Literature DB >> 27936807

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

Simon P Keam1, Andrew Sobala2, Sara Ten Have2, Gyorgy Hutvagner1.   

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.

Entities:  

Keywords:  SILAC; immunoprecipitation; mass spectrometry; multisynthetase complex; protein translation; small RNA; tRF; tRNA-derived fragment

Mesh:

Substances:

Year:  2016        PMID: 27936807     DOI: 10.1021/acs.jproteome.6b00267

Source DB:  PubMed          Journal:  J Proteome Res        ISSN: 1535-3893            Impact factor:   4.466


  29 in total

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9.  MINTbase v2.0: a comprehensive database for tRNA-derived fragments that includes nuclear and mitochondrial fragments from all The Cancer Genome Atlas projects.

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10.  Global identification and characterization of tRNA-derived RNA fragment landscapes across human cancers.

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