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Journal articles on the topic 'Protein import into mitochondria'

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Published: 2 June 2025

Last updated: 31 July 2025

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1

Asai, Takeyoshi, Takashi Takahashi, Masatoshi Esaki, et al. "Reinvestigation of the Requirement of Cytosolic ATP for Mitochondrial Protein Import." Journal of Biological Chemistry 279, no. 19 (2004): 19464–70. http://dx.doi.org/10.1074/jbc.m401291200.

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Protein import into mitochondria requires the energy of ATP hydrolysis inside and/or outside mitochondria. Although the role of ATP in the mitochondrial matrix in mitochondrial protein import has been extensively studied, the role of ATP outside mitochondria (external ATP) remains only poorly characterized. Here we developed a protocol for depletion of external ATP without significantly reducing the import competence of precursor proteins synthesizedin vitrowith reticulocyte lysate. We tested the effects of external ATP on the import of various precursor proteins into isolated yeast mitochondr

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2

Haastrup, Mary Oluwadamilola, Kunwar Somesh Vikramdeo, Seema Singh, Ajay Pratap Singh, and Santanu Dasgupta. "The Journey of Mitochondrial Protein Import and the Roadmap to Follow." International Journal of Molecular Sciences 24, no. 3 (2023): 2479. http://dx.doi.org/10.3390/ijms24032479.

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Mitochondria are double membrane-bound organelles that play critical functions in cells including metabolism, energy production, regulation of intrinsic apoptosis, and maintenance of calcium homeostasis. Mitochondria are fascinatingly equipped with their own genome and machinery for transcribing and translating 13 essential proteins of the oxidative phosphorylation system (OXPHOS). The rest of the proteins (99%) that function in mitochondria in the various pathways described above are nuclear-transcribed and synthesized as precursors in the cytosol. These proteins are imported into the mitocho

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3

Ahmed, Afsar U., Peter L. Beech, Sui T. Lay, Paul R. Gilson, and Paul R. Fisher. "Import-Associated Translational Inhibition: Novel In Vivo Evidence for Cotranslational Protein Import into Dictyostelium discoideum Mitochondria." Eukaryotic Cell 5, no. 8 (2006): 1314–27. http://dx.doi.org/10.1128/ec.00386-05.

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ABSTRACT To investigate protein import into the mitochondria of Dictyostelium discoideum, green fluorescent protein (GFP) was fused as a reporter protein either to variable lengths of the N-terminal region of chaperonin 60 (the first 23, 40, 80, 97, and 150 amino acids) or to the mitochondrial targeting sequence of DNA topoisomerase II. The fusion proteins were expressed in AX2 cells under the actin-15 promoter. Fluorescence images of GFP transformants confirmed that Dictyostelium chaperonin 60 is a mitochondrial protein. The level of the mitochondrially targeted GFP fusion proteins was unexpe

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4

Craig, E. E., and D. A. Hood. "Influence of aging on protein import into cardiac mitochondria." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 6 (1997): H2983—H2988. http://dx.doi.org/10.1152/ajpheart.1997.272.6.h2983.

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This study was undertaken to determine whether age-related changes in the content and composition of cardiac mitochondria could be due, in part, to alterations in mitochondrial protein import. Precursor proteins malate dehydrogenase and ornithine carbamoyltransferase were synthesized by in vitro transcription and translation and were incubated with mitochondria isolated from the hearts of young (4-mo), old (22-mo), and senescent (28-mo) rats. Mitochondria from senescent animals exhibited a twofold higher import rate of both precursors into the matrix compartment compared with mitochondria from

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5

Althoff, Lukas F. J., Markus M. Kramer, Benjamin Bührer, Denise Gaspar, and Gerald Radziwill. "Optogenetic Control of the Mitochondrial Protein Import in Mammalian Cells." Cells 13, no. 19 (2024): 1671. http://dx.doi.org/10.3390/cells13191671.

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Mitochondria provide cells with energy and regulate the cellular metabolism. Almost all mitochondrial proteins are nuclear-encoded, translated on ribosomes in the cytoplasm, and subsequently transferred to the different subcellular compartments of mitochondria. Here, we developed OptoMitoImport, an optogenetic tool to control the import of proteins into the mitochondrial matrix via the presequence pathway on demand. OptoMitoImport is based on a two-step process: first, light-induced cleavage by a TEV protease cuts off a plasma membrane-anchored fusion construct in close proximity to a mitochon

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6

Kawai, Akemi, Shuh-ichi Nishikawa, Aiko Hirata, and Toshiya Endo. "Loss of the mitochondrial Hsp70 functions causes aggregation of mitochondria in yeast cells." Journal of Cell Science 114, no. 19 (2001): 3565–74. http://dx.doi.org/10.1242/jcs.114.19.3565.

