Ontology highlight
ABSTRACT:
SUBMITTER: Yamashita S
PROVIDER: S-EPMC6488673 | biostudies-literature | 2019 Apr
REPOSITORIES: biostudies-literature
Yamashita Seisuke S Nagaike Takashi T Tomita Kozo K
Nature communications 20190429 1
Lin28-dependent oligo-uridylylation of precursor let-7 (pre-let-7) by terminal uridylyltransferase 4/7 (TUT4/7) represses let-7 expression by blocking Dicer processing, and regulates 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) of TUT4/7. Here, we report crystallographic and biochemical analyses of the LIM ...[more]