ArticleMolecular and cellular biology2000
Mutations in a tRNA import signal define distinct receptors at the two membranes of Leishmania mitochondria.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Exosome-Mediated Mitochondrial Delivery of Antisense Oligonucleotides.Nucleic acid therapeutics · 2025Article
- Proton-guided movements of tRNA within the Leishmania mitochondrial RNA import complex.Nucleic acids research · 2008Article
- Necessary and sufficient factors for the import of transfer RNA into the kinetoplast mitochondrion.EMBO reports · 2007Article
- A bifunctional tRNA import receptor from Leishmania mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- A sequence motif within trypanosome precursor tRNAs influences abundance and mitochondrial localization.Molecular and cellular biology · 2003Article
- Allosteric regulation of tRNA import: interactions between tRNA domains at the inner membrane of Leishmania mitochondria.Nucleic acids research · 2003Article
- "Ping-pong" interactions between mitochondrial tRNA import receptors within a multiprotein complex.Molecular and cellular biology · 2003Article
- Mitochondrial RNA import in Leishmania tropica: aptamers homologous to multiple tRNA domains that interact cooperatively or antagonistically at the inner membrane.Molecular and cellular biology · 2002Article
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Authors and funding
3 authors.
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Abstract
Nucleus-encoded tRNAs are selectively imported into the mitochondrion of Leishmania, a kinetoplastid protozoan. An oligoribonucleotide constituting the D stem-loop import signal of tRNA(Tyr)(GUA) was efficiently transported into the mitochondrial matrix in organello as well as in vivo. Transfer through the inner membrane could be uncoupled from that through the outer membrane and was resistant to antibody against the outer membrane receptor TAB. A number of mutations in the import signal had differential effects on outer and inner membrane transfer. Some mutants which efficiently traversed the outer membrane were unable to enter the matrix. Conversely, restoration of the loop-closing GC pair in reverse resulted in reversion of transfer through the inner, but not the outer, membrane, and binding of the RNA to the inner membrane was restored. These experiments indicate the presence at the two membranes of receptors with distinct specificities which mediate stepwise transfer into the mitochondrial matrix. The combination of oligonucleotide mutagenesis and biochemical fractionation may provide a general tool for the identification of tRNA transport factors.
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