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Journal articles on the topic 'Mitochondrial targeting sequence'

Author: Grafiati

Published: 25 May 2024

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1

LEISSRING, Malcolm A., Wesley FARRIS, Xining WU, et al. "Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria." Biochemical Journal 383, no. 3 (2004): 439–46. http://dx.doi.org/10.1042/bj20041081.

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IDE (insulin-degrading enzyme) is a widely expressed zinc-metallopeptidase that has been shown to regulate both cerebral amyloid β-peptide and plasma insulin levels in vivo. Genetic linkage and allelic association have been reported between the IDE gene locus and both late-onset Alzheimer's disease and Type II diabetes mellitus, suggesting that altered IDE function may contribute to some cases of these highly prevalent disorders. Despite the potentially great importance of this peptidase to health and disease, many fundamental aspects of IDE biology remain unresolved. Here we identify a previo

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2

Faria, Rúben, Eric Vivés, Prisca Boisguerin, Angela Sousa, and Diana Costa. "Development of Peptide-Based Nanoparticles for Mitochondrial Plasmid DNA Delivery." Polymers 13, no. 11 (2021): 1836. http://dx.doi.org/10.3390/polym13111836.

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A mitochondrion is a cellular organelle able to produce cellular energy in the form of adenosine triphosphate (ATP). As in the nucleus, mitochondria contain their own genome: the mitochondrial DNA (mtDNA). This genome is particularly susceptible to mutations that are at the basis of a multitude of disorders, especially those affecting the heart, the central nervous system and muscles. Conventional clinical practice applied to mitochondrial diseases is very limited and ineffective; a clear need for innovative therapies is demonstrated. Gene therapy seems to be a promising approach. The use of m

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Baysal, Can, Ana Pérez-González, Álvaro Eseverri, et al. "Recognition motifs rather than phylogenetic origin influence the ability of targeting peptides to import nuclear-encoded recombinant proteins into rice mitochondria." Transgenic Research 29, no. 1 (2019): 37–52. http://dx.doi.org/10.1007/s11248-019-00176-9.

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Abstract Mitochondria fulfil essential functions in respiration and metabolism as well as regulating stress responses and apoptosis. Most native mitochondrial proteins are encoded by nuclear genes and are imported into mitochondria via one of several receptors that recognize N-terminal signal peptides. The targeting of recombinant proteins to mitochondria therefore requires the presence of an appropriate N-terminal peptide, but little is known about mitochondrial import in monocotyledonous plants such as rice (Oryza sativa). To gain insight into this phenomenon, we targeted nuclear-encoded enh

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Kaufmann, Thomas, Sarah Schlipf, Javier Sanz, Karin Neubert, Reuven Stein, and Christoph Borner. "Characterization of the signal that directs Bcl-xL, but not Bcl-2, to the mitochondrial outer membrane." Journal of Cell Biology 160, no. 1 (2003): 53–64. http://dx.doi.org/10.1083/jcb.200210084.

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It is assumed that the survival factors Bcl-2 and Bcl-xL are mainly functional on mitochondria and therefore must contain mitochondrial targeting sequences. Here we show, however, that only Bcl-xL is specifically targeted to the mitochondrial outer membrane (MOM) whereas Bcl-2 distributes on several intracellular membranes. Mitochondrial targeting of Bcl-xL requires the COOH-terminal transmembrane (TM) domain flanked at both ends by at least two basic amino acids. This sequence is a bona fide targeting signal for the MOM as it confers specific mitochondrial localization to soluble EGFP. The si

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Takada, Y., N. Kaneko, H. Esumi, P. E. Purdue, and C. J. Danpure. "Human peroxisomal l-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon." Biochemical Journal 268, no. 2 (1990): 517–20. http://dx.doi.org/10.1042/bj2680517.

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The amino acid sequence of human hepatic peroxisomal L-alanine: glyoxylate aminotransferase 1 (AGTI) deduced from cDNA shows 78% sequence identity with that of rat mitochondrial AGTI, but lacks the N-terminal 22 amino acids (the putative mitochondrial targeting signal). In humans this signal appears to have been deleted during evolution by a point mutation of the initiation codon ATG to ATA. These data suggest that the targeting defect in primary hyperoxaluria type 1, in which AGT1 is diverted from the peroxisomes to the mitochondria, could be due to a point mutation that reintroduces all or p

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Majumdar, Ramanath, та William A. Bridger. "Mitochondrial translocation and processing of the precursor to the α-subunit of rat liver succinyl-CoA synthetase". Biochemistry and Cell Biology 68, № 1 (1990): 292–99. http://dx.doi.org/10.1139/o90-040.

