Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract.
J Cell Biol
; 119(1): 17-25, 1992 Oct.
Article
em En
| MEDLINE
| ID: mdl-1527167
ABSTRACT
The role of the Drosophila lamin protein in nuclear envelope assembly was studied using a Drosophila in vitro assembly system that reconstitutes nuclei from added sperm chromatin or naked DNA. Upon incubation of the embryonic assembly extract with anti-Drosophila lamin antibodies, the attachment of nuclear membrane vesicles to chromatin surface and nuclear envelope formation did not occur. Lamina assembly and nuclear membrane vesicles attachment to the chromatin were inhibited only when the activity of the 75-kD lamin isoform was inhibited in both soluble and membrane-vesicles fractions. Incubation of decondensed sperm chromatin with an extract that was depleted of nuclear membranes revealed the presence of lamin molecules on the chromatin periphery. In addition, high concentrations of bacterially expressed lamin molecules added to the extract, were able to associate with the chromatin periphery, and did not inhibit nuclear envelope assembly. After nuclear reconstitution, a fraction of the lamin pool was converted into the typical 74- and 76-kD isoforms. Together, these data strongly support an essential role of the lamina in nuclear envelope assembly.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
DNA
/
Proteínas Nucleares
/
Cromatina
/
Núcleo Celular
/
Membrana Nuclear
Limite:
Animals
Idioma:
En
Revista:
J Cell Biol
Ano de publicação:
1992
Tipo de documento:
Article
País de afiliação:
Israel