Jp. Vonkries et al., CHICKEN MAR BINDING-PROTEIN P120 IS IDENTICAL TO HUMAN HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN (HNRNP)-U, Nucleic acids research, 22(7), 1994, pp. 1215-1220
We have previously identified two proteins from chicken oviduct nuclei
that specifically bind to matrix/scaffold attachment regions (MARs/SA
Rs). Here one of these proteins, named p120 due to its apparent molecu
lar weight, is purified to near homogeneity and shown to be identical
to a previously described component of heterogeneous nuclear ribonucle
oprotein particles, hnRNP U, on the basis of amino acid sequence analy
sis of tryptic peptides. p120 binds to multiple MAR fragments provided
they have a minimal length of approximately 700 bp. Binding of MAR fr
agments is specifically competed by homoribopolymers poly(G) and poly(
l), which form four-stranded structures. Our results suggest that p120
/hnRNP U may serve a dual function, first as a component of hnRNP part
icles, and second as an element in the higher-order organization of ch
romatin.