AI Article Synopsis
- HU is a nucleoid-associated protein that plays a crucial role in organizing bacterial DNA and is involved in processes like DNA repair and transposition.
- HU has a specific binding affinity for DNA with mismatched regions longer than 3 base pairs and also for bulged DNA, binding single-stranded DNA (ssDNA) in a unique way that differs from traditional interactions with double-stranded DNA.
- HU's preferential binding to poly(dG) indicates its potential importance in protecting bacterial DNA from damage, as it covers ssDNA without destabilizing double-helical structures.
Article Abstract
The nucleoid-associated protein HU plays an important role in bacterial nucleoid organization and is involved in numerous processes including transposition, recombination and DNA repair. We show here that HU binds specifically DNA containing mismatched region longer than 3 bp as well as DNA bulges. HU binds single-stranded DNA (ssDNA) in a binding mode that is reminiscent but different from earlier reported specific HU interactions with double-helical DNA lesions. An HU dimer requires 24 nt of ssDNA for initial binding, and 12 nt of ssDNA for each additional dimer binding. In the presence of equimolar amounts of HU dimer and DNA, the ssDNA molecule forms an U-loop (hairpin-like) around the protein, providing contacts with both sides of the HU body. This mode differs from the binding of the single-strand-binding protein (SSB) to ssDNA: in sharp contrast to SSB, HU binds ssDNA non-cooperatively and does not destabilize double-helical DNA. Furthermore HU has a strong preference for poly(dG), while binding to poly(dA) is the weakest. HU binding to ssDNA is probably important for its capacity to cover and protect bacterial DNA both intact and carrying lesions.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2241890 | PMC |
| http://dx.doi.org/10.1093/nar/gkm667 | DOI Listing |
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