ArticleThe Journal of cell biology2000
Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Galactokinase 1 Positively Regulates Mitochondrial Respiration by Phosphorylating TIMM13 as a Protein Kinase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Structural basis of client specificity in mitochondrial membrane-protein chaperones.Science advances · 2020Article
- Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5-dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics.Molecular biology of the cell · 2017Article
- TIM29 is a subunit of the human carrier translocase required for protein transport.FEBS letters · 2016Article
- Oxidative folding in the mitochondrial intermembrane space in human health and disease.International journal of molecular sciences · 2013Article
- The power of yeast to model diseases of the powerhouse of the cell.Frontiers in bioscience (Landmark edition) · 2013Review
- Mitochondrial protein synthesis, import, and assembly.Genetics · 2012Article
- Lateral release of proteins from the TOM complex into the outer membrane of mitochondria.The EMBO journal · 2011Article
- Substrate specificity of the TIM22 mitochondrial import pathway revealed with small molecule inhibitor of protein translocation.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import.Molecular biology of the cell · 2009Article
- The Tim8-Tim13 complex has multiple substrate binding sites and binds cooperatively to Tim23.Journal of molecular biology · 2008Article
- Precursor oxidation by Mia40 and Erv1 promotes vectorial transport of proteins into the mitochondrial intermembrane space.Molecular biology of the cell · 2008Article
- Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits.Molecular biology of the cell · 2008Article
- A fluorescence assay for peptide translocation into mitochondria.Analytical biochemistry · 2007Article
- The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import.Molecular biology of the cell · 2007Article
- Formation of membrane-bound ring complexes by prohibitins in mitochondria.Molecular biology of the cell · 2005Article
- Essential role of Mia40 in import and assembly of mitochondrial intermembrane space proteins.The EMBO journal · 2004Article
- Reconstituted TOM core complex and Tim9/Tim10 complex of mitochondria are sufficient for translocation of the ADP/ATP carrier across membranes.Molecular biology of the cell · 2004Article
- Mitochondria use different mechanisms for transport of multispanning membrane proteins through the intermembrane space.Molecular and cellular biology · 2003Article
- Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex.Molecular and cellular biology · 2002Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
Abstract
Tim23p (translocase of the inner membrane) is an essential import component located in the mitochondrial inner membrane. To determine how the Tim23 protein itself is transported into mitochondria, we used chemical cross-linking to identify proteins adjacent to Tim23p during its biogenesis. In the absence of an inner membrane potential, Tim23p is translocated across the mitochondrial outer membrane, but not inserted into the inner membrane. At this intermediate stage, we find that Tim23p forms cross-linked products with two distinct protein complexes of the intermembrane space, Tim8p-Tim13p and Tim9p-Tim10p. Tim9p and Tim10p cross-link to the COOH-terminal domain of the Tim23 protein, which carries all of the targeting signals for Tim23p. Therefore, our results suggest that the Tim9p-Tim10p complex plays a key role in Tim23p import. In contrast, Tim8p and Tim13p cross-link to the hydrophilic NH(2)-terminal segment of Tim23p, which does not carry essential import information and, thus, the role of Tim8p-Tim13p is unclear. Tim23p contains two matrix-facing, positively charged loops that are essential for its insertion into the inner membrane. The positive charges are not required for interaction with the Tim9p-Tim10p complex, but are essential for cross-linking of Tim23p to components of the inner membrane insertion machinery, including Tim54p, Tim22p, and Tim12p.
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