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Complexes of HMO1 with DNA: Structure and Affinity. | LitMetric

AI Article Synopsis

  • * Research using circular dichroism spectroscopy shows that the HMO1:DNA complex forms without altering the structure of either component, indicating a stable interaction.
  • * Molecular modeling studies highlight that specific regions in HMO1 enhance the stability of the DNA complex, particularly when binding to IFHL sequences, which may clarify the protein's selective recognition of certain DNA regions.

Article Abstract

HMO1 is an architectural nuclear DNA-binding protein that stimulates the activity of some remodelers and regulates the transcription of ribosomal protein genes, often binding to a DNA motif called IFHL. However, the molecular mechanism dictating this sequence specificity is unclear. Our circular dichroism spectroscopy studies show that the HMO1:DNA complex forms without noticeable changes in the structure of DNA and HMO1. Molecular modeling/molecular dynamics studies of the DNA complex with HMO1 Box B reveal two extended sites at the N-termini of helices I and II of Box B that are involved in the formation of the complex and stabilize the DNA bend induced by intercalation of the F114 side chain between base pairs. A comparison of the affinities of HMO1 for 24 bp DNA fragments containing either randomized or IFHL sequences reveals a twofold increase in the stability of the complex in the latter case, which may explain the selectivity in the recognition of the IFHL-containing promoter regions.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11430298PMC
http://dx.doi.org/10.3390/biom14091184DOI Listing

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