Relevant bibliographies by topics / Mitochondrial oxidative folding

Academic literature on the topic 'Mitochondrial oxidative folding'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Mitochondrial oxidative folding"

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Morgan, Bruce, and Hui Lu. "Oxidative folding competes with mitochondrial import of the small Tim proteins." Biochemical Journal 411, no. 1 (March 13, 2008): 115–22. http://dx.doi.org/10.1042/bj20071476.

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All small Tim proteins of the mitochondrial intermembrane space contain two conserved CX3C motifs, which form two intramolecular disulfide bonds essential for function, but only the cysteine-reduced, but not oxidized, proteins can be imported into mitochondria. We have shown that Tim10 can be oxidized by glutathione under cytosolic concentrations. However, it was unknown whether oxidative folding of other small Tims can occur under similar conditions and whether oxidative folding competes kinetically with mitochondrial import. In the present study, the effect of glutathione on the cysteine-redox state of Tim9 was investigated, and the standard redox potential of Tim9 was determined to be approx. −0.31 V at pH 7.4 and 25 °C with both the wild-type and Tim9F43W mutant proteins, using reverse-phase HPLC and fluorescence approaches. The results show that reduced Tim9 can be oxidized by glutathione under cytosolic concentrations. Next, we studied the rate of mitochondrial import and oxidative folding of Tim9 under identical conditions. The rate of import was approx. 3-fold slower than that of oxidative folding of Tim9, resulting in approx. 20% of the precursor protein being imported into an excess amount of mitochondria. A similar correlation between import and oxidative folding was obtained for Tim10. Therefore we conclude that oxidative folding and mitochondrial import are kinetically competitive processes. The efficiency of mitochondrial import of the small Tim proteins is controlled, at least partially in vitro, by the rate of oxidative folding, suggesting that a cofactor is required to stabilize the cysteine residues of the precursors from oxidation in vivo.
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Wrobel, Lidia, Agata Trojanowska, Malgorzata E. Sztolsztener, and Agnieszka Chacinska. "Mitochondrial protein import: Mia40 facilitates Tim22 translocation into the inner membrane of mitochondria." Molecular Biology of the Cell 24, no. 5 (March 2013): 543–54. http://dx.doi.org/10.1091/mbc.e12-09-0649.

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The mitochondrial intermembrane space assembly (MIA) pathway is generally considered to be dedicated to the redox-dependent import and biogenesis of proteins localized to the intermembrane space of mitochondria. The oxidoreductase Mia40 is a central component of the pathway responsible for the transfer of disulfide bonds to intermembrane space precursor proteins, causing their oxidative folding. Here we present the first evidence that the function of Mia40 is not restricted to the transport and oxidative folding of intermembrane space proteins. We identify Tim22, a multispanning membrane protein and core component of the TIM22 translocase of inner membrane, as a protein with cysteine residues undergoing oxidation during Tim22 biogenesis. We show that Mia40 is involved in the biogenesis and complex assembly of Tim22. Tim22 forms a disulfide-bonded intermediate with Mia40 upon import into mitochondria. Of interest, Mia40 binds the Tim22 precursor also via noncovalent interactions. We propose that Mia40 not only is responsible for disulfide bond formation, but also assists the Tim22 protein in its integration into the inner membrane of mitochondria.
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Böttinger, Lena, Agnieszka Gornicka, Tomasz Czerwik, Piotr Bragoszewski, Adrianna Loniewska-Lwowska, Agnes Schulze-Specking, Kaye N. Truscott, Bernard Guiard, Dusanka Milenkovic, and Agnieszka Chacinska. "In vivo evidence for cooperation of Mia40 and Erv1 in the oxidation of mitochondrial proteins." Molecular Biology of the Cell 23, no. 20 (October 15, 2012): 3957–69. http://dx.doi.org/10.1091/mbc.e12-05-0358.

