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Showing 1–7 of 7 results
Advanced filters: Author: Chris J. Norbury Clear advanced filters

  • Turnover of mRNA has mainly been studied in the budding yeast, Saccharomyces cerevisiae, and is thought to be initiated by deadenylation. Now Rissland and Norbury reveal that additional, parallel decay pathways are at work in the fission yeast, Schizosaccharomyces pombe. They find that mRNA decapping is frequently independent of deadenylation and that Cid1-dependent uridylation of polyadenylated mRNAs seems to stimulate decapping as part of a novel mRNA turnover pathway. As human cells contain Cid1 orthologs, uridylation may form the basis of a widespread, conserved mechanism of mRNA decay.

    • Olivia S Rissland
    • Chris J Norbury
    Research
    Nature Structural & Molecular Biology
    Volume: 16, P: 616-623

  • The post-transcriptional addition of uridyl ribonucleotides by terminal uridyltransferases (TUTases) to the ′A ends of various cytoplasmic RNAs, including microRNAs, has been implicated in regulating their stability, biogenesis or activity. The crystal structure of Schizosaccharomyces pombe TUTase Cid1 in its apo form and bound to UTP provides insight into the enzyme's active site, UTP selectivity and RNA-binding mechanism.

    • Luke A Yates
    • Sophie Fleurdépine
    • Robert J C Gilbert
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 782-787

  • The addition or removal of poly(A) tails from the 3′ ends of eukaryotic RNAs is a key regulator of RNA stability and, consequently, of gene expression. Recent work has revealed that RNA turnover is also controlled by the addition of oligo(U) tails.

    • Chris J. Norbury
    Reviews
    Nature Reviews Molecular Cell Biology
    Volume: 14, P: 643-653

  • Here, the authors show that cytoplasmic uridylyltransferases TUT7 and TUT4 bind let-7 pre-miRNA by alternative means in the absence and presence of Lin28A, which directly interacts with both RNA and enzyme to convert from a distributive to a processive mode of action.

    • Gangshun Yi
    • Mingda Ye
    • Robert J. C. Gilbert
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 1426-1438