y., Yoshida, M., and Shimura, K. (1984) J. Biochem. 95, 423–429). The HMG(1+2) was cleaved with trypsin, followed by peptide separation by ionic exchange column chromatography with Polybuffer exchanger PBE94. The effects of five peptide fractions thus obtained on the thermal denatu ration of DNA were measured. A peptide containing a high glutamic and aspartic (HGA) region, of the composition Glu₃₄Asp₁₅Lys₃ unwound DNA depending on the presence of Mg²⁺ or Ca²⁺ while other peptide fractions did not, suggesting that the HGA region in HMG(1+2) is an active site in the unwind reaction of the double helical structure of DNA.

Keywords

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