ArticleMolecular and cellular biology2007
A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.
Article in Molecular and cellular biology, 2007. 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, 72 citations in OpenAlex.
- Construction of mitochondrial-targeted ferritin carrier: subunit-terminal fused mitochondrial presequences facilitate efficient delivery.Journal of advanced research · 2026Article
- LETMD1 regulates mitochondrial protein synthesis and import to guard brown fat mitochondrial integrity and function.iScience · 2024Article
- Functional mapping of N-terminal residues in the yeast proteome uncovers novel determinants for mitochondrial protein import.PLoS genetics · 2023Article
- Parkinson's disease-associated VPS35 mutant reduces mitochondrial membrane potential and impairs PINK1/Parkin-mediated mitophagy.Translational neurodegeneration · 2021Article
- Transport of Proteins into Mitochondria.The protein journal · 2019Review
- Granzyme B enters the mitochondria in a Sam50-, Tim22- and mtHsp70-dependent manner to induce apoptosis.Cell death and differentiation · 2017Article
- Review
- High Pressure-Induced mtDNA Alterations in Retinal Ganglion Cells and Subsequent Apoptosis.Frontiers in cellular neuroscience · 2016Article
- The mitochondrial ADP/ATP carrier associates with the inner membrane presequence translocase in a stoichiometric manner.The Journal of biological chemistry · 2014Article
- Structural changes in the mitochondrial Tim23 channel are coupled to the proton-motive force.Nature structural & molecular biology · 2013Article
- Multistep protein unfolding during nanopore translocation.Nature nanotechnology · 2013Article
- Evidence of evolutionary constraints that influences the sequence composition and diversity of mitochondrial matrix targeting signals.PloS one · 2013Article
- Enhanced J-protein interaction and compromised protein stability of mtHsp70 variants lead to mitochondrial dysfunction in Parkinson's disease.Human molecular genetics · 2012Article
- Mitochondrial protein import and the genesis of steroidogenic mitochondria.Molecular and cellular endocrinology · 2011Review
- Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting.Molecular and cellular biology · 2010Article
- Oxidative mechanisms of brain dysfunction during sepsis.Neurochemical research · 2010Review
- Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.The international journal of biochemistry & cell biology · 2009Article
- Review
- 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
- Multiple pathways for sorting mitochondrial precursor proteins.EMBO reports · 2008Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The import of mitochondrial preproteins requires an electric potential across the inner membrane and the hydrolysis of ATP in the matrix. We assessed the contributions of the two energy sources to the translocation driving force responsible for movement of the polypeptide chain through the translocation channel and the unfolding of preprotein domains. The import-driving activity was directly analyzed by the determination of the protease resistances of saturating amounts of membrane-spanning translocation intermediates. The ability to generate a strong translocation-driving force was solely dependent on the activity of the ATP-dependent import motor complex in the matrix. For a sustained import-driving activity on the preprotein in transit, an unstructured N-terminal segment of more than 70 to 80 amino acid residues was required. The electric potential of the inner membrane was required to maintain the import-driving activity at a high level. The electrophoretic force of the potential exhibited only a limited capacity to unfold preprotein domains. We conclude that the membrane potential increases the probability of a dynamic interaction of the preprotein with the import motor. Polypeptide translocation and unfolding are mainly driven by the inward-directed translocation activity based on the functional cooperation of the import motor components.
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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.