Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein.
AUTOR(ES)
Kamata, N
RESUMO
FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=359728Documentos Relacionados
- Inhibitory effect of myristylation on transrepression by FBR (Gag-Fos) protein.
- N-ethylmaleimide inhibition of the DNA-binding activity of the herpes simplex virus type 1 major DNA-binding protein.
- Helix-destabilizing properties of the adenovirus DNA-binding protein.
- Nucleoside triphosphate-dependent DNA-binding properties of mos protein.
- Detection of a novel minisatellite-specific DNA-binding protein.
