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Complexes of HMO1 with DNA: Structure and Affinity.
- Source :
-
Biomolecules (2218-273X) . Sep2024, Vol. 14 Issue 9, p1184. 13p. - Publication Year :
- 2024
-
Abstract
- Saccharomyces cerevisiae 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 2218273X
- Volume :
- 14
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Biomolecules (2218-273X)
- Publication Type :
- Academic Journal
- Accession number :
- 180015680
- Full Text :
- https://doi.org/10.3390/biom14091184