Authors
S Dixit6; S Dixit7; S Dixit4; M Müller-McNicoll5; V David6; V David7; K Zarnack1; J Ule3; H Hashimi6; H Hashimi7; H Hashimi4; J Lukeš6; J Lukeš7; J Lukeš4; J Lukeš2;
1 Buchmann Institute for Molecular Life Sciences, Goethe University, Germany; 2 Canadian Institute for Advanced Research, Toronto, Canada, Canada; 3 Department of Molecular Neuroscience, UCL Institute of Neurology, London; 4 Faculty of Science, University of South Bohemia, Ceske Budejovice (Budweis), Czech Republic, Czech Republic; 5 Institute for Cell Biology and Neuroscience, Goethe University, Germany; 6 Institute of Parasitology, Biology Centre, ASCR, Czech Republic; 7 Institute of Parasitology, Biology Centre, ASCR, Czech Republic
Discussion
A dozen mRNAs are edited by multiple insertions and/or deletions of uridine residues in the mitochondrion of Trypanosoma brucei. Several protein complexes have been implicated to perform this type of RNA editing, including the mitochondrial RNA binding complex 1 (MRB1). Two protein components of MRB1 loosely associated with its core are MRB8170 and MRB4160, which represent novel RNA binding proteins. However, information related to both the protein’s role in RNA editing and its effect on target mRNAs is limited. Quantitative data obtained in this study revealed preferential binding of these proteins to mitochondrial mRNAs, positively correlating with their editing extent. Integrating in vivo and in vitro data, we propose a model in which differential binding of MRB8170 and/or MRB4160 onto pre-edited mRNA marks initiation of editing, which helps to recruit other components of MRB1, ensuring efficient editing.
