ArticleBiology of the cell2021
Novel IM-associated protein Tim54 plays a role in the mitochondrial import of internal signal-containing proteins in Trypanosoma brucei.
Article in Biology of the cell, 2021. 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, 14 citations in OpenAlex.
- TbTim20 facilitates protein import at a low membrane potential in trypanosomes lacking the mitochondrial genome.The FEBS journal · 2026Article
- DRBD18 acts as a transcript-specific RNA editing auxiliary factor inRNA (New York, N.Y.) · 2025Article
- Pam16 and Pam18 were repurposed during Trypanosoma brucei evolution to regulate the replication of mitochondrial DNA.PLoS biology · 2024Article
- Article
- Unique Interactions of the Small Translocases of the Mitochondrial Inner Membrane (Tims) inInternational journal of molecular sciences · 2024Article
- Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase.International journal of molecular sciences · 2021Review
- The Diversity of the Mitochondrial Outer Membrane Protein Import Channels: Emerging Targets for Modulation.Molecules (Basel, Switzerland) · 2021Review
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
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Authors and funding
7 authors at 1 institution in 1 country.
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Abstract
backgroundThe translocase of the mitochondrial inner membrane (TIM) imports most of the nucleus-encoded proteins that are destined for the matrix, inner membrane (IM) and the intermembrane space (IMS). Trypanosoma brucei, the infectious agent for African trypanosomiasis, possesses a unique TIM complex consisting of several novel proteins in association with a relatively conserved protein TbTim17. Tandem affinity purification of the TbTim17 protein complex revealed TbTim54 as a potential component of this complex.
resultsTbTim54, a trypanosome-specific IMS protein, is peripherally associated with the IM and is present in a protein complex slightly larger than the TbTim17 complex. TbTim54 knockdown (KD) reduced the import of TbTim17 and compromised the integrity of the TbTim17 complex. TbTim54 KD inhibited the in vitro mitochondrial import and assembly of the internal signal-containing mitochondrial carrier proteins MCP3, MCP5 and MCP11 to a greater extent than TbTim17 KD. Furthermore, TbTim54 KD, but not TbTim17 KD, significantly hampered the mitochondrial targeting of ectopically expressed MCP3 and MCP11. These observations along with our previous finding that the mitochondrial import of N-terminal signal-containing proteins like cytochrome oxidase subunit 4 and MRP2 was affected to a greater extent by TbTim17 KD than TbTim54 KD indicating a substrate-specificity of TbTim54 for internal-signal containing mitochondrial proteins. In other organisms, small Tim chaperones in the IMS are known to participate in the translocation of MCPs. We found that TbTim54 can directly interact with at least two of the six known small TbTim proteins, TbTim11 and TbTim13, as well as with the N-terminal domain of TbTim17.
conclusionTbTim54 interacts with TbTim17. It also plays a crucial role in the mitochondrial import and complex assembly of internal signal-containing IM proteins in T. brucei. SIGNIFICANCE: We are the first to characterise TbTim54, a novel TbTim that is involved primarily in the mitochondrial import of MCPs and TbTim17 in T. brucei.
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