Intrinsically disordered N-terminal regions suppress cotranslational protein degradation.

N-terminal intrinsically disordered regions suppress cotranslational protein degradation, with the human hRpl7A IDR reducing CFTR CTPD by over 80% when transplanted.

• Why it matters: IDRs are usually viewed as proteolysis-promoting, but how they affect cotranslational degradation during synthesis is unclear.
• What they did: Mapping the degron of yeast ribosomal protein Rpl8A showed its N-terminal IDR suppresses CTPD while the adjacent structured domain acts as a degron; nine additional yeast proteins were tested, and conservation was examined in human cells.
• The result: The N-terminal IDR of human ribosomal protein hRpl7A protects against CTPD, and mass spectrometry indicates HSP70 chaperones Ssa and Ssb bind the Rpl8A N-terminal IDR, implying chaperone recruitment supports cotranslational folding.

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