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The intermembrane space of mitochondria accommodates the essential mitochondrial intermembrane space assembly (MIA) machinery that catalyzes oxidative folding of proteins. The disulfide bond formation pathway is based on a relay of reactions involving disulfide transfer from the sulfhydryl oxidase Erv1 to Mia40 and from Mia40 to substrate proteins. However, the substrates of the MIA typically contain two disulfide bonds. It was unclear what the mechanisms are that ensure that proteins are released from Mia40 in a fully oxidized form. In this work, we dissect the stage of the oxidative folding relay, in which Mia40 binds to its substrate. We identify dynamics of the Mia40–substrate intermediate complex. Our experiments performed in a native environment, both in organello and in vivo, show that Erv1 directly participates in Mia40–substrate complex dynamics by forming a ternary complex. Thus Mia40 in cooperation with Erv1 promotes the formation of two disulfide bonds in the substrate protein, ensuring the efficiency of oxidative folding in the intermembrane space of mitochondria.
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Fischer, Manuel, Sebastian Horn, Anouar Belkacemi, Kerstin Kojer, Carmelina Petrungaro, Markus Habich, Muna Ali, et al. "Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells." Molecular Biology of the Cell 24, no. 14 (July 15, 2013): 2160–70. http://dx.doi.org/10.1091/mbc.e12-12-0862.

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Oxidation of cysteine residues to disulfides drives import of many proteins into the intermembrane space of mitochondria. Recent studies in yeast unraveled the basic principles of mitochondrial protein oxidation, but the kinetics under physiological conditions is unknown. We developed assays to follow protein oxidation in living mammalian cells, which reveal that import and oxidative folding of proteins are kinetically and functionally coupled and depend on the oxidoreductase Mia40, the sulfhydryl oxidase augmenter of liver regeneration (ALR), and the intracellular glutathione pool. Kinetics of substrate oxidation depends on the amount of Mia40 and requires tightly balanced amounts of ALR. Mia40-dependent import of Cox19 in human cells depends on the inner membrane potential. Our observations reveal considerable differences in the velocities of mitochondrial import pathways: whereas preproteins with bipartite targeting sequences are imported within seconds, substrates of Mia40 remain in the cytosol for several minutes and apparently escape premature degradation and oxidation.
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Szarka, András, and Gábor Bánhegyi. "Oxidative folding: recent developments." BioMolecular Concepts 2, no. 5 (October 1, 2011): 379–90. http://dx.doi.org/10.1515/bmc.2011.038.

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AbstractDisulfide bond formation in proteins is an effective tool of both structure stabilization and redox regulation. The prokaryotic periplasm and the endoplasmic reticulum of eukaryotes were long considered as the only compartments for enzyme mediated formation of stable disulfide bonds. Recently, the mitochondrial intermembrane space has emerged as the third protein-oxidizing compartment. The classic view on the mechanism of oxidative folding in the endoplasmic reticulum has also been reshaped by new observations. Moreover, besides the structure stabilizing function, reversible disulfide bridge formation in some proteins of the endoplasmic reticulum, seems to play a regulatory role. This review briefly summarizes the present knowledge of the redox systems supporting oxidative folding, emphasizing recent developments.
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Bragoszewski, Piotr, Michal Wasilewski, Paulina Sakowska, Agnieszka Gornicka, Lena Böttinger, Jian Qiu, Nils Wiedemann, and Agnieszka Chacinska. "Retro-translocation of mitochondrial intermembrane space proteins." Proceedings of the National Academy of Sciences 112, no. 25 (June 8, 2015): 7713–18. http://dx.doi.org/10.1073/pnas.1504615112.

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The content of mitochondrial proteome is maintained through two highly dynamic processes, the influx of newly synthesized proteins from the cytosol and the protein degradation. Mitochondrial proteins are targeted to the intermembrane space by the mitochondrial intermembrane space assembly pathway that couples their import and oxidative folding. The folding trap was proposed to be a driving mechanism for the mitochondrial accumulation of these proteins. Whether the reverse movement of unfolded proteins to the cytosol occurs across the intact outer membrane is unknown. We found that reduced, conformationally destabilized proteins are released from mitochondria in a size-limited manner. We identified the general import pore protein Tom40 as an escape gate. We propose that the mitochondrial proteome is not only regulated by the import and degradation of proteins but also by their retro-translocation to the external cytosolic location. Thus, protein release is a mechanism that contributes to the mitochondrial proteome surveillance.
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Tang, Xiaofan, Lynda K. Harris, and Hui Lu. "Effects of Liposome and Cardiolipin on Folding and Function of Mitochondrial Erv1." International Journal of Molecular Sciences 21, no. 24 (December 10, 2020): 9402. http://dx.doi.org/10.3390/ijms21249402.