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Ssc1p, a member of the Hsp70 family in the mitochondrial matrix of budding yeast, mediates protein import into mitochondria and prevents irreversible aggregation of proteins in the mitochondrial matrix during folding/assembly or at elevated temperature. Here, we show that functional inactivation of the mitochondrial Hsp70 system causes aggregation of mitochondria. When temperature-sensitive mitochondrial Hsp70 mutant cells were incubated at restrictive temperature, a tubular network of mitochondria was collapsed to form aggregates. Inhibition of protein synthesis in the cytosol did not suppres

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7

Seo, Young Ah, Veronica Lopez, and Shannon L. Kelleher. "A histidine-rich motif mediates mitochondrial localization of ZnT2 to modulate mitochondrial function." American Journal of Physiology-Cell Physiology 300, no. 6 (2011): C1479—C1489. http://dx.doi.org/10.1152/ajpcell.00420.2010.

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Female reproductive tissues such as mammary glands, ovaries, uterus, and placenta are phenotypically dynamic, requiring tight integration of bioenergetic and apoptotic mechanisms. Mitochondrial zinc (Zn) pools have emerged as a central player in regulating bioenergetics and apoptosis. Zn must first be imported into mitochondria to modulate mitochondrion-specific functions; however, mitochondrial Zn import mechanisms have not been identified. Here we documented that the Zn transporter ZnT2 is associated with the inner mitochondrial membrane and acts as an auxiliary Zn importer into mitochondria

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8

Endo, Toshiya, and Haruka Sakaue. "Multifaceted roles of porin in mitochondrial protein and lipid transport." Biochemical Society Transactions 47, no. 5 (2019): 1269–77. http://dx.doi.org/10.1042/bst20190153.

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Abstract Mitochondria are essential eukaryotic organelles responsible for primary cellular energy production. Biogenesis, maintenance, and functions of mitochondria require correct assembly of resident proteins and lipids, which require their transport into and within mitochondria. Mitochondrial normal functions also require an exchange of small metabolites between the cytosol and mitochondria, which is primarily mediated by a metabolite channel of the outer membrane (OM) called porin or voltage-dependent anion channel. Here, we describe recently revealed novel roles of porin in the mitochondr

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9

Ilkow, Carolina S., Daniel Weckbecker, Woo Jung Cho, et al. "The Rubella Virus Capsid Protein Inhibits Mitochondrial Import." Journal of Virology 84, no. 1 (2009): 119–30. http://dx.doi.org/10.1128/jvi.01348-09.

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ABSTRACT The rubella virus (RV) capsid is an RNA-binding protein that functions in nucleocapsid assembly at the Golgi complex, the site of virus budding. In addition to its role in virus assembly, pools of capsid associate with mitochondria, a localization that is not consistent with virus assembly. Here we examined the interaction of capsid with mitochondria and showed that this viral protein inhibits the import and processing of mitochondrial precursor proteins in vitro. Moreover, RV-infected cells were found to contain lower intramitochondrial levels of matrix protein p32. In addition to in

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10

Hamilton, James, Tatiana Brustovetsky, Rajesh Khanna, and Nickolay Brustovetsky. "Mutant huntingtin does not cross the mitochondrial outer membrane." Human Molecular Genetics 29, no. 17 (2020): 2962–75. http://dx.doi.org/10.1093/hmg/ddaa185.

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Abstract Mutant huntingtin (mHTT) is associated with mitochondria, but the exact mitochondrial location of mHTT has not been definitively established. Recently, it was reported that mHTT is present in the intermembrane space and inhibits mitochondrial protein import by interacting with TIM23, a major component of mitochondrial protein import machinery, but evidence for functional ramifications were not provided. We assessed mHTT location using synaptic and nonsynaptic mitochondria isolated from brains of YAC128 mice and subjected to alkali treatment or limited trypsin digestion. Mitochondria w

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11

Harbauer, Angelika B., Magdalena Opalińska, Carolin Gerbeth, et al. "Cell cycle–dependent regulation of mitochondrial preprotein translocase." Science 346, no. 6213 (2014): 1109–13. http://dx.doi.org/10.1126/science.1261253.

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Mitochondria play central roles in cellular energy conversion, metabolism, and apoptosis. Mitochondria import more than 1000 different proteins from the cytosol. It is unknown if the mitochondrial protein import machinery is connected to the cell division cycle. We found that the cyclin-dependent kinase Cdk1 stimulated assembly of the main mitochondrial entry gate, the translocase of the outer membrane (TOM), in mitosis. The molecular mechanism involved phosphorylation of the cytosolic precursor of Tom6 by cyclin Clb3-activated Cdk1, leading to enhanced import of Tom6 into mitochondria. Tom6 p

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12

Zara, V., K. Dietmeier, A. Palmisano, et al. "Yeast mitochondria lacking the phosphate carrier/p32 are blocked in phosphate transport but can import preproteins after regeneration of a membrane potential." Molecular and Cellular Biology 16, no. 11 (1996): 6524–31. http://dx.doi.org/10.1128/mcb.16.11.6524.

