tRNA-Derived RNA Fragments Associate with Human Multisynthetase Complex (MSC) and Modulate Ribosomal Protein Translation

Simon P. Keam, Andrew Sobala, Sara ten Have, Gyorgy Hutvagner (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    71 Citations (Scopus)

    Abstract

    The functionality of small RNAs from abundant species of "housekeeping" noncoding RNAs (e.g., rRNA, tRNA, snRNA, snoRNA, etc.) remains a highly studied topic. The current state of research on short RNAs derived from transfer RNA (tRNA), called tRNA-derived fragments (tRFs), has been restricted largely to expression studies and limited functional studies. 5' tRFs are known translational inhibitors in mammalian cells, yet little is known about their functionality. Here we report on the first experimental evidence of the tRF protein interactome, identifying the mammalian multisynthetase complex as the primary interactor of the 5' tRF Gln19. We also present proteome-wide SILAC evidence that 5' tRFs increase ribosomal and poly(A)-binding protein translation.

    Original languageEnglish
    Pages (from-to)413-420
    Number of pages8
    JournalJournal of Proteome Research
    Volume16
    Issue number2
    Early online date22 Nov 2016
    DOIs
    Publication statusPublished - 22 Nov 2016

    Keywords

    • tRF
    • multisynthetase complex
    • tRNA-derived fragment
    • small RNA
    • SILAC
    • immunoprecipitation
    • protein translation
    • mass spectrometry

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