Nucleic Acids Research, Vol 26, Issue 5 1205-1213, Copyright © 1998 by Oxford University Press
D Blom, A de Haan, M van den Berg, P Sloof, M Jirku, J Lukes and R Benne
In parasitic kinetoplastid protozoa, mitochondrial (mt) mRNAs are post-
transcriptionally edited by insertion and deletion of uridylate residues,
the information being provided by guide (g) RNAs. In order to further
explore the role and evolutionary history of this process, we searched for
editing in mt RNAs of the free-living bodonid Bodo saltans. We found
extensive editing in the transcript for NADH dehydrogenase (ND) subunit 5,
which is unedited in trypanosomatids. In contrast, B.saltans cytochrome c
oxidase (cox) subunit 2 and maxicircle unidentified reading frame (MURF) 2
RNAs display limited editing in the same regions as their trypanosomatid
counterparts. A putative intramolecular cox2 gRNA and the gene for gMURF2-I
directing the insertion of only one U in the 5' editing domain of MURF2
RNA, are conserved in B.saltans. This lends (further) evolutionary support
to the proposed role of these sequences as gRNAs. Phylogenetic analysis
showed that B.saltans is more closely related to trypanosomatids than the
cryptobiids Trypanoplasma borreli and Cryptobia helicis, in line with the
trypanosomatid-like cox2 and MURF2 RNA editing patterns. Nevertheless,
other features like the apparent absence of a catenated mtDNA network, are
shared with bodonid and cryptobiid species. ND5 RNA editing may represent
yet another example of editing 'on the way out' during kinetoplastid
evolution, but in view of the fact that cox2 RNA is unedited in T. borreli
and C.helicis, we infer that the editing of this RNA may have arisen
relatively recently. Our results provide the first examples of RNA editing
in a free-living kinetoplastid, indicating that there is no direct link
between U-insertion/deletion editing and a parasitic lifestyle.
ARTICLES
RNA editing in the free-living bodonid Bodo saltans [published erratum appears in Nucleic Acids Res 1998 Dec 1;26(23):5539]
Department of Biochemistry/AMC, University of Amsterdam, Academic Medical Centre, Meibergdreef 15, 1105 AZ, Amsterdam, The Netherlands.
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