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 Terminal uridylyltransferases are writers of poly(U) tails in diverse RNA uridylation pathways. In the let-7 pathway, the LIN28:pre-let-7:TUTase ribonucleoprotein complex regulates the processing and maturation of the let-7 microRNA, and plays an important role in both physiology and disease. The presence of redundant TUTase orthologs and the diverse pathways poses challenges to revealing the molecular mechanisms of TUTases. We developed a precise tool to identify nanobodies that inhibited the LIN28:pre-let-7:TUTase interaction. The nanobody Nb-S2A4 specifically interacted with the LIN28:let-7 interaction fragment in TUT4, which is critical for oligouridylation and monouridylation of let-7. Our data illustrate that the nanobody tool is effective in distinguishing functions among protein orthologs and diverse pathways.

A nanobody targeting the LIN28:let-7 interaction fragment of TUT4 blocks uridylation of let-7