ArticleThe Biochemical journal2005
Surface salt bridges modulate the DNA site size of bacterial histone-like HU proteins.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 28 citations in OpenAlex.
- Sodium Ion-Induced Structural Transition on the Surface of a DNA-Interacting Protein.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Phosphorylation Regulation of a Histone-like HU Protein fromProtein and peptide letters · 2022Article
- Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.Extremophiles : life under extreme conditions · 2020Article
- HU ofFrontiers in microbiology · 2018Article
- Structural and mechanistic basis of zinc regulation across the E. coli Zur regulon.PLoS biology · 2014Article
- Rapid purification of HU protein fromMolecular biology research communications · 2014Article
- Cloning the hbs gene from Bacillus subtilis and expression of the HBsu protein in Escherichia coli.Iranian journal of microbiology · 2010Article
- DNA organization by the apicoplast-targeted bacterial histone-like protein of Plasmodium falciparum.Nucleic acids research · 2008Article
- DNA protection by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima.Nucleic acids research · 2008Article
- Transcriptional regulation of multi-drug tolerance and antibiotic-induced responses by the histone-like protein Lsr2 in M. tuberculosis.PLoS pathogens · 2007Article
- Escherichia coli HU protein has a role in the repair of abasic sites in DNA.Nucleic acids research · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial histone-like DNA-binding proteins are best known for their role in compacting the genomic DNA. Of these proteins, HU is ubiquitous and highly conserved across the eubacterial kingdom. Using the HBsu (Bacillus subtilis-encoded HU homologue) as a model, we explore here the molecular basis for the ability of some HU homologues to engage a longer approx. 35 bp DNA site as opposed to the much shorter sites reported for other homologues. Using electrophoretic mobility-shift assays, we show that the DNA site size for HBsu is approx. 10-13 bp and that a specific surface salt bridge limits the DNA site size for HBsu. Surface exposure of the highly conserved Lys3, achieved by substitution of its salt-bridging partner Asp26 with Ala, leads to enhanced DNA compaction by HBsu-D26A (where D26A stands for the mutant Asp26-->Ala), consistent with the interaction of Lys3 with the ends of a 25 bp duplex. Both HBsu and HBsu-D26A bend DNA, as demonstrated by their equivalent ability to promote ligase-mediated DNA cyclization, indicating that residues involved in mediating DNA kinks are unaltered in the mutant protein. We suggest that Lys3 is important for DNA wrapping due to its position at a distance from the DNA kinks where it can exert optimal leverage on flanking DNA and that participation of Lys3 in a surface salt bridge competes for its interaction with DNA phosphates, thereby reducing the occluded site size.
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