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Succinyl-CoA synthetase functions in the mitochondrial matrix as an αβ-dimer. Its constitutive subunits are thus expected to be encoded in the nucleus and synthesized in the cytoplasm as precursors containing signal sequences for mitochondrial translocation. We have previously reported the isolation and sequence of a rat liver cDNA clone (λSCS19) that apparently encodes the cytoplasmic precursor to the α-subunit. Here we report the preparation of mRNA transcripts of this cDNA insert and their in vitro translation to produce labeled protein that can be translocated across the membranes of subse

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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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8

Romesberg, Amy, and Bennett Van Houten. "Targeting Mitochondrial Function with Chemoptogenetics." Biomedicines 10, no. 10 (2022): 2459. http://dx.doi.org/10.3390/biomedicines10102459.

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Mitochondria are ATP-generating organelles in eukaryotic cells that produce reactive oxygen species (ROS) during oxidative phosphorylation (OXPHOS). Mitochondrial DNA (mtDNA) is packaged within nucleoids and, due to its close proximity to ROS production, endures oxidative base damage. This damage can be repaired by base excision repair (BER) within the mitochondria, or it can be degraded via exonucleases or mitophagy. Persistent mtDNA damage may drive the production of dysfunctional OXPHOS components that generate increased ROS, or OXPHOS components may be directly damaged by ROS, which then c

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9

Chang, Yu-Jung, Kuan-Wei Chen, and Linyi Chen. "Mitochondrial ROS1 Increases Mitochondrial Fission and Respiration in Oral Squamous Cancer Carcinoma." Cancers 12, no. 10 (2020): 2845. http://dx.doi.org/10.3390/cancers12102845.

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Increased ROS proto-oncogene 1 (ROS1) expression has been implicated in the invasiveness of human oral squamous cell carcinoma (OSCC). The cellular distribution of ROS1 has long-been assumed at the plasma membrane. However, a previous work reported a differential cellular distribution of mutant ROS1 derived from chromosomal translocation, resulting in increased carcinogenesis. We thus hypothesized that cellular distribution of upregulated ROS1 in OSCC may correlate with invasiveness. We found that ROS1 can localize to mitochondria in the highly invasive OSCC and identified a mitochondria-targe

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10

Santos, Herbert J., Yoko Chiba, Takashi Makiuchi, et al. "Import of Entamoeba histolytica Mitosomal ATP Sulfurylase Relies on Internal Targeting Sequences." Microorganisms 8, no. 8 (2020): 1229. http://dx.doi.org/10.3390/microorganisms8081229.

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Mitochondrial matrix proteins synthesized in the cytosol often contain amino (N)-terminal targeting sequences (NTSs), or alternately internal targeting sequences (ITSs), which enable them to be properly translocated to the organelle. Such sequences are also required for proteins targeted to mitochondrion-related organelles (MROs) that are present in a few species of anaerobic eukaryotes. Similar to other MROs, the mitosomes of the human intestinal parasite Entamoeba histolytica are highly degenerate, because a majority of the components involved in various processes occurring in the canonical

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11

DAILEY, Tamara A., John H. WOODRUFF, and Harry A. DAILEY. "Examination of mitochondrial protein targeting of haem synthetic enzymes: in vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase." Biochemical Journal 386, no. 2 (2005): 381–86. http://dx.doi.org/10.1042/bj20040570.

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The initial and the terminal three enzymes of the mammalian haem biosynthetic pathway are nuclear encoded, cytoplasmically synthesized and post-translationally translocated into the mitochondrion. The first enzyme, ALAS (5-aminolaevulinate synthase), occurs as an isoenzyme encoded on different chromosomes and is synthesized either as a housekeeping protein (ALAS-1) in all non-erythroid cell types, or only in differentiating erythroid precursor cells (ALAS-2). Both ALAS proteins possess mitochondrial targeting sequences that have putative haem-binding motifs. In the present study, evidence is p

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Addya, Sankar, Hindupur K. Anandatheerthavarada, Gopa Biswas, Shripad V. Bhagwat, Jayati Mullick, and Narayan G. Avadhani. "Targeting of NH2-terminal–processed Microsomal Protein to Mitochondria: A Novel Pathway for the Biogenesis of Hepatic Mitochondrial P450MT2." Journal of Cell Biology 139, no. 3 (1997): 589–99. http://dx.doi.org/10.1083/jcb.139.3.589.

