Journal
NUCLEIC ACIDS RESEARCH
Volume 40, Issue 4, Pages 1828-1840Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkr867
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Funding
- National Institute of Health [RO1 AI34501]
- Vrije Universiteit Brussel (VUB) [GOA65]
- Vlaams Instituut Biotechnologie (VIB)
- Fund for Scientific Research of Flanders [FWOAL551]
- Hercules Foundation [HERC2]
- Institute for the encouragement of Scientific Research and Innovation of Brussels
- Belgian Government under Interuniversity Attraction Poles (I.A.P.) [P6/19]
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The parasite Trypanosoma brucei, the causative agent of sleeping sickness across sub-Saharan Africa, depends on a remarkable U-insertion/deletion RNA editing process in its mitochondrion. A approximately 20 S multi-protein complex, called the editosome, is an essential machinery for editing pre-mRNA molecules encoding the majority of mitochondrial proteins. Editosomes contain a common core of twelve proteins where six OB-fold interaction proteins, called A1-A6, play a crucial role. Here, we report the structure of two single-strand nucleic acid-binding OB-folds from interaction proteins A3 and A6 that surprisingly, form a heterodimer. Crystal growth required the assistance of an anti-A3 nanobody as a crystallization chaperone. Unexpectedly, this anti-A3 nanobody binds to both A3(OB) and A6, despite only similar to 40% amino acid sequence identity between the OB-folds of A3 and A6. The A3(OB)-A6 heterodimer buries 35% more surface area than the A6 homodimer. This is attributed mainly to the presence of a conserved Pro-rich loop in A3(OB). The implications of the A3(OB)-A6 heterodimer, and of a dimer of heterodimers observed in the crystals, for the architecture of the editosome are profound, resulting in a proposal of a 'five OB-fold center' in the core of the editosome.
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