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Structural and functional basis of mammalian microRNA biogenesis by Dicer

D. Zapletal, E. Taborska, J. Pasulka, R. Malik, K. Kubicek, M. Zanova, C. Much, M. Sebesta, V. Buccheri, F. Horvat, I. Jenickova, M. Prochazkova, J. Prochazka, M. Pinkas, J. Novacek, DF. Joseph, R. Sedlacek, C. Bernecky, D. O'Carroll, R. Stefl, P. Svoboda

. 2022 ; 82 (21) : 4064-4079.e13. [pub] 2022Nov03

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem, komentáře

Perzistentní odkaz   https://www.medvik.cz/link/bmc22032737
E-zdroje Online Plný text

NLK Cell Press Free Archives od 1997-12-01 do Před 1 rokem
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Free Medical Journals od 1997 do Před 1 rokem
Open Access Digital Library od 1997-12-01
Elsevier Open Access Journals od 1997-12-01 do 2023-06-15
Elsevier Open Archive Journals od 1997-12-01 do Před 1 rokem

Odkazy

PubMed 36332606
DOI 10.1016/j.molcel.2022.10.010
Knihovny.cz E-zdroje

MicroRNA (miRNA) and RNA interference (RNAi) pathways rely on small RNAs produced by Dicer endonucleases. Mammalian Dicer primarily supports the essential gene-regulating miRNA pathway, but how it is specifically adapted to miRNA biogenesis is unknown. We show that the adaptation entails a unique structural role of Dicer's DExD/H helicase domain. Although mice tolerate loss of its putative ATPase function, the complete absence of the domain is lethal because it assures high-fidelity miRNA biogenesis. Structures of murine Dicer•-miRNA precursor complexes revealed that the DExD/H domain has a helicase-unrelated structural function. It locks Dicer in a closed state, which facilitates miRNA precursor selection. Transition to a cleavage-competent open state is stimulated by Dicer-binding protein TARBP2. Absence of the DExD/H domain or its mutations unlocks the closed state, reduces substrate selectivity, and activates RNAi. Thus, the DExD/H domain structurally contributes to mammalian miRNA biogenesis and underlies mechanistical partitioning of miRNA and RNAi pathways.

Citace poskytuje Crossref.org

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