ArticleMolecular and cellular biology1997
Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 49 citations in OpenAlex.
- Privileged proteins with a second residence: dual targeting and conditional re-routing of mitochondrial proteins.The FEBS journal · 2024Review
- A two-step mitochondrial import pathway couples the disulfide relay with matrix complex I biogenesis.The Journal of cell biology · 2023Article
- The selectivity filter of the mitochondrial protein import machinery.BMC biology · 2020Article
- Proteolytic cleavage by the inner membrane peptidase (IMP) complex or Oct1 peptidase controls the localization of the yeast peroxiredoxin Prx1 to distinct mitochondrial compartments.The Journal of biological chemistry · 2017Article
- Revisiting trends on mitochondrial mega-channels for the import of proteins and nucleic acids.Journal of bioenergetics and biomembranes · 2017Review
- The ins and outs of algal metal transport.Biochimica et biophysica acta · 2012Review
- Pink1 kinase and its membrane potential (Deltaψ)-dependent cleavage product both localize to outer mitochondrial membrane by unique targeting mode.The Journal of biological chemistry · 2012Article
- Multiple lines of evidence localize signaling, morphology, and lipid biosynthesis machinery to the mitochondrial outer membrane of Arabidopsis.Plant physiology · 2011Article
- Bimodal targeting of cytochrome P450s to endoplasmic reticulum and mitochondria: the concept of chimeric signals.The FEBS journal · 2011Review
- Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL.The Journal of cell biology · 2010Article
- c-type cytochrome assembly in Saccharomyces cerevisiae: a key residue for apocytochrome c1/lyase interaction.Genetics · 2010Article
- A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space.Molecular and cellular biology · 2006Article
- Import of small Tim proteins into the mitochondrial intermembrane space.The EMBO journal · 2003Article
- Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins.The EMBO journal · 2003Article
- Proteomic approach to identify novel mitochondrial proteins in Arabidopsis.Plant physiology · 2001Article
- Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small tom proteins, and import receptors.Molecular and cellular biology · 2001Article
- Cloning and characterization of a maize cytochrome-b5 reductase with Fe3+-chelate reduction capability.The Biochemical journal · 1999Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mitochondrial NADH-cytochrome b5 reductase (Mcr1p) is encoded by a single nuclear gene and imported into two different submitochondrial compartments: the outer membrane and the intermembrane space. We now show that the amino-terminal 47 amino acids suffice to target the Mcr1 protein to both destinations. The first 12 residues of this sequence function as a weak matrix-targeting signal; the remaining residues are mostly hydrophobic and serve as an intramitochondrial sorting signal for the outer membrane and the intermembrane space. A double point mutation within the hydrophobic region of the targeting sequence virtually abolishes the ability of the precursor to be inserted into the outer membrane but increases the efficiency of transport into the intermembrane space. Import of Mcr1p into the intermembrane space requires an electrochemical potential across the inner membrane, as well as ATP in the matrix, and is strongly impaired in mitochondria lacking Tom7p or Tim11p, two components of the translocation machineries in the outer and inner mitochondrial membranes, respectively. These results indicate that intramitochondrial sorting of the Mcr1 protein is mediated by specific interactions between the bipartite targeting sequence and components of both mitochondrial translocation systems.
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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.