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Cytochrome P4501A1 is a hepatic, microsomal membrane–bound enzyme that is highly induced by various xenobiotic agents. Two NH2-terminal truncated forms of this P450, termed P450MT2a and MT2b, are also found localized in mitochondria from β-naphthoflavone–induced livers. In this paper, we demonstrate that P4501A1 has a chimeric NH2-terminal signal that facilitates the targeting of the protein to both the ER and mitochondria. The NH2-terminal 30–amino acid stretch of P4501A1 is thought to provide signals for ER membrane insertion and also stop transfer. The present study provides evidence that a

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Wattenberg, Binks W., Denise Clark, and Stephanie Brock. "An Artificial Mitochondrial Tail Signal/Anchor Sequence Confirms a Requirement for Moderate Hydrophobicity for Targeting." Bioscience Reports 27, no. 6 (2007): 385–401. http://dx.doi.org/10.1007/s10540-007-9061-0.

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Tail-anchored proteins are a group of membrane proteins oriented with their amino terminus in the cytoplasm and their carboxy terminus embedded in intracellular membranes. This group includes the apoptosis-mediating proteins of the Bcl-2 family as well as the vesicle targeting proteins of the SNARE group, among others. A stretch of hydrophobic amino acids at the extreme carboxy terminus of these proteins serves both as a membrane anchor and as a targeting signal. Tail-anchored proteins are differentially targeted to either the endoplasmic reticulum or the mitochondrial outer membrane and the m

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Boguta, M., L. A. Hunter, W. C. Shen, E. C. Gillman, N. C. Martin, and A. K. Hopper. "Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol." Molecular and Cellular Biology 14, no. 4 (1994): 2298–306. http://dx.doi.org/10.1128/mcb.14.4.2298-2306.1994.

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MOD5, a gene responsible for the modification of A37 to isopentenyl A37 of both cytosolic and mitochondrial tRNAs, encodes two isozymes. Initiation of translation at the first AUG of the MOD5 open reading frame generates delta 2-isopentenyl pyrophosphate:tRNA isopentanyl transferase I (IPPT-I), which is located predominantly, but not exclusively, in the mitochondria. Initiation of translation at a second AUG generates IPPT-II, which modifies cytoplasmic tRNA. IPPT-II is unable to target to mitochondria. The N-terminal sequence present in IPPT-I and absent in IPPT-II is therefore necessary for

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Boguta, M., L. A. Hunter, W. C. Shen, E. C. Gillman, N. C. Martin, and A. K. Hopper. "Subcellular locations of MOD5 proteins: mapping of sequences sufficient for targeting to mitochondria and demonstration that mitochondrial and nuclear isoforms commingle in the cytosol." Molecular and Cellular Biology 14, no. 4 (1994): 2298–306. http://dx.doi.org/10.1128/mcb.14.4.2298.

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MOD5, a gene responsible for the modification of A37 to isopentenyl A37 of both cytosolic and mitochondrial tRNAs, encodes two isozymes. Initiation of translation at the first AUG of the MOD5 open reading frame generates delta 2-isopentenyl pyrophosphate:tRNA isopentanyl transferase I (IPPT-I), which is located predominantly, but not exclusively, in the mitochondria. Initiation of translation at a second AUG generates IPPT-II, which modifies cytoplasmic tRNA. IPPT-II is unable to target to mitochondria. The N-terminal sequence present in IPPT-I and absent in IPPT-II is therefore necessary for

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16

Emr, S. D., A. Vassarotti, J. Garrett, B. L. Geller, M. Takeda, and M. G. Douglas. "The amino terminus of the yeast F1-ATPase beta-subunit precursor functions as a mitochondrial import signal." Journal of Cell Biology 102, no. 2 (1986): 523–33. http://dx.doi.org/10.1083/jcb.102.2.523.