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Two different functions have been proposed for the phosphate carrier protein/p32 of Saccharomyces cerevisiae mitochondria: transport of phosphate and requirement for import of precursor proteins into mitochondria. We characterized a yeast mutant lacking the gene for the phosphate carrier/p32 and found both a block in the import of phosphate and a strong reduction in the import of preproteins transported to the mitochondrial inner membrane and matrix. Binding of preproteins to the surface of mutant mitochondria and import of outer membrane proteins were not inhibited, indicating that the inhibi

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13

Chew, Orinda, and James Whelan. "Dual targeting ability of targeting signals is dependent on the nature of the mature protein." Functional Plant Biology 30, no. 7 (2003): 805. http://dx.doi.org/10.1071/fp03077.

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The targeting ability of three signals previously shown to support the import of passenger proteins into both mitochondria and chloroplasts was investigated with authentic mitochondrial or chloroplastic proteins. An in vitro dual import assay that maintained import specificity showed that the ability of dual signals to support mitochondrial and chloroplastic import depended on the nature of the passenger protein. All dual targeting signals supported import of their native mature protein as a passenger into both mitochondria and chloroplasts. However the glutathione reductase targeting signal o

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14

Takahashi, Mark, Alan Chesley, Damien Freyssenet, and David A. Hood. "Contractile activity-induced adaptations in the mitochondrial protein import system." American Journal of Physiology-Cell Physiology 274, no. 5 (1998): C1380—C1387. http://dx.doi.org/10.1152/ajpcell.1998.274.5.c1380.

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We previously demonstrated that subsarcolemmal (SS) and intermyofibrillar (IMF) mitochondrial subfractions import proteins at different rates. This study was undertaken to investigate 1) whether protein import is altered by chronic contractile activity, which induces mitochondrial biogenesis, and 2) whether these two subfractions adapt similarly. Using electrical stimulation (10 Hz, 3 h/day for 7 and 14 days) to induce contractile activity, we observed that malate dehydrogenase import into the matrix of the SS and IMF mitochondia isolated from stimulated muscle was significantly increased by 1

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15

Fünfschilling, Ursula, and Sabine Rospert. "Nascent Polypeptide–associated Complex Stimulates Protein Import into Yeast Mitochondria." Molecular Biology of the Cell 10, no. 10 (1999): 3289–99. http://dx.doi.org/10.1091/mbc.10.10.3289.

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To identify yeast cytosolic proteins that mediate targeting of precursor proteins to mitochondria, we developed an in vitro import system consisting of purified yeast mitochondria and a radiolabeled mitochondrial precursor protein whose C terminus was still attached to the ribosome. In this system, the N terminus of the nascent chain was translocated across both mitochondrial membranes, generating a translocation intermediate spanning both membranes. The nascent chain could then be completely chased into the mitochondrial matrix after release from the ribosome. Generation of this import interm

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16

Wiedemann, Nils, and Nikolaus Pfanner. "Mitochondrial Machineries for Protein Import and Assembly." Annual Review of Biochemistry 86, no. 1 (2017): 685–714. http://dx.doi.org/10.1146/annurev-biochem-060815-014352.

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Mitochondria are essential organelles with numerous functions in cellular metabolism and homeostasis. Most of the >1,000 different mitochondrial proteins are synthesized as precursors in the cytosol and are imported into mitochondria by five transport pathways. The protein import machineries of the mitochondrial membranes and aqueous compartments reveal a remarkable variability of mechanisms for protein recognition, translocation, and sorting. The protein translocases do not operate as separate entities but are connected to each other and to machineries with functions in energetics, membran

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17

Yamamoto, Hayashi, Nobuka Itoh, Shin Kawano, et al. "Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria." Proceedings of the National Academy of Sciences 108, no. 1 (2010): 91–96. http://dx.doi.org/10.1073/pnas.1014918108.

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Mitochondria import most of their resident proteins from the cytosol, and the import receptor Tom20 of the outer-membrane translocator TOM40 complex plays an essential role in specificity of mitochondrial protein import. Here we analyzed the effects of Tom20 binding on NMR spectra of a long mitochondrial presequence and found that it contains two distinct Tom20-binding elements. In vitro import and cross-linking experiments revealed that, although the N-terminal Tom20-binding element is essential for targeting to mitochondria, the C-terminal element increases efficiency of protein import in th

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18

Mokranjac, D., and W. Neupert. "Protein import into mitochondria." Biochemical Society Transactions 33, no. 5 (2005): 1019–23. http://dx.doi.org/10.1042/bst0331019.

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Mitochondria comprise approx. 1000–3000 different proteins, almost all of which must be imported from the cytosol into the organelle. So far, six complex molecular machines, protein translocases, were identified that mediate this process. The TIM23 complex is a major translocase in the inner mitochondrial membrane. It uses two energy sources, namely membrane potential and ATP, to facilitate preprotein translocation across the inner membrane and insertion into the inner membrane. Recent research has led to the discovery of a number of new constituents of the TIM23 complex and to the unravelling

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19

Harkness, TA, FE Nargang, I. van der Klei, W. Neupert, and R. Lill. "A crucial role of the mitochondrial protein import receptor MOM19 for the biogenesis of mitochondria." Journal of Cell Biology 124, no. 5 (1994): 637–48. http://dx.doi.org/10.1083/jcb.124.5.637.

