NUCLEAR MATRIX PROTEIN ARBP RECOGNIZES A NOVEL DNA-SEQUENCE MOTIF WITH HIGH-AFFINITY

被引:42
作者
BUHRMESTER, H [1 ]
VONKRIES, JP [1 ]
STRATLING, WH [1 ]
机构
[1] UNIV HAMBURG,HOSP EPPENDORF,INST PHYSIOL CHEM,D-20246 HAMBURG,GERMANY
关键词
D O I
10.1021/bi00012a029
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
ARBP is a nuclear protein that specifically binds to matrix/scaffold attachment regions (MARs/SARs). Here we characterize by DNase I footprinting, dimethyl sulfate protection, and mobility shift assays two binding sites for ARBP within a chicken lysozyme MAR fragment. Our results indicate that ARBP recognizes a novel DNA sequence motif containing the central sequence 5'-GGTGT-3' and flanking AT-rich sequences. Binding occurs through major groove contacts to two guanines of the central sequence. Collective and single-base substitutions in the 5'-GGTGT-3' core motif result in loss or significant reductions of ARBP binding, underscoring the importance of the GC-rich core sequence. Structural elements of the sequence motif are probably also recognized. The affinity of ARBP to both binding sites is surprisingly high [K-D = (2-6) x 10(-10) M]. High-affinity recognition of the identified DNA motif in MARs/SARs by ARBP is likely an important feature in the domain organization of chromatin.
引用
收藏
页码:4108 / 4117
页数:10
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