ArticleScientific reports2016
Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 25 citations in OpenAlex.
- Modeling the role of charged residues in thermophilic proteins by rotamer and dynamic cross correlation analysis.Journal of molecular modeling · 2023Article
- Article
- Structure-based inhibitors targeting the alpha-helical domain of the Spiroplasma melliferum histone-like HU protein.Scientific reports · 2020Article
- The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Consensus protein engineering on the thermostable histone-like bacterial protein HUs significantly improves stability and DNA binding affinity.Extremophiles : life under extreme conditions · 2020Article
- Nucleoid-Associated Protein HU: A Lilliputian in Gene Regulation of Bacterial Virulence.Frontiers in cellular and infection microbiology · 2019Review
- Comparison of histone-like HU protein DNA-binding properties and HU/IHF protein sequence alignment.PloS one · 2017Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The three-dimensional structure of the histone-like HU protein from the mycoplasma Spiroplasma melliferum KC3 (HUSpm) was determined at 1.4 Å resolution, and the thermal stability of the protein was evaluated by differential scanning calorimetry. A detailed analysis revealed that the three-dimensional structure of the HUSpm dimer is similar to that of its bacterial homologues but is characterized by stronger hydrophobic interactions at the dimer interface. This HUSpm dimer interface lacks salt bridges but is stabilized by a larger number of hydrogen bonds. According to the DSC data, HUSpm has a high denaturation temperature, comparable to that of HU proteins from thermophilic bacteria. To elucidate the structural basis of HUSpm thermal stability, we identified amino acid residues potentially responsible for this property and modified them by site-directed mutagenesis. A comparative analysis of the melting curves of mutant and wild-type HUSpm revealed the motifs that play a key role in protein thermal stability: non-conserved phenylalanine residues in the hydrophobic core, an additional hydrophobic loop at the N-terminal region of the protein, the absence of the internal cavity present at the dimer interface of some HU proteins, and the presence of additional hydrogen bonds between the monomers that are missing in homologous proteins.
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