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Mol. Cell. Biol., Apr 1996, 1410-1418, Vol 16, No. 4
RA Corell, LK Read, GR Riley, JK Nellissery, TE Allen, ML Kable, MD Wachal, SD Seiwert, PJ Myler and KD Stuart
Transcripts from many mitochondrial genes in kinetoplastids undergo RNA
editing, a posttranscriptional process which inserts and deletes uridines.
By assaying for deletion editing in vitro, we found that the editing
activity from Trypanosoma brucei mitochondrial lysates (S.D. Seiwert and
K.D. Stuart), Science 266:114-117,1994) sediments with a peak of
approximately 20S. RNA helicase, terminal uridylyl transferase, RNA ligase,
and adenylation activities, which may have a role in editing, cosediment in
a broad distribution, with most of each activity at 35 to 40S. Most ATPase
6 (A6) guide RNA and unedited A6 mRNA sediments at 20 to 30S, with some
sedimenting further into the gradient, while most edited A6 mRNA sediments
at >35S. Several mitochondrial proteins which cross-link specifically
with guide RNA upon UV treatment also sediment in glycerol gradients.
Notably, a 65- kDa protein sediments primarily at approximately 20S, a
90-kDa protein sediments at 35 to 40S, and a 25-kDa protein is present at
<10S. Most ribonucleoprotein complexes that form with gRNA in vitro
sediment at 10 to 20S, except for one, which sediments at 30 to 45S. These
results suggest that RNA editing takes place within a multicomponent
complex. The potential functions of and relationships between the 20S and
35 to 40S complexes are discussed.
Copyright © 1996, American Society for Microbiology
Complexes from Trypanosoma brucei that exhibit deletion editing and other editing-associated properties
Seattle Biomedical Research Institute, Washington 98109-1651, USA.
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