ArticleProceedings of the National Academy of Sciences of the United States of America1999
Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Molecular machineries and pathways of mitochondrial protein transport.Nature reviews. Molecular cell biology · 2025Review
- Protein import in mitochondria biogenesis: guided by targeting signals and sustained by dedicated chaperones.RSC advances · 2021Review
- The mitochondrial intermembrane space: the most constricted mitochondrial sub-compartment with the largest variety of protein import pathways.Open biology · 2021Review
- Role of the membrane potential in mitochondrial protein unfolding and import.Scientific reports · 2019Article
- Recent Advances in Mitochondria-Targeted Gene Delivery.Molecules (Basel, Switzerland) · 2018Review
- Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts.Plant physiology · 2018Article
- Article
- 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
- The Tom40 assembly process probed using the attachment of different intramitochondrial sorting signals.Molecular biology of the cell · 2012Article
- Gene delivery to mitochondria by targeting modified adenoassociated virus suppresses Leber's hereditary optic neuropathy in a mouse model.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Mutant NADH dehydrogenase subunit 4 gene delivery to mitochondria by targeting sequence-modified adeno-associated virus induces visual loss and optic atrophy in mice.Molecular vision · 2012Article
- Dual function MITO-Porter, a nano carrier integrating both efficient cytoplasmic delivery and mitochondrial macromolecule delivery.Molecular therapy : the journal of the American Society of Gene Therapy · 2011Article
- Mdm35p imports Ups proteins into the mitochondrial intermembrane space by functional complex formation.The EMBO journal · 2010Article
- Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria.The Journal of cell biology · 2009Article
- Tim23-Tim50 pair coordinates functions of translocators and motor proteins in mitochondrial protein import.The Journal of cell biology · 2009Article
- Trypanosoma brucei: differential requirement of membrane potential for import of proteins into mitochondria in two developmental stages.Experimental parasitology · 2008Article
- Comparison of the protein-unfolding pathways between mitochondrial protein import and atomic-force microscopy measurements.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space.Molecular and cellular biology · 2003Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The import of cytochrome b(2) into mitochondria consists of two steps. The translocation of the first part of the presequence across the inner membrane is coupled with the translocation of the tightly folded heme-binding domain across the outer membrane and requires a membrane potential DeltaPsi and the functions of mitochondrial Hsp70 (mHsp70) in the matrix. Once the heme-binding domain has passed the outer membrane, the translocation of the rest of the polypeptide chain across the outer membrane becomes independent of DeltaPsi and mHsp70. Here we analyzed the late DeltaPsi- and mHsp70-independent step in the transport of cytochrome b(2) fusion proteins into the intermembrane space (IMS). The import of the cytochrome b(2) fusion proteins containing two protein domains linked by a spacer segment into mitochondria was arrested at a stage at which one domain folded on each side of the outer membrane, along the pathway that is consistent with the stop-transfer model. The mature-size form of the translocation intermediate could move across the outer membrane in both directions, and the stabilization of the protein domain in the IMS promoted the forward translocation. On the other hand, the intermediate-size form of the translocation intermediate, which retains the anchorage to the inner membrane, was transported into the IMS independently of the stability of the protein domain in the IMS. These results suggest that two distinct mechanisms, the Brownian ratchet and the anchor diffusion mechanisms, can operate for the transmembrane movement of the mature-size form and the intermediate-size form, respectively, of cytochrome b(2) species.
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