Homodimers of chromosomal proteins HMG-14 and HMG-17 in nucleosome cores.
In this work, we report that nucleosome core particles interact with an equimolar mixture of the chromosomal proteins HMG-14 and HMG-17 to form, exclusively, complexes containing two molecules of either HMG-14 or HMG-17 (homodimers). Analysis of the binding of various mixtures of wild-type proteins and their deletion mutants indicates that homodimer formation is not dependent on contacts between the nucleosome-bound HMG-14/-17 proteins themselves. We suggest that HMG-14/-17 proteins in nucleosomes cross-talk by inducing specific allosteric transitions in the chromatin subunit.
Postnikov
Y V
YV
Laboratory of Molecular Carcinogenesis, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Trieschmann
L
L
Rickers
A
A
Bustin
M
M
D000494:Allosteric Regulation; D000918:Antibody Specificity; D006609:High Mobility Group Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D009707:Nucleosomes / Q000378:metabolism*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D017384:Sequence Deletion
D006609:High Mobility Group Proteins; D009707:Nucleosomes; D011994:Recombinant Proteins