ArticleMolecular and cellular biology1998
Characterization of the mitochondrial inner membrane translocase complex: the Tim23p hydrophobic domain interacts with Tim17p but not with other Tim23p molecules.
Article in Molecular and cellular biology, 1998. 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.
- Cation selectivity of the presequence translocase channel Tim23 is crucial for efficient protein import.eLife · 2017Article
- Bacterial tail anchors can target to the mitochondrial outer membrane.Biology direct · 2017Article
- Article
- A disulfide bond in the TIM23 complex is crucial for voltage gating and mitochondrial protein import.The Journal of cell biology · 2016Article
- Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motor.The Journal of biological chemistry · 2014Article
- Activation of the pleiotropic drug resistance pathway can promote mitochondrial DNA retention by fusion-defective mitochondria in Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2014Article
- Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.Genetics · 2012Article
- Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease complex.Molecular biology of the cell · 2008Article
- Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane.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
- The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import.Molecular biology of the cell · 2007Article
- A genomewide screen for petite-negative yeast strains yields a new subunit of the i-AAA protease complex.Molecular biology of the cell · 2006Article
- Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex.The EMBO journal · 2003Article
- Tim50, a novel component of the TIM23 preprotein translocase of mitochondria.The EMBO journal · 2003Article
- Import of proteins into mitochondria: a novel pathomechanism for progressive neurodegeneration.Journal of inherited metabolic disease · 2001Review
- Division of mitochondria requires a novel DNM1-interacting protein, Net2p.Molecular biology of the cell · 2001Article
- Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria.The Journal of cell biology · 2000Article
- MCC and PSC, the putative protein import channels of mitochondria.Journal of bioenergetics and biomembranes · 2000Review
- Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane.Molecular biology of the cell · 2000Article
- The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.The Journal of cell biology · 1999Article
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Authors and funding
3 authors.
Funding
Abstract
Tim23p is a mitochondrial inner membrane protein essential for the import of proteins from the cytosol. Tim23p contains an amino-terminal hydrophilic segment and a carboxyl-terminal hydrophobic domain (Tim23Cp). To study the functions and interactions of the two parts of Tim23p separately, we constructed tim23N, encoding only the hydrophilic region of Tim23p, and tim23C, encoding only the hydrophobic domain of Tim23p. Only the Tim23C protein is imported into mitochondria, indicating that the mitochondrial targeting information in Tim23p resides in its membrane spans or intervening loops. Tim23Cp, however, cannot substitute for full-length Tim23p, suggesting that the hydrophilic portion of Tim23p also performs an essential function in mitochondrial protein import. We found that overexpression of Tim23Cp is toxic to yeast cells that carry the tim23-1 mutation. Excess Tim23Cp causes Tim23-1p to disappear, leaving tim23-1 cells without a full-length version of the Tim23 protein. If Tim17p, another inner membrane import component, is overexpressed along with Tim23Cp, the toxicity of Tim23Cp is largely reversed and the Tim23-1 protein no longer disappears. In coimmunoprecipitations from solubilized mitochondria, Tim17p associates with the Tim23C protein. In addition, we show that Tim23p and Tim17p can be chemically cross-linked to each other in intact mitochondria. We conclude that the hydrophobic domain encoded by tim23C targets Tim23p to the mitochondria and mediates the direct interaction between Tim23p and Tim17p. In contrast, Tim23Cp cannot be coimmunoprecipitated with Tim23p, raising the possibility that the hydrophobic domain of Tim23p does not interact with other Tim23 molecules.
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