ArticleThe EMBO journal1997
Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 68 citations in OpenAlex.
- A hybrid TIM complex mediates protein import into hydrogenosomes of Trichomonas vaginalis.BMC biology · 2024Article
- Tim17 Updates: A Comprehensive Review of an Ancient Mitochondrial Protein Translocator.Biomolecules · 2020Review
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.Science advances · 2017Article
- Disorders of phospholipid metabolism: an emerging class of mitochondrial disease due to defects in nuclear genes.Frontiers in genetics · 2015Review
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Mitochondrial membrane complex that contains proteins necessary for tRNA import in Trypanosoma brucei.The Journal of biological chemistry · 2012Article
- Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex.The Journal of cell biology · 2011Article
- Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting.Molecular and cellular biology · 2010Article
- Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.The international journal of biochemistry & cell biology · 2009Article
- The mitochondrial protein translocation motor: structural conservation between the human and yeast Tim14/Pam18-Tim16/Pam16 co-chaperones.International journal of molecular sciences · 2009Article
- Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits.Molecular biology of the cell · 2008Article
- Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex.The EMBO journal · 2003Article
- Biogenesis of Tim proteins of the mitochondrial carrier import pathway: differential targeting mechanisms and crossing over with the main import pathway.Molecular biology of the cell · 1999Article
- The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.The Journal of cell biology · 1999Article
- Article
- Strong precursor-pore interactions constrain models for mitochondrial protein import.Biophysical journal · 1998Article
- Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules.Molecular and cellular biology · 1998Article
- The Tim54p-Tim22p complex mediates insertion of proteins into the mitochondrial inner membrane.The Journal of cell biology · 1997Article
- The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44.The EMBO journal · 1997Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The protein transport machinery of the inner mitochondrial membrane contains three essential Tim proteins. Tim17 and Tim23 are thought to build a preprotein translocation channel, while Tim44 transiently interacts with the matrix heat shock protein Hsp70 to form an ATP-driven import motor. For this report we characterized the biogenesis and interactions of Tim proteins. (i) Import of the precursor of Tim44 into the inner membrane requires mtHsp70, whereas import and inner membrane integration of the precursors of Tim17 and Tim23 are independent of functional mtHsp70. (ii) Tim17 efficiently associates with Tim23 and mtHsp70, but only weakly with Tim44. (iii) Depletion of Tim44 does not affect the co-precipitation of Tim17 with antibodies directed against mtHsp70. (iv) Tim23 associates with both Tim44 and Tim17, suggesting the presence of two Tim23 pools in the inner membrane, a Tim44-Tim23-containing sub-complex and a Tim23-Tim17-containing sub-complex. (v) The association of mtHsp70 with the Tim23-Tim17 sub-complex is ATP sensitive and can be distinguished from the mtHsp70-Tim44 interaction by the differential influence of an amino acid substitution in mtHsp70. (vi) Genetic evidence, suppression of the protein import defect of a tim17 yeast mutant by overexpression of mtHsp70 and synthetic lethality of conditional mutants in the genes of Tim17 and mtHsp70, supports a functional interaction of mtHsp70 with Tim17. We conclude that the protein transport machinery of the mitochondrial inner membrane consists of dynamically interacting sub-complexes, each of which transiently binds mtHsp70.
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