On the mechanism of induction of heterochromatin by the RNA-binding protein vigilin.
Vigilin is an RNA-binding protein localized to both the cytoplasm and the nucleus and has been previously implicated in heterochromatin formation and chromosome segregation. We demonstrate here that the C-terminal domain of human vigilin binds to the histone methyltransferase SUV39H1 in vivo. This association is independent of RNA and maps ... to a site on vigilin that is not involved in its interaction with several other known protein partners. Cells that express high levels of the C-terminal fragment display chromosome segregation defects, and ChIP analyses show changes in the status of pericentric beta-satellite and rDNA chromatin from heterochromatic to more euchromatic form. Finally, a cell line with inducible expression of the vigilin C-terminal fragment displays inducible alterations in beta-satellite chromatin. These and other results lead us to present a new model for vigilin-mediated, RNA-induced gene silencing.
Mesh Terms:
Antigens, Nuclear, Cell Line, Chromatin Immunoprecipitation, Chromosome Segregation, DEAD-box RNA Helicases, DNA-Binding Proteins, Gene Silencing, Heterochromatin, Humans, Methyltransferases, Neoplasm Proteins, Protein Structure, Tertiary, RNA, RNA-Binding Proteins, Repressor Proteins
Antigens, Nuclear, Cell Line, Chromatin Immunoprecipitation, Chromosome Segregation, DEAD-box RNA Helicases, DNA-Binding Proteins, Gene Silencing, Heterochromatin, Humans, Methyltransferases, Neoplasm Proteins, Protein Structure, Tertiary, RNA, RNA-Binding Proteins, Repressor Proteins
RNA
Date: Sep. 01, 2008
PubMed ID: 18648073
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