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Erv1 (EC number 1.8.3.2) is an essential mitochondrial enzyme catalyzing protein import and oxidative folding in the mitochondrial intermembrane space. Erv1 has both oxidase and cytochrome c reductase activities. While both Erv1 and cytochrome c were reported to be membrane associated in mitochondria, it is unknown how the mitochondrial membrane environment may affect the function of Erv1. Here, in this study, we used liposomes to mimic the mitochondrial membrane and investigated the effect of liposomes and cardiolipin on the folding and function of yeast Erv1. Enzyme kinetics of both the oxidase and cytochrome c reductase activity of Erv1 were studied using oxygen consumption analysis and spectroscopic methods. Our results showed that the presence of liposomes has mild impacts on Erv1 oxidase activity, but significantly inhibited the catalytic efficiency of Erv1 cytochrome c reductase activity in a cardiolipin-dependent manner. Taken together, the results of this study provide important insights into the function of Erv1 in the mitochondria, suggesting that molecular oxygen is a better substrate than cytochrome c for Erv1 in the yeast mitochondria.
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Clarke, Benjamin E., Bernadett Kalmar, and Linda Greensmith. "Enhanced Expression of TRAP1 Protects Mitochondrial Function in Motor Neurons under Conditions of Oxidative Stress." International Journal of Molecular Sciences 23, no. 3 (February 4, 2022): 1789. http://dx.doi.org/10.3390/ijms23031789.

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TNF-receptor associated protein (TRAP1) is a cytoprotective mitochondrial-specific member of the Hsp90 heat shock protein family of protein chaperones that has been shown to antagonise mitochondrial apoptosis and oxidative stress, regulate the mitochondrial permeability transition pore and control protein folding in mitochondria. Here we show that overexpression of TRAP1 protects motor neurons from mitochondrial dysfunction and death induced by exposure to oxidative stress conditions modelling amyotrophic lateral sclerosis (ALS). ALS is a fatal neurodegenerative disease in which motor neurons degenerate, leading to muscle weakness and atrophy and death, typically within 3 years of diagnosis. In primary murine motor neurons, shRNA-mediated knockdown of TRAP1 expression results in mitochondrial dysfunction but does not further exacerbate damage induced by oxidative stress alone. Together, these results show that TRAP1 may be a potential therapeutic target for neurodegenerative diseases such as ALS, where mitochondrial dysfunction has been shown to be an early marker of pathogenesis.
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Sideris, Dionisia P., and Kostas Tokatlidis. "Oxidative Protein Folding in the Mitochondrial Intermembrane Space." Antioxidants & Redox Signaling 13, no. 8 (October 15, 2010): 1189–204. http://dx.doi.org/10.1089/ars.2010.3157.

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Kojer, Kerstin, Valentina Peleh, Gaetano Calabrese, Johannes M. Herrmann, and Jan Riemer. "Kinetic control by limiting glutaredoxin amounts enables thiol oxidation in the reducing mitochondrial intermembrane space." Molecular Biology of the Cell 26, no. 2 (January 15, 2015): 195–204. http://dx.doi.org/10.1091/mbc.e14-10-1422.

