Heterochromatin aggregation during DNA elimination in Tetrahymena is facilitated by a prion-like protein.
J Cell Sci
; 130(2): 480-489, 2017 01 15.
Article
em En
| MEDLINE
| ID: mdl-27909245
ABSTRACT
Regulated aggregations of prion and prion-like proteins play physiological roles in various biological processes. However, their structural roles in the nucleus are poorly understood. Here, we show that the prion-like protein Jub6p is involved in the regulation of chromatin structure in the ciliated protozoan Tetrahymena thermophila Jub6p forms sodium dodecyl sulfate (SDS)-resistant aggregates when it is ectopically expressed in vegetative cells and binds to RNA in vitro Jub6p is a heterochromatin component and is important for the formation of heterochromatin bodies during the process of programmed DNA elimination. We suggest that RNA-protein aggregates formed by Jub6p are an essential architectural component for the assembly of heterochromatin bodies.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Príons
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DNA
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Heterocromatina
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Tetrahymena thermophila
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Agregados Proteicos
Idioma:
En
Revista:
J Cell Sci
Ano de publicação:
2017
Tipo de documento:
Article