Numerous interactions act redundantly to assemble a tunable size of P bodies in Saccharomyces cerevisiae.
Proc Natl Acad Sci U S A
; 114(45): E9569-E9578, 2017 11 07.
Article
em En
| MEDLINE
| ID: mdl-29078371
ABSTRACT
Eukaryotic cells contain multiple RNA-protein assemblies referred to as RNP granules, which are thought to form through multiple protein-protein interactions analogous to a liquid-liquid phase separation. One class of RNP granules consists of P bodies, which consist of nontranslating mRNAs and the general translation repression and mRNA degradation machinery. P bodies have been suggested to form predominantly through interactions of Edc3 and a prion-like domain on Lsm4. In this work, we provide evidence that P-body assembly can be driven by multiple different protein-protein and/or protein-RNA interactions, including interactions involving Dhh1, Psp2, and Pby1. Moreover, the relative importance of specific interactions can vary with different growth conditions. Based on these observations, we develop a summative model wherein the P-body assembly phenotype of a given mutant can be predicted from the number of currently known protein-protein interactions between P-body components.
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MEDLINE
Assunto principal:
Saccharomyces cerevisiae
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Proteínas de Ligação a RNA
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Partículas de Ribonucleoproteínas em Forma de Abóbada
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Grânulos Citoplasmáticos
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Proteínas de Saccharomyces cerevisiae
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article