PMID: 9524232Apr 3, 1998Paper

Involvement of phosphorylation in binding of nuclear scaffold proteins from rat liver to a highly repetitive DNA component

Biochimica Et Biophysica Acta
Y HibinoN Sugano

Abstract

The results of our previous work [Hibino et al., Biochim. Biophys. Acta 1174 (1993) 162-170] suggested that a highly repetitive DNA component facilitates bending of the helix axis to be recognized by the nuclear scaffold proteins from rat liver, P123 and P130. In the present experiment, it was shown that binding of these proteins to such a repetitive DNA component from rat liver nuclei (370-bp XmnI fragment) is based on a cooperative mode of interaction, although the binding activity of P130 is much higher than that of P123. The immunoblot analysis with anti-phosphoamino acid antibodies suggested that phosphorylation of serine and threonine residues occurs on P123 and P130, but also of tyrosine residue(s) on P130. The phosphatase assay showed that phosphoryl groups on these proteins may be involved in altering the DNA binding activities of the proteins. Thus, the results in the present study imply that phosphorylation of a nuclear scaffold protein in addition to the degree of bending of the DNA helix axis plays an important role in anchoring chromatin to the nuclear scaffold and in construction of a higher-order chromatin structure.

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Citations

Mar 26, 2005·Chromosome Research : an International Journal on the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology·Inna S KuznetsovaOlga I Podgornaya
Jul 4, 2006·Biochimica Et Biophysica Acta·Yasuhide HibinoKoichi Hiraga
Jan 12, 2021·JCI Insight·Ahmed M Malik, Sami J Barmada

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