ArticleThe EMBO journal2001
The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- A Function-Centric Framework for Mitochondrial Quality Control.Biomolecules · 2026Review
- Article
- Single-molecule evidence of Entropic Pulling by Hsp70 chaperones.Nature communications · 2024Article
- Multiple variants of the human presequence translocase motor subunit Magmas govern the mitochondrial import.The Journal of biological chemistry · 2021Article
- Constraint-based modeling of yeast mitochondria reveals the dynamics of protein import and iron-sulfur cluster biogenesis.iScience · 2021Article
- Accessing Mitochondrial Protein Import in Living Cells by Protein Microinjection.Frontiers in cell and developmental biology · 2021Article
- Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts.Plant physiology · 2018Article
- Mutations in the heat-shock protein A9 (HSPA9) gene cause the EVEN-PLUS syndrome of congenital malformations and skeletal dysplasia.Scientific reports · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Quantifying the role of chaperones in protein translocation by computational modeling.Frontiers in molecular biosciences · 2015Article
- Inducible HSP70 regulates superoxide dismutase-2 and mitochondrial oxidative stress in the endothelial cells from developing lungs.American journal of physiology. Lung cellular and molecular physiology · 2014Article
- Upregulation of phosphorylated HSP27, PRDX2, GRP75, GRP78 and GRP94 in acquired middle ear cholesteatoma growth.International journal of molecular sciences · 2013Article
- Evidence of evolutionary constraints that influences the sequence composition and diversity of mitochondrial matrix targeting signals.PloS one · 2013Article
- A model system for mitochondrial biogenesis reveals evolutionary rewiring of protein import and membrane assembly pathways.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Mortalin, apoptosis, and neurodegeneration.Biomolecules · 2012Article
- Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix.The international journal of biochemistry & cell biology · 2009Article
- Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.The Journal of biological chemistry · 2009Article
- A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.Molecular and cellular biology · 2007Article
- Prediction of the translocation kinetics of a protein from its mechanical properties.Biophysical journal · 2006Article
- Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unfolding is an essential process during translocation of preproteins into mitochondria; however, controversy exists as to whether mitochondria play an active role in unfolding. We have established an in vitro system with a kinetic saturation of the mitochondrial import machinery, yielding translocation rates comparable to in vivo import rates. Preproteins with short N-terminal segments in front of a folded domain show a characteristic delay of the onset of translocation (lag phase) although the maximal import rate is similar to that of longer preproteins. The lag phase is shortened by extending the N-terminal segment to improve the accessibility to matrix heat shock protein 70 and abolished by unfolding of the preprotein. A mutant mtHsp70 defective in binding to the inner membrane prolongs the lag phase and reduces the translocation activity. A direct comparison of the rate of spontaneous unfolding in solution with that during translocation demonstrates that unfolding by mitochondria is significantly faster, proving an active unfolding process. We conclude that access of mtHsp70 to N-terminal preprotein segments is critical for active unfolding and initiation of translocation.
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