ArticleThe EMBO journal1998
Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins.
Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 59 citations in OpenAlex.
- A subpopulation of arenavirus nucleoprotein localizes to mitochondria.Scientific reports · 2021Article
- Adaptation of a Genetic Screen Reveals an Inhibitor for Mitochondrial Protein Import Component Tim44.The Journal of biological chemistry · 2017Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Cellular and molecular life sciences : CMLS · 2014Review
- Pink1 kinase and its membrane potential (Deltaψ)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode.The Journal of biological chemistry · 2012Article
- Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.Molecular and cellular biology · 2008Article
- A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.Molecular and cellular biology · 2007Article
- Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60.Cell stress & chaperones · 2006Review
- Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex.Molecular and cellular biology · 2002Article
- Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins.Molecular and cellular biology · 2001Article
- The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.The EMBO journal · 2001Article
- Protein unfolding by mitochondria. The Hsp70 import motor.EMBO reports · 2000Review
- Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence.Molecular biology of the cell · 2000Article
- 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
- Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex.The EMBO journal · 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The essential gene TIM44 encodes a subunit of the inner mitochondrial membrane preprotein translocase that forms a complex with the matrix heat-shock protein Hsp70. The specific role of Tim44 in protein import has not yet been defined because of the lack of means to block its function. Here we report on a Saccharomyces cerevisiae mutant allele of TIM44 that allows selective and efficient inactivation of Tim44 in organello. Surprisingly, the mutant mitochondria are still able to import preproteins. The import rate is only reduced by approximately 30% compared with wild-type as long as the preproteins do not carry stably folded domains. Moreover, the number of import sites is not reduced. However, the mutant mitochondria are strongly impaired in pulling folded domains of preproteins close to the outer membrane and in promoting their unfolding. Our results demonstrate that Tim44 is not an essential structural component of the import channel, but is crucial for import of folded domains. We suggest that the concerted action of Tim44 and mtHsp70 drives unfolding of preproteins and accelerates translocation of loosely folded preproteins. While mtHsp70 is essential for import of both tightly and loosly folded preproteins, Tim44 plays a more specialized role in translocation of tightly folded domains.
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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.