Conformational changes of DNA minicircles upon the binding of the archaebacterial histone-like protein MC1.
J Biol Chem
; 270(11): 6286-91, 1995 Mar 17.
Article
em En
| MEDLINE
| ID: mdl-7890766
ABSTRACT
Binding of the archaebacterial histone-like protein MC1 to DNA minicircles has been examined by gel retardation and electron microscopy. MC1 preferentially binds to a 207-base pair relaxed DNA minicircle as compared with the linear fragment. Random binding is observed at very low ionic strength, and a slight increase in salt concentration highly favors the formation of a complex that corresponds to the binding of two MC1 molecules per DNA ring. Measurements of dissociation rates show that this complex is remarkably stable, and electron microscopy reveals that it is characterized by two diametrically opposed kinks. These results are discussed in regard to the mechanisms by which MC1 affects DNA structure.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ribonucleoproteínas
/
Proteínas de Bactérias
/
DNA Circular
/
Methanosarcina
/
Proteínas Arqueais
/
Conformação de Ácido Nucleico
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
França