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• W2023270883 startingPage "2205" @default.
• W2023270883 abstract "The essential RNA helicase, Mtr4, performs a critical role in RNA processing and degradation as an activator of the nuclear exosome. The molecular basis for this vital function is not understood and detailed analysis is significantly limited by the lack of structural data. In this study, we present the crystal structure of Mtr4. The structure reveals a new arch-like domain that is specific to Mtr4 and Ski2 (the cytosolic homologue of Mtr4). In vivo and in vitro analyses demonstrate that the Mtr4 arch domain is required for proper 5.8S rRNA processing, and suggest that the arch functions independently of canonical helicase activity. In addition, extensive conservation along the face of the putative RNA exit site highlights a potential interface with the exosome. These studies provide a molecular framework for understanding fundamental aspects of helicase function in exosome activation, and more broadly define the molecular architecture of Ski2-like helicases." @default.
• W2023270883 created "2016-06-24" @default.
• W2023270883 creator A5005188301 @default.
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• W2023270883 creator A5078791951 @default.
• W2023270883 creator A5088209220 @default.
• W2023270883 date "2010-05-28" @default.
• W2023270883 modified "2023-10-08" @default.
• W2023270883 title "The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing" @default.
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• W2023270883 doi "https://doi.org/10.1038/emboj.2010.107" @default.
• W2023270883 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2905245" @default.
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• W2023270883 hasPublicationYear "2010" @default.
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