ArticleProtein science : a publication of the Protein Society2010
The intermembrane space domain of Tim23 is intrinsically disordered with a distinct binding region for presequences.
Article in Protein science : a publication of the Protein Society, 2010. 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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24 citing papers in PubMed, 45 citations in OpenAlex.
- Two domains of Tim50 coordinate translocation of proteins across the two mitochondrial membranes.Life science alliance · 2023Article
- Interactions of amyloidogenic proteins with mitochondrial protein import machinery in aging-related neurodegenerative diseases.Frontiers in physiology · 2023Review
- High-Resolution Conformational Analysis of RGDechi-Derived Peptides Based on a Combination of NMR Spectroscopy and MD Simulations.International journal of molecular sciences · 2022Article
- Mapping protein interactions in the active TOM-TIM23 supercomplex.Nature communications · 2021Article
- Coordinated Translocation of Presequence-Containing Precursor Proteins Across Two Mitochondrial Membranes: Knowns and Unknowns of How TOM and TIM23 Complexes Cooperate With Each Other.Frontiers in physiology · 2021Review
- Structural basis of client specificity in mitochondrial membrane-protein chaperones.Science advances · 2020Article
- Mgr2 regulates mitochondrial preprotein import by associating with channel-forming Tim23 subunit.Molecular biology of the cell · 2020Article
- A mutagenesis analysis of Tim50, the major receptor of the TIM23 complex, identifies regions that affect its interaction with Tim23.Scientific reports · 2019Article
- BioSITe: A Method for Direct Detection and Quantitation of Site-Specific Biotinylation.Journal of proteome research · 2018Article
- Cardiolipin mediates membrane and channel interactions of the mitochondrial TIM23 protein import complex receptor Tim50.Science advances · 2017Article
- Article
- The structure of Tim50(164-361) suggests the mechanism by which Tim50 receives mitochondrial presequences.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Folding and self-association of atTic20 in lipid membranes: implications for understanding protein transport across the inner envelope membrane of chloroplasts.BMC biochemistry · 2014Article
- Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes.The Journal of biological chemistry · 2014Article
- Presequence recognition by the tom40 channel contributes to precursor translocation into the mitochondrial matrix.Molecular and cellular biology · 2014Article
- Molecular insights revealing interaction of Tim23 and channel subunits of presequence translocase.Molecular and cellular biology · 2013Article
- Signal recognition initiates reorganization of the presequence translocase during protein import.The EMBO journal · 2013Article
- Role of the AAA protease Yme1 in folding of proteins in the intermembrane space of mitochondria.Molecular biology of the cell · 2012Article
- Direct interaction of mitochondrial targeting presequences with purified components of the TIM23 protein complex.The Journal of biological chemistry · 2011Article
- Tim50's presequence receptor domain is essential for signal driven transport across the TIM23 complex.The Journal of cell biology · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins targeted to the mitochondrial matrix are translocated through the outer and the inner mitochondrial membranes by two protein complexes, the translocase of the outer membrane (TOM) and one of the translocases of the inner membrane (TIM23). The protein Tim23, the core component of TIM23, consists of an N-terminal, soluble domain in the intermembrane space (IMS) and a C-terminal domain that forms the import pore across the inner membrane. Before translocation proceeds, precursor proteins are recognized by the N-terminal domain of Tim23, Tim23N (residues 1-96). By using NMR spectroscopy, we show that Tim23N is a monomeric protein belonging to the family of intrinsically disordered proteins. Titrations of Tim23N with two presequences revealed a distinct binding region of Tim23N formed by residues 71-84. In a charge-hydropathy plot containing all soluble domains of TOM and TIM23, Tim23N was found to be the only domain with more than 40 residues in the IMS that is predicted to be intrinsically disordered, suggesting that Tim23N might function as hub in the mitochondrial import machinery protein network.
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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.