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The structural landscape of native editosomes in African trypanosomes
Author(s) -
Ulrich Göringer H.,
Subbaraju Katari Venkata,
Böhm Cordula
Publication year - 2010
Publication title -
wiley interdisciplinary reviews: rna
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.225
H-Index - 71
eISSN - 1757-7012
pISSN - 1757-7004
DOI - 10.1002/wrna.67
Subject(s) - guide rna , rna , rna editing , messenger rna , translation (biology) , biology , computational biology , non coding rna , protein biosynthesis , microbiology and biotechnology , biochemistry , gene , crispr , cas9
The majority of mitochondrial pre‐messenger RNAs in African trypanosomes are substrates of a U‐nucleotide‐specific insertion/deletion‐type RNA editing reaction. The process converts nonfunctional pre‐mRNAs into translation‐competent molecules and can generate protein diversity by alternative editing. High molecular mass protein complexes termed editosomes catalyze the processing reaction. They stably interact with pre‐edited mRNAs and small noncoding RNAs, known as guide RNAs (gRNAs), which act as templates in the reaction. Editosomes provide a molecular surface for the individual steps of the catalytic reaction cycle and although the protein inventory of the complexes has been studied in detail, a structural analysis of the processing machinery has only recently been accomplished. Electron microscopy in combination with single particle reconstruction techniques has shown that steady state isolates of editosomes contain ensembles of two classes of stable complexes with calculated apparent hydrodynamic sizes of 20S and 35–40S. 20S editosomes are free of substrate RNAs, whereas 35–40S editosomes are associated with endogenous mRNA and gRNA molecules. Both complexes are characterized by a diverse structural landscape, which include complexes that lack or possess defined subdomains. Here, we summarize the consensus models and structural landmarks of both complexes. We correlate structural features with functional characteristics and provide an outlook into dynamic aspects of the editing reaction cycle. WIREs RNA 2011 2 395–407 DOI: 10.1002/wrna.67 This article is categorized under: RNA Interactions with Proteins and Other Molecules > RNA–Protein Complexes RNA Processing > RNA Editing and Modification

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