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 journalArticle

21 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

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Keywords

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

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