Calcium binding to HMG1 protein induces DNA looping by the HMG-box domains
Language English Country England, Great Britain Media print
Document type Journal Article
PubMed
8187884
DOI
10.1016/0014-5793(94)00364-5
PII: 0014-5793(94)00364-5
Knihovny.cz E-resources
- MeSH
- DNA chemistry metabolism MeSH
- Microscopy, Electron MeSH
- Ethylmaleimide pharmacology MeSH
- Liver chemistry MeSH
- Nucleic Acid Conformation * MeSH
- Rats MeSH
- High Mobility Group Proteins chemistry metabolism MeSH
- Recombinant Proteins chemistry metabolism MeSH
- Cattle MeSH
- Thymus Gland chemistry MeSH
- Calcium metabolism pharmacology MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- DNA MeSH
- Ethylmaleimide MeSH
- High Mobility Group Proteins MeSH
- Recombinant Proteins MeSH
- Calcium MeSH
Electron microscopy has shown that non-histone chromosomal HMG1 could induce DNA looping or compaction in the presence (but not in the absence) of Ca2+. The effect of calcium on DNA looping and compaction was interpreted as calcium binding to the acidic C-domain of HMG1. Both individual DNA-binding HMG1-box domains A and B were found to be involved in DNA looping and compaction. Treatment of HMG1 with a thiol-specific reagent, N-ethylmaleimide, inhibited the ability of the protein to induce DNA looping and compaction but not the electrostatic interaction with DNA. These results indicated that cysteine-sulfhydryl groups of the HMG1-box domains A and B are specifically involved in DNA looping and compaction, and that in the absence of calcium the acidic C-domain down-regulates these effects by modulation of the DNA-binding properties of the HMG1-box domains.
References provided by Crossref.org
Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1
