ArticleThe EMBO journal1993
The signal that sorts yeast cytochrome b2 to the mitochondrial intermembrane space contains three distinct functional regions.
Article in The EMBO journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 84 citations in OpenAlex.
- Completion of mitochondrial division requires the intermembrane space protein Mdi1/Atg44.The Journal of cell biology · 2023Article
- An intermembrane space protein facilitates completion of mitochondrial division in yeast.bioRxiv : the preprint server for biology · 2023Article
- Dissecting the molecular mechanisms of mitochondrial import and maturation of peroxiredoxins from yeast and mammalian cells.Biophysical reviews · 2021Review
- Adaptation of a Genetic Screen Reveals an Inhibitor for Mitochondrial Protein Import Component Tim44.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
- Dissecting stop transfer versus conservative sorting pathways for mitochondrial inner membrane proteins in vivo.The Journal of biological chemistry · 2013Article
- A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding.The Journal of cell biology · 2009Article
- The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix.The Journal of biological chemistry · 2008Article
- Effect of protein structure on mitochondrial import.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria.The Journal of cell biology · 2005Article
- Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space.The EMBO journal · 2005Article
- The proteome of Saccharomyces cerevisiae mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.The EMBO journal · 2001Article
- 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
- The dimensions of the protein import channels in the outer and inner mitochondrial membranes.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Article
- Active unfolding of precursor proteins during mitochondrial protein import.The EMBO journal · 1997Article
- Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria.Molecular and cellular biology · 1997Article
- Role of the propilin leader peptide in the maturation of F pilin.Journal of bacteriology · 1996Article
- Import of a DHFR hybrid protein into glycosomes in vivo is not inhibited by the folate-analogue aminopterin.The Journal of cell biology · 1996Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome b2, a protein of the yeast mitochondrial intermembrane space, is synthesized with an 80 residue bipartite presequence. The amino-terminal portion resembles a matrix-targeting signal. The carboxy-terminal portion acts as a 'sorting signal' for the intermembrane space and contains a hydrophobic stretch. In order to define this sorting signal, we fused the first 167 residues of the cytochrome b2 precursor to a passenger protein, expressed the fusion protein in yeast and selected for mutations that caused mislocalization of the passenger protein to the matrix. Most mutations mapped within the first 81 amino-terminal residues of the cytochrome b2 moiety. They were located in three regions, all downstream of the matrix-targeting domain: a cluster of three basic residues upstream of the hydrophobic stretch, the hydrophobic stretch itself and the first residue of mature cytochrome b2. The level of missorting caused by mutations within the hydrophobic stretch did not correlate with their effects on hydrophobicity, but appeared to be related to changes in the conformation of this stretch. We conclude that the intermembrane space sorting signal of cytochrome b2 is decoded by protein-protein interactions rather than by simple partitioning into a lipid bilayer.
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