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The mitochondrial intermembrane space (IMS) harbors an oxidizing machinery that drives import and folding of small cysteine-containing proteins without targeting signals. The main component of this pathway is the oxidoreductase Mia40, which introduces disulfides into its substrates. We recently showed that the IMS glutathione pool is maintained as reducing as that of the cytosol. It thus remained unclear how equilibration of protein disulfides with the IMS glutathione pool is prevented in order to allow oxidation-driven protein import. Here we demonstrate the presence of glutaredoxins in the IMS and show that limiting amounts of these glutaredoxins provide a kinetic barrier to prevent the thermodynamically feasible reduction of Mia40 substrates by the IMS glutathione pool. Moreover, they allow Mia40 to exist in a predominantly oxidized state. Consequently, overexpression of glutaredoxin 2 in the IMS results in a more reduced Mia40 redox state and a delay in oxidative folding and mitochondrial import of different Mia40 substrates. Our findings thus indicate that carefully balanced glutaredoxin amounts in the IMS ensure efficient oxidative folding in the reducing environment of this compartment.
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Dissertations / Theses on the topic "Mitochondrial oxidative folding"

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Tran, Peter. "Investigation of the Glutaredoxin system with the biogenesis of mitochondrial intermembrane space proteins." Thesis, University of Manchester, 2016. https://www.research.manchester.ac.uk/portal/en/theses/investigation-of-the-glutaredoxin-system-with-the-biogenesis-of-mitochondrial-intermembrane-space-proteins(9c206b27-529b-4c76-812a-4ba0fb2e7305).html.

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Mitochondrial protein biogenesis depends on the import of nucleus-encoded precursors from the cytosol. Import is highly regulated and specific for different subcompartments, with intermembrane space (IMS) import driven by an oxidative mechanism on conserved cysteine residues. Oxidative folding in the IMS is facilitated by the mitochondria import and assembly (MIA) pathway. Proteins can only be imported into the IMS in Cys-reduced unfolded forms, as oxidation prevents translocation into the IMS. How the import-competent forms are maintained in the cytoplasm is lesser characterised compared to the MIA pathway. Two recent studies suggest that the cytosolic Thioredoxin (Trx) and Glutaredoxin (Grx) reductase systems play a role in facilitating IMS protein import, with previous evidence identifying a role for yeast Trxs in small Tim protein biogenesis. In this study, the redox properties of the yeast Trx and Grx systems were investigated, as well as whether the yeast Grx system play a role in the biogenesis of two typical types of IMS precursor proteins. First, in vitro studies were carried out to determine the standard redox potentials (E°’) of the Trx and Grx enzymes. This was a quantifiable parameter of reducing activity and the results were described in Chapter 3. This study determined the E°’Trx1 value, which was shown to be a more effective reductant compared to other orthologs. Experimental limitations prevented the Grx system E°’ values being determined. Next, whether the Grx plays a role in the biogenesis of the CX3C motif-containing small Tim proteins were investigated using yeast genetic in vivo and biochemical analysis methods. The results were described in Chapter 4. There, Grxs were observed to not affect cell growth, but in using overexpressed Tim9 as an import model, significant differences were observed for the Grx system as GRX deletion significantly decreased overexpressed Tim9 levels. Study on the isolated mitochondria and cytosol with overexpressed Tim9 was unclear however. This study also observed a genetic interaction between GRX andYME1 that recovered cell functioning under respiratory conditions. Finally, whether the Grx system plays a role in the biogenesis of CX9C motif-containing proteins (Mia40, Mia40C and Cox17) was studied in Chapter 5. Whilst Mia40C (C-domain of Mia40) and Cox17 are imported into mitochondria via the MIA pathway, the full-length Mia40 is a substrate of the presequence-targeted TIM23 pathway. The results indicated that import of the full-length Mia40 was unaffected by GRX deletion. However, studies of an overexpressed Mia40C as a substrate of the MIA pathway, showed strong mitochondrial protein level decreases caused by deletion of the Grx proteins. This decrease was also accompanied by an accumulation of unimported Mia40C in the cytosol. Cox17 as an alternative MIA pathway substrate also showed decreased mitochondrial levels in the GRX deletion mutants. These results altogether suggest that the cytosolic Grx system can function in the biogenesis of CX9C motif-containing IMS proteins imported through the MIA pathway, as well as the CX3C small Tim proteins. The topic of how IMS proteins are degraded in the cell was also raised by the study of Yme1.
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Guo, Liang. "Structural and functional studies of mitochondrial small Tim proteins." Thesis, University of Manchester, 2013. https://www.research.manchester.ac.uk/portal/en/theses/structural-and-functional-studies-of-mitochondrial-small-tim-proteins(03dde6fd-6692-4af5-9023-b85a33803fcd).html.

