ArticleProceedings of the National Academy of Sciences of the United States of America2006
A bifunctional tRNA import receptor from Leishmania mitochondria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 52 citations in OpenAlex.
- Engineered mitochondria in diseases: mechanisms, strategies, and applications.Signal transduction and targeted therapy · 2025Review
- Mitochondrion-to-nucleus communication mediated by RNA export: a survey of potential mechanisms and players across eukaryotes.Biology letters · 2024Review
- Mitochondrion-targeted RNA therapies as a potential treatment strategy for mitochondrial diseases.Molecular therapy. Nucleic acids · 2022Review
- Mitochondrial Genome Editing to Treat Human Osteoarthritis-A Narrative Review.International journal of molecular sciences · 2022Review
- Mitochondrial Genome Engineering: The Revolution May Not Be CRISPR-Ized.Trends in genetics : TIG · 2018Review
- tRNAs and proteins use the same import channel for translocation across the mitochondrial outer membrane of trypanosomes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mitochondrial membrane complex that contains proteins necessary for tRNA import in Trypanosoma brucei.The Journal of biological chemistry · 2012Article
- In vivo study in Trypanosoma brucei links mitochondrial transfer RNA import to mitochondrial protein import.EMBO reports · 2011Article
- Ecto-F₁-ATPase: a moonlighting protein complex and an unexpected apoA-I receptor.World journal of gastroenterology · 2010Review
- Evolution of macromolecular import pathways in mitochondria, hydrogenosomes and mitosomes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2010Review
- A mosaic of RNA binding and protein interaction motifs in a bifunctional mitochondrial tRNA import factor from Leishmania tropica.Nucleic acids research · 2008Article
- Proton-guided movements of tRNA within the Leishmania mitochondrial RNA import complex.Nucleic acids research · 2008Article
- RNA editing in Trypanosoma brucei requires three different editosomes.Molecular and cellular biology · 2008Article
- Elongation factor 1a mediates the specificity of mitochondrial tRNA import in T. brucei.The EMBO journal · 2007Article
- The ins and outs of tRNA transport.EMBO reports · 2007Article
- Necessary and sufficient factors for the import of transfer RNA into the kinetoplast mitochondrion.EMBO reports · 2007Article
- The voltage-dependent anion channel, a major component of the tRNA import machinery in plant mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Transfer RNA travels from the cytoplasm to organelles.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
- Expression of concern
- Retracted
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In kinetoplastid protozoa, import of cytosolic tRNAs into mitochondria occurs through tRNAs interacting with membrane-bound proteins, the identities of which are unknown. The inner membrane RNA import complex of Leishmania tropica contains multiple proteins and is active for import in vitro. RIC1, the largest subunit of this complex, is structurally homologous to the conserved alpha subunit of F1 ATP synthase. The RIC1 gene complemented an atpA mutation in Escherichia coli. Antisense-mediated knockdown of RIC1/F1alpha in Leishmania resulted in depletion of several mitochondrial tRNAs belonging to distinct subsets (types I and II) that interact cooperatively or antagonistically within the import complex. The knockdown-induced defect in import of type I tRNAs was rectified in a reconstituted system by purified RIC1/F1alpha alone, but recovery of type II tRNA import additionally required a type I tRNA. RIC1/F1alpha formed stable complexes with type I, but not type II, tRNAs through the cooperation of its nucleotide binding and C-terminal domains. Thus, RIC1/F1alpha is a type I tRNA import receptor. As expected of a bifunctional protein, RIC1/F1alpha is shared by both the import complex and by respiratory complex V. Alternative use of ancient respiratory proteins may have been an important step in the evolution of tRNA import.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.