CHICKEN MAR BINDING-PROTEIN P120 IS IDENTICAL TO HUMAN HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN (HNRNP)-U

被引:61
作者
VONKRIES, JP
BUCK, F
STRATLING, WH
机构
[1] UNIV HAMBURG,KRANKENHAUS EPPENDORF,INST PHYSIOL CHEM,D-20246 HAMBURG,GERMANY
[2] UNIV HAMBURG,KRANKENHAUS EPPENDORF,INST ZELLBIOCHEM & KLIN NEUROBIOL,D-20246 HAMBURG,GERMANY
关键词
D O I
10.1093/nar/22.7.1215
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 amino acid sequence analysis of tryptic peptides. p120 binds to multiple MAR fragments provided they have a minimal length of approximately 700 bp. Binding of MAR fragments 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 particles, and second as an element in the higher-order organization of chromatin.
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页码:1215 / 1220
页数:6
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