A conformational study of the sequence specific binding of HMG-I (Y) with the bovine interleukin-2 cDNA.
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.
Lehn
D A
DA
Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4350.
Elton
T S
TS
Johnson
K R
KR
Reeves
R
R
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D006609:High Mobility Group Proteins / Q000378:metabolism*; D007376:Interleukin-2 / Q000235:genetics*; D009691:Nucleic Acid Denaturation; D011485:Protein Binding
D006609:High Mobility Group Proteins; D007376:Interleukin-2; D004247:DNA