ABCE1 is a highly conserved RNA silencing suppressor
Journal article, 2015
ATP-binding cassette sub-family E member 1 (ABCE1) is a highly conserved protein among eukaryotes and archaea. Recent studies have identified ABCE1 as a ribosomerecycling factor important for translation termination in mammalian cells, yeast and also archaea. Here we report another conserved function of ABCE1. We have previously described AtRLI2, the homolog of ABCE1 in the plant Arabidopsis thaliana, as an endogenous suppressor of RNA silencing. In this study we show that this function is conserved: human ABCE1 is able to suppress RNA silencing in Nicotiana benthamiana plants, in mammalian HEK293 cells and in the worm Caenorhabditis elegans. Using co-immunoprecipitation and mass spectrometry, we found a number of potential ABCE1-interacting proteins that might support its function as an endogenous suppressor of RNA interference. The interactor candidates are associated with epigenetic regulation, transcription, RNA processing and mRNA surveillance. In addition, one of the identified proteins is translin, which together with its binding partner TRAX supports RNA interference.
Author
Kairi Kärblane
Competence Centre for Cancer Research
Tallinn University of Technology (TalTech)
Jelena Gerassimenko
Tallinn University of Technology (TalTech)
Competence Centre for Cancer Research
Lenne Nigul
Tallinn University of Technology (TalTech)
Alla Piirsoo
Tallinn University of Technology (TalTech)
Agata Smialowska
Chalmers, Biology and Biological Engineering, Systems and Synthetic Biology
Södertörn University
Karolinska Institutet
Kadri Vinkel
Tallinn University of Technology (TalTech)
Per Kylsten
Södertörn University
Europaskolan
Karl Ekwall
Södertörn University
Karolinska Institutet
Peter Swoboda
Karolinska Institutet
Erkki Truve
Competence Centre for Cancer Research
Tallinn University of Technology (TalTech)
Cecilia Sarmiento
Tallinn University of Technology (TalTech)
Competence Centre for Cancer Research
PLoS ONE
1932-6203 (ISSN) 19326203 (eISSN)
Vol. 10 2 e0116702Subject Categories
Chemical Sciences
DOI
10.1371/journal.pone.0116702
PubMed
25659154