Insight into the interaction between the RNA helicase CGH-1 and EDC-3 and its implications.
Sci Rep
; 11(1): 20359, 2021 10 13.
Article
em En
| MEDLINE
| ID: mdl-34645931
ABSTRACT
Previous studies indicated that the P-body components, CGH-1 and EDC-3 may play a crucial role in the regulation of lifespan in Caenorhabditis elegans. Homo sapiens DDX6 or Saccharomyces cerevisiae Dhh1p (CGH-1 in C. elegans) could form complexes with EDC3 (Edc3p in yeast), respectively, which is significant for translation inhibition and mRNA decay. However, it is currently unclear how CGH-1 can be recognized by EDC-3 in C. elegans. Here, we provided structural and biochemical insights into the interaction between CGH-1 and EDC-3. Combined with homology modeling, mutation, and ITC assays, we uncovered an interface between CGH-1 RecA2 domain and EDC-3 FDF-FEK. Additionally, GST-pulldown and co-localization experiments confirmed the interaction between CGH-1 and EDC-3 in vitro and in vivo. We also analyzed PATR-1-binding interface on CGH-1 RecA2 by ITC assays. Moreover, we unveiled the similarity and differences of the binding mode between EDC-3 and CAR-1 or PATR-1. Taken together, these findings provide insights into the recognition of DEAD-box protein CGH-1 by EDC-3 FDF-FEK motif, suggesting important functional implications.
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Base de dados:
MEDLINE
Assunto principal:
RNA Nucleotidiltransferases
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Saccharomyces cerevisiae
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Caenorhabditis elegans
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RNA Helicases
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Proteínas de Saccharomyces cerevisiae
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Proteínas de Caenorhabditis elegans
Idioma:
En
Ano de publicação:
2021
Tipo de documento:
Article