ArticleThe Journal of cell biology1997
The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
66 citing papers in PubMed, 212 citations in OpenAlex.
- Unique Interactions of the Small Translocases of the Mitochondrial Inner Membrane (Tims) inInternational journal of molecular sciences · 2024Article
- Adenine nucleotide carrier protein dysfunction in human disease.IUBMB life · 2023Review
- Article
- Mitochondrial protein translocation machinery: From TOM structural biogenesis to functional regulation.The Journal of biological chemistry · 2022Review
- Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase.International journal of molecular sciences · 2021Review
- Novel IM-associated protein Tim54 plays a role in the mitochondrial import of internal signal-containing proteins in Trypanosoma brucei.Biology of the cell · 2021Article
- Role of the Mitochondrial Protein Import Machinery and Protein Processing in Heart Disease.Frontiers in cardiovascular medicine · 2021Review
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- Independent accretion of TIM22 complex subunits in the animal and fungal lineages.F1000Research · 2020Article
- Mitochondrial proteins: from biogenesis to functional networks.Nature reviews. Molecular cell biology · 2019Review
- Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.Cell · 2018Article
- The divergent N-terminal domain of Tim17 is critical for its assembly in the TIM complex in Trypanosoma brucei.Molecular and biochemical parasitology · 2017Article
- Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space.Cell and tissue research · 2017Review
- TIM29 is a subunit of the human carrier translocase required for protein transport.FEBS letters · 2016Article
- Phosphatidylcholine Affects Inner Membrane Protein Translocases of Mitochondria.The Journal of biological chemistry · 2016Article
- Tim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability.eLife · 2016Article
- How lipids modulate mitochondrial protein import.Journal of bioenergetics and biomembranes · 2016Review
- Tim62, a Novel Mitochondrial Protein in Trypanosoma brucei, Is Essential for Assembly and Stability of the TbTim17 Protein Complex.The Journal of biological chemistry · 2015Article
- Functional complementation analyses reveal that the single PRAT family protein of trypanosoma brucei is a divergent homolog of Tim17 in saccharomyces cerevisiae.Eukaryotic cell · 2015Article
- Trypanosome alternative oxidase possesses both an N-terminal and internal mitochondrial targeting signal.Eukaryotic cell · 2014Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
We have identified a new protein, Tim54p, located in the yeast mitochondrial inner membrane. Tim54p is an essential import component, required for the insertion of at least two polytopic proteins into the inner membrane, but not for the translocation of precursors into the matrix. Several observations suggest that Tim54p and Tim22p are part of a protein complex in the inner membrane distinct from the previously characterized Tim23p-Tim17p complex. First, multiple copies of the TIM22 gene, but not TIM23 or TIM17, suppress the growth defect of a tim54-1 temperature-sensitive mutant. Second, Tim22p can be coprecipitated with Tim54p from detergent-solubilized mitochondria, but Tim54p and Tim22p do not interact with either Tim23p or Tim17p. Finally, the tim54-1 mutation destabilizes the Tim22 protein, but not Tim23p or Tim17p. Our results support the idea that the mitochondrial inner membrane carries two independent import complexes: one required for the translocation of proteins across the inner membrane (Tim23p-Tim17p), and the other required for the insertion of proteins into the inner membrane (Tim54p-Tim22p).
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Registered trials
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.