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- W2807613466 abstract "Significance Aberrant or unwanted transcripts can be degraded by the RNA exosome with the help of the nuclear exosome-targeting (NEXT) complex. NEXT, composed of RNA-binding protein RBM7, scaffold ZCCHC8, and helicase MTR4, is implicated in stress response, neurodegeneration, and viral ribogenesis. Here, we characterize the activities of NEXT that support its role in exosome-mediated decay. NEXT catalyzes 3′→5′ helicase activity and disrupts RNA:RNA and DNA:RNA duplexes more efficiently than MTR4. Optimal activity is observed when substrates include a uridine-rich motif, for interactions with RBM7, and a 3′ poly(A) tail. The ZCCHC8 C-terminal domain binds the helicase core and can stimulate MTR4 helicase/ATPase activities. Our results highlight the interplay among NEXT subunits to ensure effective targeting of substrates." @default.
- W2807613466 created "2018-06-13" @default.
- W2807613466 creator A5013774625 @default.
- W2807613466 creator A5031957131 @default.
- W2807613466 date "2018-05-29" @default.
- W2807613466 modified "2023-10-16" @default.
- W2807613466 title "Structural basis for MTR4–ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex" @default.
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- W2807613466 doi "https://doi.org/10.1073/pnas.1803530115" @default.
- W2807613466 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6004480" @default.
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- W2807613466 hasPublicationYear "2018" @default.
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