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The novel genetic method of "sheltered RIP" (repeat induced point mutation) was used to generate a Neurospora crassa mutant in which MOM19, a component of the protein import machinery of the mitochondrial outer membrane, can be depleted. Deficiency in MOM19 resulted in a severe growth defect, but the cells remained viable. The number of mitochondrial profiles was not grossly changed, but mutant mitochondria were highly deficient in cristae membranes, cytochromes, and protein synthesis activity. Protein import into isolated mutant mitochondria was decreased by factors of 6 to 30 for most protei

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20

Murcha, Monika W., Dina Elhafez, A. Harvey Millar, and James Whelan. "The C-terminal Region of TIM17 Links the Outer and Inner Mitochondrial Membranes inArabidopsisand Is Essential for Protein Import." Journal of Biological Chemistry 280, no. 16 (2005): 16476–83. http://dx.doi.org/10.1074/jbc.m413299200.

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The translocase of the inner membrane 17 (AtTIM17-2) protein fromArabidopsishas been shown to link the outer and inner mitochondrial membranes. This was demonstrated by several approaches: (i)In vitroorganelle import assays indicated the importedAtTIM17-2 protein remained protease accessible in the outer membrane when inserted into the inner membrane. (ii) N-terminal and C-terminal tagging indicated that it was the C-terminal region that was located in the outer membrane. (iii) Antibodies raised to the C-terminal 100 amino acids recognize a 31-kDa protein from purified mitochondria, but cross-

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21

Miyazaki, Emi, Yuichiro Kida, Katsuyoshi Mihara, and Masao Sakaguchi. "Switching the Sorting Mode of Membrane Proteins from Cotranslational Endoplasmic Reticulum Targeting to Posttranslational Mitochondrial Import." Molecular Biology of the Cell 16, no. 4 (2005): 1788–99. http://dx.doi.org/10.1091/mbc.e04-08-0707.

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Hydrophobic membrane proteins are cotranslationally targeted to the endoplasmic reticulum (ER) membrane, mediated by hydrophobic signal sequence. Mitochondrial membrane proteins escape this mechanism despite their hydrophobic character. We examined sorting of membrane proteins into the mitochondria, by using mitochondrial ATP-binding cassette (ABC) transporter isoform (ABC-me). In the absence of 135-residue N-terminal hydrophilic segment (N135), the membrane domain was integrated into the ER membrane in COS7 cells. Other sequences that were sufficient to import soluble protein into mitochondri

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22

Mohanraj, Karthik, Urszula Nowicka, and Agnieszka Chacinska. "Mitochondrial control of cellular protein homeostasis." Biochemical Journal 477, no. 16 (2020): 3033–54. http://dx.doi.org/10.1042/bcj20190654.

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Mitochondria are involved in several vital functions of the eukaryotic cell. The majority of mitochondrial proteins are coded by nuclear DNA. Constant import of proteins from the cytosol is a prerequisite for the efficient functioning of the organelle. The protein import into mitochondria is mediated by diverse import pathways and is continuously under watch by quality control systems. However, it is often challenged by both internal and external factors, such as oxidative stress or energy shortage. The impaired protein import and biogenesis leads to the accumulation of mitochondrial precursor

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23

Saleem, Ayesha, Sobia Iqbal, Yuan Zhang, and David A. Hood. "Effect of p53 on mitochondrial morphology, import, and assembly in skeletal muscle." American Journal of Physiology-Cell Physiology 308, no. 4 (2015): C319—C329. http://dx.doi.org/10.1152/ajpcell.00253.2014.

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The purpose of this study was to investigate whether p53 regulates mitochondrial function via changes in mitochondrial protein import, complex IV (COX) assembly, or the expression of key proteins involved in mitochondrial dynamics and degradation. Mitochondria from p53 KO mice displayed ultra-structural alterations and were more punctate in appearance. This was accompanied by protein-specific alterations in fission, fusion, and mitophagy-related proteins. However, matrix-destined protein import into subsarcolemmal or intermyofibrillar mitochondria was unaffected in the absence of p53, despite

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Hamilton, VaNae, Ujjal K. Singha, Joseph T. Smith, Ebony Weems, and Minu Chaudhuri. "Trypanosome Alternative Oxidase Possesses both an N-Terminal and Internal Mitochondrial Targeting Signal." Eukaryotic Cell 13, no. 4 (2014): 539–47. http://dx.doi.org/10.1128/ec.00312-13.

