2012
DOI: 10.1093/nar/gks211
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Architecture of the trypanosome RNA editing accessory complex, MRB1

Abstract: Trypanosoma brucei undergoes an essential process of mitochondrial uridine insertion and deletion RNA editing catalyzed by a 20S editosome. The multiprotein mitochondrial RNA-binding complex 1 (MRB1) is emerging as an equally essential component of the trypanosome RNA editing machinery, with additional functions in gRNA and mRNA stabilization. The distinct and overlapping protein compositions of reported MRB1 complexes and diverse MRB1 functions suggest that the complex is composed of subcomplexes with RNA-dep… Show more

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Cited by 72 publications
(180 citation statements)
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“…Several pentatricopeptide proteins, which are so named because they contain the eponymous RNA-binding motif, have been shown to be membrane associated along with mt ribosomal RNA (Pusnik et al 2007). Among these is the kinetoplast polyadenylation/ uridylation factor 1 (kPAF1), also known as PPR1, which interacts with both MRB1 and mt ribosomes (Aphasizheva et al 2011;Ammerman et al 2012).…”
Section: Discussionmentioning
confidence: 99%
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“…Several pentatricopeptide proteins, which are so named because they contain the eponymous RNA-binding motif, have been shown to be membrane associated along with mt ribosomal RNA (Pusnik et al 2007). Among these is the kinetoplast polyadenylation/ uridylation factor 1 (kPAF1), also known as PPR1, which interacts with both MRB1 and mt ribosomes (Aphasizheva et al 2011;Ammerman et al 2012).…”
Section: Discussionmentioning
confidence: 99%
“…MRB8620 has been shown to interact with the MRB1 core complex and the TbRGG2 subcomplex by yeast two-hybrid analysis and various tandem affinity purification (TAPs) of tagged MRB1 subunits Weng et al 2008;Hernandez et al 2010;Ammerman et al 2011Ammerman et al , 2012Kafková et al 2012). To confirm that MRB8620 is an integral component of the MRB1 complex, we analyzed proteins copurifying with the C-terminally PTP-tagged MRB8620 without nuclease treatment by LC-MS/MS mass spectroscopy.…”
Section: Mrb8620 Interacts With Other Mrb1 Subunitsmentioning
confidence: 99%
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“…This could be achieved through the components of the SSU* complexes shared with the KPAP polyadenylation complex and/or other parts of the mRNA processing machinery. Several such components have been identified by the proteomics analyses in L. tarentolae and T. brucei, including the PPR29 protein investigated herein and several other PPR (Tb927.11.5500) and non-PPR proteins (Tb927.11.1250, Tb927.11.2530) (17,28,43,46,54). It is noteworthy that this effect is mRNA-specific, as follows from the observation that the LT of the RPS12 mRNA remains unchanged.…”
Section: Discussionmentioning
confidence: 57%