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

Donev, Rossen Mintchev, Doneva, Teodora A., Bowen, W. Richard and Sheer, Denise 2002. HnRNP-A1 binds directly to double-stranded DNA in vitro within a 36 bp sequence. Molecular and Cellular Biochemistry 233 (1-2) , pp. 181-185. 10.1023/A:1015504318726

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Abstract

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 binRNP-A1.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine
Subjects:	R Medicine > R Medicine (General)
Uncontrolled Keywords:	hnRNP-A1; DNA-binding; atomic force microscopy (AFM); protein-DNA interaction.
Publisher:	Springer Verlag
ISSN:	0300-8177
Last Modified:	19 Mar 2016 23:46
URI:	https://orca.cardiff.ac.uk/id/eprint/64540

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