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Most mitochondrial proteins are encoded by nuclear DNA, and synthesised in the cytosol, then imported into the different mitochondrial subcompartments. To reach their destination, mitochondrial inner membrane proteins require import across the outer mitochondrial membrane, and through the intermembrane space. This passage through the IMS is assisted by the small Tim proteins. This family is characterised by conserved cysteine residues arranged in a twin CX3C motif. They can form Tim9-Tim10 and Tim8-Tim13 complexes, while Tim12 appears to form part of a Tim9-Tim10-Tim12 complex that is associated with the inner membrane translocase TIM22 complex. Current models suggest that the biogenesis of small Tim proteins and their assembly into complexes is dependent on the redox states of the proteins. However, the role of the conserved cysteine residues, and the disulphide bonds formed by them, in small Tim biogenesis and complex formation is not clear. As there is no research about the structural characterisation of Tim12 and double cysteine mutants of Tim9, purification of these proteins was attempted using different methods. To investigate how cysteine mutants affect complex formation, the purified double cysteine mutants of Tim9 were studied using in vitro methods. It showed that the double cysteine mutants were partially folded, and they can form complexes with Tim10 with low affinities, suggesting disulphide bonds are important for the structures and complex formation of small Tim proteins. The effect of cysteine mutants on mitochondrial function was addressed using in vivo methods. It showed that cysteines of small Tim proteins were not equally essential for cell viability, and growth defect of the lethal cysteine mutant was caused by low level of protein. Thus, the conclusion of this study is that disulphide bond formation is highly important for correct Tim9- Tim10 complex formation, and yeast can survive with low levels of complex, but it results in instability of the individual proteins.
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Liedgens, Linda [Verfasser], and Michael [Akademischer Betreuer] Lanzer. "Investigation of oxidative protein folding in protist mitochondria and elucidation of the catalytic mechanism of glutaredoxins / Linda Liedgens ; Betreuer: Michael Lanzer." Heidelberg : Universitätsbibliothek Heidelberg, 2019. http://d-nb.info/1196794502/34.

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LUCHINAT, ENRICO. "In-cell NMR for structural and functional studies of proteins in their native environment." Doctoral thesis, 2013. http://hdl.handle.net/2158/787126.

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In this PhD thesis, the in-cell NMR approach was applied to study protein folding and maturation processes at atomic level in living cells. This approach, which relies on protein overexpression, was first applied on living bacterial cells, and was subsequently extended to cultured human cells. Observing the proteins in human cells allowed understanding how the correct cellular environment influences protein folding and redox state, how it controls the availability and binding of the metal cofactors, and how it mediates the effect of specific interacting partners in ways which are yet to be modelled in vitro.
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GALLO, ANGELO. "Characterization of oxidative folding pathway in mitochondria from single structure to protein-protein iteraction." Doctoral thesis, 2010. http://hdl.handle.net/2158/484858.

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GALLO, ANGELO. "Characterization of oxidative folding pathway in mitochondria from single structure to protein-protein interaction." Doctoral thesis, 2010. http://hdl.handle.net/2158/486657.

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Book chapters on the topic "Mitochondrial oxidative folding"

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Herrmann, Johannes M., Bruce Morgan, and Katja Hansen. "CHAPTER 3.2. Disulfide Bond Formation in Mitochondria." In Oxidative Folding of Proteins, 205–23. Cambridge: Royal Society of Chemistry, 2018. http://dx.doi.org/10.1039/9781788013253-00205.

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Sideris, Dionisia P., and Kostas Tokatlidis. "Trapping Oxidative Folding Intermediates During Translocation to the Intermembrane Space of Mitochondria: In Vivo and In Vitro Studies." In Methods in Molecular Biology, 411–23. Totowa, NJ: Humana Press, 2010. http://dx.doi.org/10.1007/978-1-60327-412-8_25.

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