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
Jelena Gerassimenko
Competence Centre for Cancer Research
Tallinn University of Technology
Lenne Nigul
Tallinn University of Technology
Alla Piirsoo
Tallinn University of Technology
Agata Smialowska
Chalmers University of Technology
Karolinska Institutet
School of Life Sciences, Sodertorn University College
Kadri Vinkel
Tallinn University of Technology
Per Kylsten
Europaskolan
School of Life Sciences, Sodertorn University College
Karl Ekwall
School of Life Sciences, Sodertorn University College
Karolinska Institutet
Peter Swoboda
Karolinska Institutet
Erkki Truve
Competence Centre for Cancer Research
Tallinn University of Technology
Cecilia Sarmiento
Tallinn University of Technology
Competence Centre for Cancer Research
PLoS ONE
1932-6203 (ISSN)
Vol. 10 2Subject Categories (SSIF 2011)
Chemical Sciences
DOI
10.1371/journal.pone.0116702
PubMed
25659154