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ABSTRACTRecognition of mitochondrial targeting signals (MTS) by receptor translocases of outer and inner membranes of mitochondria is one of the prerequisites for import of nucleus-encoded proteins into this organelle. The MTS for a majority of trypanosomatid mitochondrial proteins have not been well defined. Here we analyzed the targeting signal for trypanosome alternative oxidase (TAO), which functions as the sole terminal oxidase in the infective form ofTrypanosoma brucei. Deleting the first 10 of 24 amino acids predicted to be the classical N-terminal MTS of TAO did not affect its import i

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Pon, L., T. Moll, D. Vestweber, B. Marshallsay, and G. Schatz. "Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins." Journal of Cell Biology 109, no. 6 (1989): 2603–16. http://dx.doi.org/10.1083/jcb.109.6.2603.

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To identify the membrane regions through which yeast mitochondria import proteins from the cytoplasm, we have tagged these regions with two different partly translocated precursor proteins. One of these was bound to the mitochondrial surface of ATP-depleted mitochondria and could subsequently be chased into mitochondria upon addition of ATP. The other intermediate was irreversibly stuck across both mitochondrial membranes at protein import sites. Upon subfraction of the mitochondria, both intermediates cofractionated with membrane vesicles whose buoyant density was between that of inner and ou

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Emtage, JL, and RE Jensen. "MAS6 encodes an essential inner membrane component of the yeast mitochondrial protein import pathway." Journal of Cell Biology 122, no. 5 (1993): 1003–12. http://dx.doi.org/10.1083/jcb.122.5.1003.

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To identify new components that mediate mitochondrial protein import, we analyzed mas6, an import mutant in the yeast Saccharomyces cerevisiae. mas6 mutants are temperature sensitive for viability, and accumulate mitochondrial precursor proteins at the restrictive temperature. We show that mas6 does not correspond to any of the presently identified import mutants, and we find that mitochondria isolated from mas6 mutants are defective at an early stage of the mitochondrial protein import pathway. MAS6 encodes a 23-kD protein that contains several potential membrane spanning domains, and yeast s

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27

Jadiya, Pooja, and Dhanendra Tomar. "Mitochondrial Protein Quality Control Mechanisms." Genes 11, no. 5 (2020): 563. http://dx.doi.org/10.3390/genes11050563.

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Mitochondria serve as a hub for many cellular processes, including bioenergetics, metabolism, cellular signaling, redox balance, calcium homeostasis, and cell death. The mitochondrial proteome includes over a thousand proteins, encoded by both the mitochondrial and nuclear genomes. The majority (~99%) of proteins are nuclear encoded that are synthesized in the cytosol and subsequently imported into the mitochondria. Within the mitochondria, polypeptides fold and assemble into their native functional form. Mitochondria health and integrity depend on correct protein import, folding, and regulate

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Hauser, R., M. Pypaert, T. Hausler, E. K. Horn, and A. Schneider. "In vitro import of proteins into mitochondria of Trypanosoma brucei and Leishmania tarentolae." Journal of Cell Science 109, no. 2 (1996): 517–23. http://dx.doi.org/10.1242/jcs.109.2.517.

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In eukaryotic evolution, the earliest branch of organisms to have mitochondria are the trypanosomatids. Their mitochondrial biogenesis not only includes import of most proteins, but also, unlike in other organisms, import of the whole set of tRNAs. In order to investigate these processes, we devised novel procedures for the isolation of mitochondria from two trypanosomatid species: Trypanosoma brucei and Leishmania tarentolae. Isotonic cell lysis followed by equilibrium density centrifugation in Nycodenz gradients yielded mitochondrial fractions exhibiting a membrane potential. Furthermore, we

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Baseler, Walter A., Erinne R. Dabkowski, Courtney L. Williamson, et al. "Proteomic alterations of distinct mitochondrial subpopulations in the type 1 diabetic heart: contribution of protein import dysfunction." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 300, no. 2 (2011): R186—R200. http://dx.doi.org/10.1152/ajpregu.00423.2010.

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Diabetic cardiomyopathy is associated with increased risk of heart failure in type 1 diabetic patients. Mitochondrial dysfunction is suggested as an underlying contributor to diabetic cardiomyopathy. Cardiac mitochondria are characterized by subcellular spatial locale, including mitochondria located beneath the sarcolemma, subsarcolemmal mitochondria (SSM), and mitochondria situated between the myofibrils, interfibrillar mitochondria (IFM). The goal of this study was to determine whether type 1 diabetic insult in the heart influences proteomic make-up of spatially distinct mitochondrial subpop

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Ruan, Linhao, Yuhao Wang, Xi Zhang, Alexis Tomaszewski, Joshua T. McNamara, and Rong Li. "Mitochondria-Associated Proteostasis." Annual Review of Biophysics 49, no. 1 (2020): 41–67. http://dx.doi.org/10.1146/annurev-biophys-121219-081604.

