ArticleThe EMBO journal1993
Targeting of cytochrome b2 into the mitochondrial intermembrane space: specific recognition of the sorting signal.
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 31 papers.
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Who cites it
31 citing papers in PubMed.
- Reversal of mitochondrial proteomic loss in Type 1 diabetic heart with overexpression of phospholipid hydroperoxide glutathione peroxidase.American journal of physiology. Regulatory, integrative and comparative physiology · 2013Article
- Dissecting stop transfer versus conservative sorting pathways for mitochondrial inner membrane proteins in vivo.The Journal of biological chemistry · 2013Article
- Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting.Molecular and cellular biology · 2010Article
- A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding.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
- Proteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteins.Molecular biology of the cell · 2006Article
- Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor.Molecular and cellular biology · 2005Article
- 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
- Protein unfolding by mitochondria. The Hsp70 import motor.EMBO reports · 2000Review
- Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis.Molecular and cellular biology · 2000Article
- Unfolding of preproteins upon import into mitochondria.The EMBO journal · 1998Article
- Article
- Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria.Molecular and cellular biology · 1997Article
- Sequential action of two hsp70 complexes during protein import into mitochondria.The EMBO journal · 1997Article
- Probing the environment along the protein import pathways in yeast mitochondria by site-specific photocrosslinking.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins.Molecular and cellular biology · 1996Article
- Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.The EMBO journal · 1996Article
- The delta psi- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria.The EMBO journal · 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
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
unlabelledCytochrome b2 contains 2-fold targeting information: an amino-terminal signal for targeting to the mitochondrial matrix, followed by a second cleavable sorting signal that functions in directing the precursor into the mitochondrial intermembrane space. The role of the second sorting sequence was analyzed by replacing one, two or all of the three positively charged amino acid residues which are present at the amino-terminal side of the hydrophobic core by uncharged residues or an acidic residue. With a number of these mutant precursor proteins, processing to the mature form was reduced or completely abolished and at the same time targeting to the matrix space occurred. The accumulation in the matrix depended on a high level of intramitochondrial ATP. At low levels of matrix ATP, the mutant proteins were sorted into the intermembrane space like the wild-type precursors. THE
results(i) suggest the existence of one or more matrix components that specifically recognize the second sorting signal and thereby trigger the translocation into the intermembrane space; (ii) indicate that the mutant signals have reduced ability to interact with the recognition component(s) and then embark on the default pathway into the matrix by interacting with mitochondrial hsp70 in conjunction with matrix ATP; (iii) strongly argue against a mechanism by which the hydrophobic segment of the sorting sequence stops translocation in the hydrophobic phase of the inner membrane.
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