English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance The Dcp2 decapping enzyme targets mRNA for degradation and thereby plays a role in the regulation of gene expression. Despite numerous static crystal structures of the enzyme, it remained unclear how its catalytic activity correlates with the relative domain orientation in Dcp2. Here we used solution-state NMR spectroscopic methods and find that the active state of Dcp2 is only stably formed in the presence of the Dcp1 and Edc1 activator proteins and the mRNA cap. Importantly, our solution data provide a conclusive view of how the Dcp2 structure changes during the catalytic cycle and provide a unique example of the importance of integrated structural biology approaches to unravel the mechanism behind complex molecular machines.

Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme