Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7)

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FIGURE 3.
FIGURE 3.

Zcchc11 and Zcchc6 have a highly similar domain organization and can both mediate Lin28-dependent pre-let-7 uridylation in vitro. (A) Schematic showing the domain similarities between hZcchc11 and hZcchc6 with the N-terminal C2H2 zinc finger highlighted and critical zinc finger residues in bold. (B) Uridylation assay with Flag-IP WT mZcchc11 and a mutant harboring point mutations in two conserved asparates required for catalysis, with or without Flag-IP Lin28. (C) Alignment of the nucleotidyl transferase (Ntr) domains of hZcchc11 and hZcchc6. Aspartic acid residues critical for catalysis are boxed. (D) α-Flag WB showing relative amounts of Flag-hZcchc11 and Flag-hZcchc6 (left) or Flag-hLin28A and Flag-hLin28B (right). (E) EMSA showing similar amounts of functional Flag-hLin28A and Flag-hLin28B used in uridylation assays. (F) Uridylation assays using Flag-hZcchc11 or Flag-hZcchc6 with either Flag-hLin28A or Flag-hLin28B. (G) Uridylation assay with Flag-hZcchc6 and r.Lin28A.

This Article

  1. Published in Advance August 16, 2012, doi: 10.1261/rna.034538.112 RNA 18: 1875-1885

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