The phosphate groups of the high mobility group like protein P1 strengthens its affinity for DNA

• Published in: Biochemical and biophysical research communications Vol. 185; no. 3; pp. 1091 - 1097
• Main Authors: Østvold, Anne Carine, Hullstein, Ingunn, Laland, Søren G.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 30.06.1992; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Autoradiography; Biological and medical sciences; Blotting, Western; Chromatography, Affinity; DNA - metabolism; DNA, Single-Stranded; Fundamental and applied biological sciences. Psychology; HeLa Cells; High Mobility Group Proteins - isolation & purification; High Mobility Group Proteins - metabolism; Holoproteins; Humans; Liver - metabolism; Nuclear proteins; Phosphates - metabolism; Phosphorus Radioisotopes; Phosphorylation; Proteins; Rats; CaM kinase II; CK-2; TCA; HMG; d.s. DNA; s.s. DNA; PCA; Human; Rat; Liver; Rodentia; High mobility group protein; Molecular interaction; Single stranded DNA; Hela cell line; Structure function relationship; Vertebrata; Double stranded DNA; Mammalia; Binding capacity
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(92)91738-C

PCA soluble proteins isolated from rat liver and proliferating HeLa interphase cells were subjected to chromatography on columns containing immobilized s.s and d.s DNA. P1 from rat liver was eluted from s.s. and d.s DNA between 0,20 and 0,45 M NaCl, while dephosphorylated P1 was not retained by s.s. and d.s. DNA columns at 0,25 M, suggesting that phosphate groups enhance the affinity of P1 for DNA. P1 from proliferating HeLa interphase cells exhibit increased affinity for d.s. as well as s.s. DNA when compared to rat liver P1. The higher extent of phosphorylation in proliferating cells supports the finding that phosphate enhances rather than reduces the affinity of P1 for DNA.