Reference: Zhang Y, et al. (2021) Insight into the interaction between the RNA helicase CGH-1 and EDC-3 and its implications. Sci Rep 11(1):20359

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Abstract


Previous studies indicated that the P-body components, CGH-1 and EDC3 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 EDC3 in C. elegans. Here, we provided structural and biochemical insights into the interaction between CGH-1 and EDC3. Combined with homology modeling, mutation, and ITC assays, we uncovered an interface between CGH-1 RecA2 domain and EDC3 FDF-FEK. Additionally, GST-pulldown and co-localization experiments confirmed the interaction between CGH-1 and EDC3 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 EDC3 and CAR1 or PATR-1. Taken together, these findings provide insights into the recognition of DEAD-box protein CGH-1 by EDC3 FDF-FEK motif, suggesting important functional implications.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Zhang Y, Wang K, Yang K, Shi Y, Hong J
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