title: A conformational study of the sequence specific binding of HMG-I (Y) with the bovine interleukin-2 cDNA.
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.
authors.affiliation: Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4350.
authors.forename: D A
authors.initials: DA
authors.lastname: Lehn
authors.forename: T S
authors.initials: TS
authors.lastname: Elton
authors.forename: K R
authors.initials: KR
authors.lastname: Johnson
authors.forename: R
authors.initials: R
authors.lastname: Reeves
mesh_terms: 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
chemical_list: D006609:High Mobility Group Proteins; D007376:Interleukin-2; D004247:DNA