Thermal denaturation and fluorescence study of nucleosomes containing non-histone chromosomal protein HMG2
Language English Country Netherlands Media print
Document type Journal Article
PubMed
3676320
DOI
10.1016/0167-4781(87)90069-8
PII: 0167-4781(87)90069-8
Knihovny.cz E-resources
- MeSH
- Protein Denaturation MeSH
- Erythrocytes ultrastructure MeSH
- Spectrometry, Fluorescence MeSH
- Chickens MeSH
- Nucleosomes ultrastructure MeSH
- High Mobility Group Proteins isolation & purification physiology MeSH
- Cattle MeSH
- Hot Temperature MeSH
- Animals MeSH
- Check Tag
- Cattle MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Nucleosomes MeSH
- High Mobility Group Proteins MeSH
Interaction of calf thymus non-histone chromosomal protein HMG2 with H1,H5-depleted nucleosomes from chicken erythrocytes was studied by means of thermal denaturation and an N-(3-pyrene)maleimide fluorescence probe. Under low ionic conditions (2 mM Tris buffer plus EDTA) addition of 1-2 molecules of HMG2 per nucleosome markedly stabilized the segment of the linker DNA against thermal denaturation. Under approximately physiological ionic conditions (0.1 M NaCl) addition of two HMG2 molecules per nucleosome, labeled by N-(3-pyrene)maleimide at the sulfhydryl groups of Cys-110 of histones H3, resulted in a decrease of the pyrene excimer fluorescence corresponding to the slight movement of the sulfhydryl groups of the two histone H3 molecules apart.
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