Metaphase-specific phosphorylations weaken the association between chromosomal proteins HMG 14 and 17, and DNA.
The high-mobility-group proteins HMG 14 and 17 have been isolated from human cells arrested in metaphase. The affinity between an unphosphorylated and two phosphorylated forms of these proteins, and DNA has been investigated using columns of single-stranded and double-stranded DNA. It was shown that the most phosphorylated forms had much lower affinity for single-stranded and double-stranded DNA compared to the unphosphorylated form present in interphase cells. The results are in accordance with the view that HMG 14 and 17 may dissociate transiently from chromatin during mitosis.
Lund
T
T
Department of Biochemistry, University of Oslo, Norway.
Berg
K
K
D002853:Chromatography, Liquid; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004586:Electrophoresis; D006367:HeLa Cells; D006609:High Mobility Group Proteins / Q000378:metabolism*; D006801:Humans; D008677:Metaphase; D010766:Phosphorylation; D014407:Tumor Cells, Cultured
D004268:DNA-Binding Proteins; D006609:High Mobility Group Proteins; D004247:DNA