ArticleBiophysical journal1998
Strong precursor-pore interactions constrain models for mitochondrial protein import.
Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- BiP clustering facilitates protein folding in the endoplasmic reticulum.PLoS computational biology · 2014Article
- Simulating the pulling of stalled elongated peptide from the ribosome by the translocon.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.IET systems biology · 2012Article
- Interactions of mitochondrial presequence peptides with the mitochondrial outer membrane preprotein translocase TOM.Biophysical journal · 2010Article
- Bacterial Sec protein transport is rate-limited by precursor length: a single turnover study.Molecular biology of the cell · 2009Article
- Review
- Mitochondrial protein import motor: differential role of Tim44 in the recruitment of Pam17 and J-complex to the presequence translocase.Molecular biology of the cell · 2008Article
- DNA transport into Bacillus subtilis requires proton motive force to generate large molecular forces.Nature structural & molecular biology · 2004Article
- The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation.The EMBO journal · 2002Article
- The brownian ratchet and power stroke models for posttranslational protein translocation into the endoplasmic reticulum.Biophysical journal · 2002Article
- Protein unfolding by mitochondria. The Hsp70 import motor.EMBO reports · 2000Review
- Models of post-translational protein translocation.Biophysical journal · 2000Article
- Unfolding of preproteins upon import into mitochondria.The EMBO journal · 1998Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial precursor proteins are imported from the cytosol into the matrix compartment through a proteinaceous translocation pore. Import is driven by mitochondrial Hsp70 (mHsp70), a matrix-localized ATPase. There are currently two postulated mechanisms for this function of mHsp70: 1) The "Brownian ratchet" model proposes that the precursor chain diffuses within the pore, and that binding of mHsp70 to the lumenal portion of the chain biases this diffusion. 2) The "power stroke" model proposes that mHsp70 undergoes a conformational change that actively pulls the precursor chain through the pore. Here we formulate these two models quantitatively, and compare their performance in light of recent experimental evidence that precursor chains interact strongly with the walls of the translocation pore. Under these conditions the simulated Brownian ratchet is inefficient, whereas the power stroke mechanism seems to be a plausible description of the import process.
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