Stabilization of non-histone proteins by copper ions does not alter chromatin properties of polythene chromosomes of Chironomus plumosus

Autor:	Yu. S. Chentsov, M. S. Makarov
Rok vydání:	2011
Předmět:	Biophysics Chromosome chemistry.chemical_element Cell Biology Biology biology.organism_classification Biochemistry Copper Bivalent (genetics) Chromatin chemistry.chemical_compound Histone chemistry medicine biology.protein Chironomus plumosus Swelling medicine.symptom DNA
Zdroj:	Biochemistry (Moscow) Supplement Series A: Membrane and Cell Biology. 5:70-76
ISSN:	1990-7494 1990-7478
DOI:	10.1134/s1990747810051034
Popis:	Our previous study showed that the body of polythene chromosomes can be identified even after removal of all histones and DNA in the presence of 2 mM CuCl2; this suggested that copper ions stabilized the bonds between non-histone proteins. In this study we tried to find out if copper ions bind with non-histone proteins reversibly or irreversibly. It is shown that the bodies of normal chromosomes and chromosomes stabilized by 2 mM CuCl2 swell with partial disappearance of the banding pattern in a hypotonic solution (0.055 M NaCl) without copper ions. The selective removal of bivalent cations by 10 mM EDTA solution resulted in decondensation of normal polythene and stabilized chromosomes. The treatment of nuclear protein matrix of polythene chromosomes preparations with 10 mM EDTA resulted in the swelling of polythene chromosome body and disappearance of the banding pattern but their morphological organization maintained.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::1624fd4efe7509b04cdea3ca9d3eb455 https://doi.org/10.1134/s1990747810051034 Zobrazit plný text záznamu Full text from SpringerLink