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TitleMechanistic insights into Lin28-dependent oligo-uridylylation of pre-let-7 by TUT4.
Journal, issue, pagesNucleic Acids Res, Vol. 54, Issue 1, Year 2026
Publish dateJan 5, 2026
AuthorsXiaojie Han / Seisuke Yamashita / Kozo Tomita /
PubMed AbstractLin28-dependent oligo-uridylylation of precursor let-7 (pre-let-7) by terminal uridylyltransferases 4 and 7 (TUT4/7) represses let-7 expression by blocking Dicer processing, thereby regulating cell ...Lin28-dependent oligo-uridylylation of precursor let-7 (pre-let-7) by terminal uridylyltransferases 4 and 7 (TUT4/7) represses let-7 expression by blocking Dicer processing, thereby regulating cell differentiation and proliferation. The interaction between the Lin28:pre-let-7 complex and the N-terminal Lin28-interacting module (LIM) of TUT4/7 is required for pre-let-7 oligo-uridylylation by the C-terminal catalytic module (CM). Here, we report the cryogenic electron microscopy structure of human TUT4 complexed with Lin28A and oligo-uridylated pre-let-7, representing the elongation stage of oligo-uridylylation. Structural and biochemical analyses suggest that, after recruitment of pre-let-7 to the LIM through interactions between its terminal stem-loop and Lin28A, the CM associates with the LIM through protein-protein interactions. The double-stranded stem region of pre-let-7 is surrounded by the CM and LIM, the upper portion of the duplex unwinds, and the 3' end of pre-let-7 is positioned in the CM catalytic site for the initiation of oligo-uridylylation. At the oligo-uridylylation stage, the CM finger domain clamps the double-stranded region of pre-let-7, thereby further stabilizing the pre-let-7:TUT4 complex, enabling processive elongation of the uridine tail by the CM. Thus, the LIM functions as a stable anchor, working together with Lin28A to ensure efficient and processive oligo-uridylylation of pre-let-7.
External linksNucleic Acids Res / PubMed:41521656 / PubMed Central
MethodsEM (single particle)
Resolution3.78 - 3.82 Å
Structure data

65642

9w4r

EMDB-65642, PDB-9w4r:
Cryo-EM structure of hTUT4_mini:hLin28A:pre-let-7g miRNA_UUU, conformation 1
Method: EM (single particle) / Resolution: 3.78 Å

65643

9w4s

EMDB-65643, PDB-9w4s:
Cryo-EM structure of hTUT4_mini:hLin28A:pre-let-7g miRNA_UUU, conformation 2
Method: EM (single particle) / Resolution: 3.82 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / Complex / TUTase

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