Abstract：
:LIN28 is an RNA binding protein that plays crucial roles in pluripotency, glucose metabolism, tissue regeneration, and tumorigenesis. LIN28 binds to the let-7 primary and precursor microRNAs through bipartite recognition and induces degradation of let-7 precursors (pre-let-7) by promoting oligouridylation by terminal uridylyltransferases (TUTases). Here, we report that the zinc knuckle domain (ZKD) of mouse LIN28 recruits TUT4 to initiate the oligouridylation of let-7 precursors. Our crystal structure of human LIN28 in complex with a fragment of pre-let-7f-1 determined to 2.0 Å resolution shows that the interaction between ZKD and RNA is constrained to a small cavity with a high druggability score. We demonstrate that the specific interaction between ZKD and pre-let-7 is necessary and sufficient to induce oligouridylation by recruiting the N-terminal fragment of TUT4 (NTUT4) and the formation of a stable ZKD:NTUT4:pre-let-7 ternary complex is crucial for the acquired processivity of TUT4.
journal_name
Cell Repjournal_title
Cell reportsauthors
Wang L,Nam Y,Lee AK,Yu C,Roth K,Chen C,Ransey EM,Sliz Pdoi
10.1016/j.celrep.2017.02.044subject
Has Abstractpub_date
2017-03-14 00:00:00pages
2664-2675issue
11issn
2211-1247pii
S2211-1247(17)30242-5journal_volume
18pub_type
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