ArticleThe EMBO journal1996
The delta psi- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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Who cites it
31 citing papers in PubMed, 97 citations in OpenAlex.
- Towards a molecular mechanism underlying mitochondrial protein import through the TOM and TIM23 complexes.eLife · 2022Article
- Stendomycin selectively inhibits TIM23-dependent mitochondrial protein import.Nature chemical biology · 2017Article
- 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
- Role of Magmas in protein transport and human mitochondria biogenesis.Human molecular genetics · 2010Article
- Unfolding-resistant translocase targeting: a novel mechanism for outer mitochondrial membrane localization exemplified by the Bbeta2 regulatory subunit of protein phosphatase 2A.The Journal of biological chemistry · 2005Article
- Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space.Molecular and cellular biology · 2003Article
- The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation.The EMBO journal · 2002Article
- L and D presequence peptides derived from the precursor of F1beta subunit of the ATP synthase inhibit mitochondrial protein import by interaction with import machinery.Plant molecular biology · 2001Article
- Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae.Molecular and cellular biology · 2001Article
- 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
- Models of post-translational protein translocation.Biophysical journal · 2000Article
- MCC and PSC, the putative protein import channels of mitochondria.Journal of bioenergetics and biomembranes · 2000Review
- 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
- The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis.The EMBO journal · 1999Article
- Unfolding of preproteins upon import into mitochondria.The EMBO journal · 1998Article
- C- to N-terminal translocation of preproteins into mitochondria.The EMBO journal · 1998Article
- Article
- Strong precursor-pore interactions constrain models for mitochondrial protein import.Biophysical journal · 1998Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
New steps in the reaction cycle that drives protein translocation into the mitochondrial matrix have been defined. The membrane potential (delta psi)- and the mtHsp70/MIM44-dependent import machinery cooperate in the transfer of the presequence across the inner membrane. Translocation intermediates, arrested at a stage where only the presequence could form a complex with mtHsp70, still required delta psi for further import. Delta psi at this stage prevented retrograde movement, since mtHsp70 did not bind to the presequence with sufficient affinity. In contrast, mature regions of incoming chains adjacent to the presequence were bound by mtHsp70 tightly enough to stabilize them in the matrix. Cycling of the mtHsp70 on and off incoming chains is a continuous process in the presence of matrix ATP. Both MIM44-bound and free forms of mtHsp70 were found in association with the incoming chains. These data are consistent with a reaction pathway in which the mtHsp70/MIM44 complex acts as a molecular ratchet on the cis side of the inner membrane to drive protein translocation into the matrix.
Indexed as
Identifiers
8631295PMC450272W62747462What OpenQuestion holds
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.