Nucleic Acids Research, 1994, Vol. 22, No. 7 1215-1220
© 1994
MOLECULAR BIOLOGY |
Chicken MAR binding protein p120 is identical to human heterogeneous nuclear ribonucleoprotein (hnRNP) U
Institut für Physiologische Chemie, Universitäts-Krankenhaus Eppendorf Martinistr. 52, D-20246 Hamburg, Germany 1Institut für Zellbiochemie und Klinische Neurobiologie, Universitäts-Krankenhaus Eppendorf Martinistr. 52, D-20246 Hamburg, Germany
*To whom correspondence should be addressed
Received December 22, 1993. Revised March 4, 1994. Accepted March 4, 1994.
We have previously identified two proteins from chicken oviduct nuclei that specifically bind to matrix/scaffold attachment regions (MARs/SARs). Here one of these proteins, named p120 due to its apparent molecular weight, is purified to near homogeneity and shown to be identical to a previously described component of heterogeneous nuclear ribonucleoprotein particles, hnRNP U, on the basis of amlno acid sequence analysis of tryptic peptldes. p120 binds to multiple MAR fragments provided they have a minimal length of approximately 700 bp. Binding of MAR fragments is specifically competed by homoribo-polymers poly(G) and poly (I), which form four-stranded structures. Our results suggest that p120/hnRNP U may serve a dual function, first as a component of hnRNP particles, and second as an element in the higher-order organization of chromatin.
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