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Mitochondria are essential organelles in eukaryotes. Most mitochondrial proteins are encoded by the nuclear genome and translated in the cytosol. Nuclear-encoded mitochondrial proteins need to be imported, processed, folded, and assembled into their functional states. To maintain protein homeostasis (proteostasis), mitochondria are equipped with a distinct set of quality control machineries. Deficiencies in such systems lead to mitochondrial dysfunction, which is a hallmark of aging and many human diseases, such as neurodegenerative diseases, cardiovascular diseases, and cancer. In this review

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Rödl, Saskia, Fabian den Brave, Markus Räschle, et al. "The metabolite-controlled ubiquitin conjugase Ubc8 promotes mitochondrial protein import." Life Science Alliance 6, no. 1 (2022): e202201526. http://dx.doi.org/10.26508/lsa.202201526.

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Mitochondria play a key role in cellular energy metabolism. Transitions between glycolytic and respiratory conditions induce considerable adaptations of the cellular proteome. These metabolism-dependent changes are particularly pronounced for the protein composition of mitochondria. Here, we show that the yeast cytosolic ubiquitin conjugase Ubc8 plays a crucial role in the remodeling process when cells transition from respiratory to fermentative conditions. Ubc8 is a conserved and well-studied component of the catabolite control system that is known to regulate the stability of gluconeogenic e

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Krimmer, Thomas, Doron Rapaport, Michael T. Ryan, et al. "Biogenesis of Porin of the Outer Mitochondrial Membrane Involves an Import Pathway via Receptors and the General Import Pore of the Tom Complex." Journal of Cell Biology 152, no. 2 (2001): 289–300. http://dx.doi.org/10.1083/jcb.152.2.289.

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Porin, also termed the voltage-dependent anion channel, is the most abundant protein of the mitochondrial outer membrane. The process of import and assembly of the protein is known to be dependent on the surface receptor Tom20, but the requirement for other mitochondrial proteins remains controversial. We have used mitochondria from Neurospora crassa and Saccharomyces cerevisiae to analyze the import pathway of porin. Import of porin into isolated mitochondria in which the outer membrane has been opened is inhibited despite similar levels of Tom20 as in intact mitochondria. A matrix-destined p

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Yermovsky-Kammerer, Audra E., and Stephen L. Hajduk. "In Vitro Import of a Nuclearly Encoded tRNA into the Mitochondrion of Trypanosoma brucei." Molecular and Cellular Biology 19, no. 9 (1999): 6253–59. http://dx.doi.org/10.1128/mcb.19.9.6253.

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ABSTRACT All of the mitochondrial tRNAs of Trypanosoma bruceihave been shown to be encoded in the nucleus and must be imported into the mitochondrion. The import of nuclearly encoded tRNAs into the mitochondrion has been demonstrated in a variety of organisms and is essential for proper function in the mitochondrion. An in vitro import assay has been developed to study the pathway of tRNA import inT. brucei. The in vitro system utilizes crude isolated trypanosome mitochondria and synthetic RNAs transcribed from a cloned nucleus-encoded tRNA gene cluster. The substrate, composed of tRNASer and

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34

Hoffmann, Juliane J., and Thomas Becker. "Crosstalk between Mitochondrial Protein Import and Lipids." International Journal of Molecular Sciences 23, no. 9 (2022): 5274. http://dx.doi.org/10.3390/ijms23095274.

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Mitochondria import about 1000 precursor proteins from the cytosol. The translocase of the outer membrane (TOM complex) forms the major entry site for precursor proteins. Subsequently, membrane-bound protein translocases sort the precursor proteins into the outer and inner membrane, the intermembrane space, and the matrix. The phospholipid composition of mitochondrial membranes is critical for protein import. Structural and biochemical data revealed that phospholipids affect the stability and activity of mitochondrial protein translocases. Integration of proteins into the target membrane invol

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Yano, Masato, Kazutoyo Terada, and Masataka Mori. "AIP is a mitochondrial import mediator that binds to both import receptor Tom20 and preproteins." Journal of Cell Biology 163, no. 1 (2003): 45–56. http://dx.doi.org/10.1083/jcb.200305051.

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Most mitochondrial preproteins are maintained in a loosely folded import-competent conformation by cytosolic chaperones, and are imported into mitochondria by translocator complexes containing a preprotein receptor, termed translocase of the outer membrane of mitochondria (Tom) 20. Using two-hybrid screening, we identified arylhydrocarbon receptor–interacting protein (AIP), an FK506-binding protein homologue, interacting with Tom20. The extreme COOH-terminal acidic segment of Tom20 was required for interaction with tetratricopeptide repeats of AIP. An in vitro import assay indicated that AIP p

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Tamura, Yasushi, Yoshihiro Harada, Koji Yamano, et al. "Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria." Journal of Cell Biology 174, no. 5 (2006): 631–37. http://dx.doi.org/10.1083/jcb.200603087.

