{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Y"],"funding":["Ministry of Science and Technology of China","USTC research funds","fundamental research funds for the central universities","National Natural Science Foundation of China"],"pagination":["20359"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8514580"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_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. "],"journal":["Scientific reports"],"pubmed_title":["Insight into the interaction between the RNA helicase CGH-1 and EDC-3 and its implications."],"pmcid":["PMC8514580"],"funding_grant_id":["31870760","WK2070000145","2019YFA0508403","31970669","KY2070000075"],"pubmed_authors":["Yang K","Zhang Y","Hong J","Wang K","Shi Y"],"additional_accession":[]},"is_claimable":false,"name":"Insight into the interaction between the RNA helicase CGH-1 and EDC-3 and its implications.","description":"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. ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2026-05-09T01:25:01.925Z","creation":"2022-02-11T12:10:31.722Z"},"accession":"S-EPMC8514580","cross_references":{"pubmed":["34645931"],"doi":["10.1038/s41598-021-99919-0"]}}