HnRNP-A1 binds directly to double-stranded DNA in vitro within a 36 bp sequence

被引:12
作者
Donev, RM
Doneva, TA
Bowen, WR
Sheer, D
机构
[1] Canc Res UK London Res Inst, Human Cytogenet Lab, Lincolns Inn Field Labs, London WC2A 3PX, England
[2] Univ Coll Swansea, Dept Chem & Biol Proc Engn, Ctr Complex Fluids Proc, Swansea, W Glam, Wales
关键词
hnRNP-A1; DNA-binding; atomic force microscopy (AFM); protein-DNA interaction;
D O I
10.1023/A:1015504318726
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The heterogeneous nuclear ribonucleoprotein A1 (hnRNP-A1) is known as an RNA- and single-stranded DNA-binding protein involved in alternative splicing of mRNA, RNA transport and maintenance of chromosome telomere length. In this study we tested whether this protein could bind directly to double-stranded DNA (dsDNA). Using PCR amplification of target DNA-sequences from human chromosome 11q13 followed by their incubation with hnRNP-A1 and atomic force microscopy (AFM) of the DNA/protein complexes, we found that this protein bound to DNA within a 36 bp sequence. These results were confirmed by electrophoretic mobility shift assay (EMSA). This sequence was found widely dispersed throughout the genome. There is no overlap between the 36 bp sequence and known target sequences in RNA for binding hnRNP-A1.
引用
收藏
页码:181 / 185
页数:5
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