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Newly synthesized mitochondrial proteins are imported into mitochondria with the aid of protein translocator complexes in the outer and inner mitochondrial membranes. We report the identification of yeast Tam41, a new member of mitochondrial protein translocator systems. Tam41 is a peripheral inner mitochondrial membrane protein facing the matrix. Disruption of the TAM41 gene led to temperature-sensitive growth of yeast cells and resulted in defects in protein import via the TIM23 translocator complex at elevated temperature both in vivo and in vitro. Although Tam41 is not a constituent of the

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Straub, Sebastian P., Sebastian B. Stiller, Nils Wiedemann, and Nikolaus Pfanner. "Dynamic organization of the mitochondrial protein import machinery." Biological Chemistry 397, no. 11 (2016): 1097–114. http://dx.doi.org/10.1515/hsz-2016-0145.

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Abstract Mitochondria contain elaborate machineries for the import of precursor proteins from the cytosol. The translocase of the outer mitochondrial membrane (TOM) performs the initial import of precursor proteins and transfers the precursors to downstream translocases, including the presequence translocase and the carrier translocase of the inner membrane, the mitochondrial import and assembly machinery of the intermembrane space, and the sorting and assembly machinery of the outer membrane. Although the protein translocases can function as separate entities in vitro, recent studies revealed

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SHIAO, Young-Ji, Bénédicte BALCERZAK, and Jean E. VANCE. "A mitochondrial membrane protein is required for translocation of phosphatidylserine from mitochondria-associated membranes to mitochondria." Biochemical Journal 331, no. 1 (1998): 217–23. http://dx.doi.org/10.1042/bj3310217.

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The mechanism of import of phosphatidylserine (PtdSer) into mitochondria was investigated using a reconstituted system of isolated organelles in vitroin which PtdSer was translocated from donor membranes to mitochondria and was decarboxylated therein. Neither phosphatidylcholine nor phosphatidylethanolamine (PtdEtn) was translocated under the same conditions. Transfer of PtdSer from its site of synthesis on the endoplasmic reticulum and mitochondria-associated membranes [J. E. Vance (1990) J. Biol. Chem. 265, 7248–7256] to its site of decarboxylation on mitochondrial inner membranes is predict

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Zöller, Eva, Janina Laborenz, Lena Krämer, et al. "The intermembrane space protein Mix23 is a novel stress-induced mitochondrial import factor." Journal of Biological Chemistry 295, no. 43 (2020): 14686–97. http://dx.doi.org/10.1074/jbc.ra120.014247.

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The biogenesis of mitochondria requires the import of hundreds of precursor proteins. These proteins are transported post-translationally with the help of chaperones, meaning that the overproduction of mitochondrial proteins or the limited availability of chaperones can lead to the accumulation of cytosolic precursor proteins. This imposes a severe challenge to cytosolic proteostasis and triggers a specific transcription program called the mitoprotein-induced stress response, which activates the proteasome system. This coincides with the repression of mitochondrial proteins, including many pro

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Neupert, W., and D. Mokranjac. "Protein import into mitochondria." Biochemical Society Transactions 33, no. 5 (2005): 1019. http://dx.doi.org/10.1042/bst20051019.

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Neupert, Walter. "PROTEIN IMPORT INTO MITOCHONDRIA." Annual Review of Biochemistry 66, no. 1 (1997): 863–917. http://dx.doi.org/10.1146/annurev.biochem.66.1.863.

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Paschen, Stefan A., and Walter Neupert. "Protein Import Into Mitochondria." IUBMB Life (International Union of Biochemistry and Molecular Biology: Life) 52, no. 3-5 (2001): 101–12. http://dx.doi.org/10.1080/15216540152845894.

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Vestweber, D., and G. Schatz. "A chimeric mitochondrial precursor protein with internal disulfide bridges blocks import of authentic precursors into mitochondria and allows quantitation of import sites." Journal of Cell Biology 107, no. 6 (1988): 2037–43. http://dx.doi.org/10.1083/jcb.107.6.2037.

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Bovine pancreatic trypsin inhibitor (which contains three intramolecular disulfide bridges) was chemically coupled to the COOH terminus of a purified artificial mitochondrial precursor protein. When the resulting chimeric precursor was presented to energized isolated yeast mitochondria, its trypsin inhibitor moiety prevented the protein from completely entering the organelle; the protein remained stuck across both mitochondrial membranes, with its NH2 terminus in the matrix and its trypsin inhibitor moiety still exposed on the mitochondrial surface. The incompletely imported protein appeared t

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Sulkshane, Prasad, Jonathan Ram, and Michael H. Glickman. "Ubiquitination of Intramitochondrial Proteins: Implications for Metabolic Adaptability." Biomolecules 10, no. 11 (2020): 1559. http://dx.doi.org/10.3390/biom10111559.

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Mitochondria are constantly subjected to stressful conditions due to their unique physiology and organization. The resulting damage leads to mitochondrial dysfunction, which underlies many pathophysiological conditions. Hence, constant surveillance is required to closely monitor mitochondrial health for sound maintenance of cellular metabolism and thus, for viability. In addition to internal mitochondrial chaperones and proteases, mitochondrial health is also governed by host cell protein quality control systems. The ubiquitin-proteasome system (UPS) and autophagy constitute the main pathways

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Hood, David A., and Anna-Maria Joseph. "Mitochondrial assembly: protein import." Proceedings of the Nutrition Society 63, no. 2 (2004): 293–300. http://dx.doi.org/10.1079/pns2004342.

