Calcium binding to HMG1 protein induces DNA looping by the HMG-box domains
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články
PubMed
8187884
DOI
10.1016/0014-5793(94)00364-5
PII: 0014-5793(94)00364-5
Knihovny.cz E-zdroje
- MeSH
- DNA chemie metabolismus MeSH
- elektronová mikroskopie MeSH
- ethylmaleimid farmakologie MeSH
- játra chemie MeSH
- konformace nukleové kyseliny * MeSH
- krysa rodu Rattus MeSH
- proteiny s vysokou pohyblivostí chemie metabolismus MeSH
- rekombinantní proteiny chemie metabolismus MeSH
- skot MeSH
- thymus chemie MeSH
- vápník metabolismus farmakologie MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- DNA MeSH
- ethylmaleimid MeSH
- proteiny s vysokou pohyblivostí MeSH
- rekombinantní proteiny MeSH
- vápník 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.
Citace poskytuje Crossref.org
Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1
