ArticleProtein science : a publication of the Protein Society1993
Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP.
Article in Protein science : a publication of the Protein Society, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 113 citations in OpenAlex.
- Proteomic Analysis of Primary Colon Cancer and Synchronous Solitary Liver Metastasis.Cancer genomics & proteomicsTrial
- OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization.The Journal of cell biology · 2024Article
- DELE1 tracks perturbed protein import and processing in human mitochondria.Nature communications · 2022Article
- Cytosolic Quality Control of Mitochondrial Protein Precursors-The Early Stages of the Organelle Biogenesis.International journal of molecular sciences · 2021Review
- Myristoyl group-aided protein import into the mitochondrial intermembrane space.Scientific reports · 2019Article
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- I - insulin transfer to mitochondria.Journal of bioenergetics and biomembranes · 2014Article
- 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
- Charge requirements for proton gradient-driven translocation of anthrax toxin.The Journal of biological chemistry · 2011Article
- Role of the import motor in insertion of transmembrane segments by the mitochondrial TIM23 complex.EMBO reports · 2011Article
- Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import.The Journal of cell biology · 2009Article
- Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import.Molecular biology of the cell · 2006Article
- On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60.Cell stress & chaperones · 2006Review
- The substrate binding domain of DnaK facilitates slow protein refolding.Proceedings of the National Academy of Sciences of the United States of America · 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
- Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- 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
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Cytochrome b2 is synthesized as a precursor in the cytoplasm and imported to the intermembrane space of yeast mitochondria. We show here that the precursor contains a tightly folded heme-binding domain and that translocation of this domain across the outer membrane requires ATP. Surprisingly, it is ATP in the mitochondrial matrix rather than external ATP that drives import of the heme-binding domain. When the folded structure of the heme-binding domain is disrupted by mutation or by urea denaturation, import and correct processing take place in ATP-depleted mitochondria. These results indicate that (1) cytochrome b2 reaches the intermembrane space without completely crossing the inner membrane, and (2) some precursors fold outside the mitochondria but remain translocation-competent, and import of these precursors in vitro does not require ATP-dependent cytosolic chaperone proteins.
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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.