Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae.
J Cell Biol
; 179(3): 437-49, 2007 Nov 05.
Article
en En
| MEDLINE
| ID: mdl-17984320
ABSTRACT
Processing bodies (P-bodies) are cytoplasmic RNA granules that contain translationally repressed messenger ribonucleoproteins (mRNPs) and messenger RNA (mRNA) decay factors. The physical interactions that form the individual mRNPs within P-bodies and how those mRNPs assemble into larger P-bodies are unresolved. We identify direct protein interactions that could contribute to the formation of an mRNP complex that consists of core P-body components. Additionally, we demonstrate that the formation of P-bodies that are visible by light microscopy occurs either through Edc3p, which acts as a scaffold and cross-bridging protein, or via the "prionlike" domain in Lsm4p. Analysis of cells defective in P-body formation indicates that the concentration of translationally repressed mRNPs and decay factors into microscopically visible P-bodies is not necessary for basal control of translation repression and mRNA decay. These results suggest a stepwise model for P-body assembly with the initial formation of a core mRNA-protein complex that then aggregates through multiple specific mechanisms.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Asparagina
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Ribonucleoproteínas
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Saccharomyces cerevisiae
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Ribonucleoproteína Nuclear Pequeña U4-U6
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Proteínas de Saccharomyces cerevisiae
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Glutamina
Tipo de estudio:
Prognostic_studies
Idioma:
En
Año:
2007
Tipo del documento:
Article