Replication protein A induces the unwinding of long double-stranded DNA regions - PubMed (original) (raw)
. 1996 May 31;259(1):104-12.
doi: 10.1006/jmbi.1996.0305.
Affiliations
- PMID: 8648638
- DOI: 10.1006/jmbi.1996.0305
Replication protein A induces the unwinding of long double-stranded DNA regions
K Treuner et al. J Mol Biol. 1996.
Abstract
We have investigated nucleoprotein filaments composed of human replication protein A (RPA) and DNA by electron microscopy. At low ionic strengths, RPA complexes with single-stranded DNA are similar in length to protein-free DNA suggesting that RPA-bound DNA remains in an extended configuration under these conditions. However, severe compaction of RPA-DNA complexes occurs in buffers with > 2 mM MgCl2 or with 100 mM NaCl. At low ionic strengths, RPA binds to A + T-rich internal regions of linear double-stranded simian virus 40 (SV40) DNA and induces separation of complementary DNA strands. RPA also binds to closed-circular SV40 DNA, but requires the function of a DNA topoisomerase to invade and completely unwind duplex DNA regions. The ability of RPA to unwind long stretches of double-stranded DNA is not shared by the bacterial single-strand binding protein and the phage T4 gene 32 protein.
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