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A conformational study of the sequence specific binding of HMG-I (Y) with the bovine interleukin-2 cDNA
D A Lehn1, T S Elton, K R Johnson
1Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4350.
Biochemistry International
|May 1, 1988
Abstract:
The DNA sequence specific interaction of the high mobility group non-histone protein HMG-I (Y) with the 3' untranslated region of the bovine interleukin-2 cDNA has been studied. Circular dichroism and thermal denaturation studies suggest that HMG-I (Y) alters the conformational state and increases the thermal stability of the DNA. Additionally, amino acid sequence analysis suggests that the previously identified non-histone protein HMG-Y is an isoform of HMG-I.