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The protein import process of mitochondria is vital for the assembly of the hundreds of nuclear-derived proteins into an expanding organelle reticulum. Most of our knowledge of this complex multisubunit network comes from studies of yeast and fungal systems, with little information known about the protein import process in mammalian cells, particularly skeletal muscle. However, growing evidence indicates that the protein import machinery can respond to changes in the energy status of the cell. In particular, contractile activity, a powerful inducer of mitochondrial biogenesis, has been shown t

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Lin, Brian C., Trong H. Phung, Nicole R. Higgins, et al. "ALS/FTD mutations in UBQLN2 are linked to mitochondrial dysfunction through loss-of-function in mitochondrial protein import." Human Molecular Genetics 30, no. 13 (2021): 1230–46. http://dx.doi.org/10.1093/hmg/ddab116.

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Abstract UBQLN2 mutations cause amyotrophic lateral sclerosis (ALS) with frontotemporal dementia (FTD), but the pathogenic mechanisms by which they cause disease remain unclear. Proteomic profiling identified ‘mitochondrial proteins’ as comprising the largest category of protein changes in the spinal cord (SC) of the P497S UBQLN2 mouse model of ALS/FTD. Immunoblots confirmed P497S animals have global changes in proteins predictive of a severe decline in mitochondrial health, including oxidative phosphorylation (OXPHOS), mitochondrial protein import and network dynamics. Functional studies conf

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MUKHOPADHYAY, Abhijit, Li NI, and Henry WEINER. "A co-translational model to explain the in vivo import of proteins into HeLa cell mitochondria." Biochemical Journal 382, no. 1 (2004): 385–92. http://dx.doi.org/10.1042/bj20040065.

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The dual signal approach, i.e. a mitochondrial signal at the N-terminus and an ER (endoplasmic reticulum) or a peroxisomal signal at the C-terminus of EGFP (enhanced green fluorescent protein), was employed in transfected HeLa cells to test for a co-translational import model. The signal peptide from OTC (ornithine transcarbamylase) or arginase II was fused to the N-terminus of EGFP, and an ER or peroxisomal signal was fused to its C-terminus. The rationale was that if the free preprotein remained in the cytosol, it could be distributed between the two organelles by using a post-translational

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Wachter, C., G. Schatz, and B. S. Glick. "Protein import into mitochondria: the requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix." Molecular Biology of the Cell 5, no. 4 (1994): 465–74. http://dx.doi.org/10.1091/mbc.5.4.465.

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ATP is needed for the import of precursor proteins into mitochondria. However, the role of ATP and its site of action have been unclear. We have now investigated the ATP requirements for protein import into the mitochondrial matrix. These experiments employed an in vitro system that allowed ATP levels to be manipulated both inside and outside the mitochondrial inner membrane. Our results indicate that there are two distinct ATP requirements for mitochondrial protein import. ATP in the matrix is always needed for complete import of precursor proteins into this compartment, even when the precurs

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Nguyen, Tiffany, Renee Wong, Guanghui Wang, Marjan Gucek, Charles Steenbergen, and Elizabeth Murphy. "Acute inhibition of GSK causes mitochondrial remodeling." American Journal of Physiology-Heart and Circulatory Physiology 302, no. 11 (2012): H2439—H2445. http://dx.doi.org/10.1152/ajpheart.00033.2012.

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Recent data have shown that cardioprotection can result in the import of specific proteins into the mitochondria in a process that involves heat shock protein 90 (HSP90) and is blocked by geldanamycin (GD), a HSP90 inhibitor. To test the hypothesis that an alteration in mitochondrial import is a more widespread feature of cardioprotection, in this study, we used a broad-based proteomics approach to investigate changes in the mitochondrial proteome following cardioprotection induced by inhibition of glycogen synthase kinase (GSK)-3. Mitochondria were isolated from control hearts, and hearts wer

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Murakami, H., D. Pain, and G. Blobel. "70-kD heat shock-related protein is one of at least two distinct cytosolic factors stimulating protein import into mitochondria." Journal of Cell Biology 107, no. 6 (1988): 2051–57. http://dx.doi.org/10.1083/jcb.107.6.2051.

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We have developed an in vitro system in which the posttranslational import of Put2 (delta-pyrroline-5-carboxylate dehydrogenase), into yeast mitochondria is dependent on the addition of yeast postribosomal supernatant (PRS). When mRNA for a nuclear-encoded yeast mitochondrial matrix protein, Put2, was translated in a wheat germ cell-free system, import into posttranslationally added yeast mitochondria was negligible. However, when a yeast PRS was added, significant import was observed. The import stimulating activity of the yeast PRS was shown to consist of at least two distinct factors. One o

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