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The ATP2 gene of Saccharomyces cerevisiae codes for the cytoplasmically synthesized beta-subunit protein of the mitochondrial F1-ATPase. To define the amino acid sequence determinants necessary for the in vivo targeting and import of this protein into mitochondria, we have constructed gene fusions between the ATP2 gene and either the Escherichia coli lacZ gene or the S. cerevisiae SUC2 gene (which codes for invertase). The ATP2-lacZ and ATP2-SUC2 gene fusions code for hybrid proteins that are efficiently targeted to yeast mitochondria in vivo. The mitochondrially associated hybrid proteins fra

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Gibbs, James S., Daniela Malide, Felicita Hornung, Jack R. Bennink, and Jonathan W. Yewdell. "The Influenza A Virus PB1-F2 Protein Targets the Inner Mitochondrial Membrane via a Predicted Basic Amphipathic Helix That Disrupts Mitochondrial Function." Journal of Virology 77, no. 13 (2003): 7214–24. http://dx.doi.org/10.1128/jvi.77.13.7214-7224.2003.

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ABSTRACT The 11th influenza A virus gene product is an 87-amino-acid protein provisionally named PB1-F2 (because it is encoded by an open reading frame overlapping the PB1 open reading frame). A significant fraction of PB1-F2 localizes to the inner mitochondrial membrane in influenza A virus-infected cells. PB1-F2 appears to enhance virus-induced cell death in a cell type-dependent manner. For the present communication we have identified and characterized a region near the COOH terminus of PB1-F2 that is necessary and sufficient for its inner mitochondrial membrane localization, as determined

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Spatola Rossi, Tatiana, and Verena Kriechbaumer. "An Interplay between Mitochondrial and ER Targeting of a Bacterial Signal Peptide in Plants." Plants 12, no. 3 (2023): 617. http://dx.doi.org/10.3390/plants12030617.

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Protein targeting is essential in eukaryotic cells to maintain cell function and organelle identity. Signal peptides are a major type of targeting sequences containing a tripartite structure, which is conserved across all domains in life. They are frequently included in recombinant protein design in plants to increase yields by directing them to the endoplasmic reticulum (ER) or apoplast. The processing of bacterial signal peptides by plant cells is not well understood but could aid in the design of efficient heterologous expression systems. Here we analysed the signal peptide of the enzyme Pm

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19

Rosenkrantz, M., T. Alam, K. S. Kim, B. J. Clark, P. A. Srere, and L. P. Guarente. "Mitochondrial and nonmitochondrial citrate synthases in Saccharomyces cerevisiae are encoded by distinct homologous genes." Molecular and Cellular Biology 6, no. 12 (1986): 4509–15. http://dx.doi.org/10.1128/mcb.6.12.4509-4515.1986.

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Saccharomyces cerevisiae contains two genes, CIT1 and CIT2, encoding functional citrate synthase (K.-S. Kim, M. S. Rosenkrantz, and L. Guarente, Mol. Cell. Biol. 6:1936-1942, 1986). We show here that CIT2 encodes a nonmitochondrial form of citrate synthase. The DNA sequence of CIT2 presented provides a possible explanation for why the CIT2 product, unlike the CIT1 product, fails to be imported into mitochondria. While the products of these two genes are highly homologous, they diverge strikingly at their amino termini. The amino terminus of the CIT1 primary translation product extends 39 resid

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Rosenkrantz, M., T. Alam, K. S. Kim, B. J. Clark, P. A. Srere, and L. P. Guarente. "Mitochondrial and nonmitochondrial citrate synthases in Saccharomyces cerevisiae are encoded by distinct homologous genes." Molecular and Cellular Biology 6, no. 12 (1986): 4509–15. http://dx.doi.org/10.1128/mcb.6.12.4509.

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Saccharomyces cerevisiae contains two genes, CIT1 and CIT2, encoding functional citrate synthase (K.-S. Kim, M. S. Rosenkrantz, and L. Guarente, Mol. Cell. Biol. 6:1936-1942, 1986). We show here that CIT2 encodes a nonmitochondrial form of citrate synthase. The DNA sequence of CIT2 presented provides a possible explanation for why the CIT2 product, unlike the CIT1 product, fails to be imported into mitochondria. While the products of these two genes are highly homologous, they diverge strikingly at their amino termini. The amino terminus of the CIT1 primary translation product extends 39 resid

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Cotteret, Sophie, and Jonathan Chernoff. "Nucleocytoplasmic Shuttling of Pak5 Regulates Its Antiapoptotic Properties." Molecular and Cellular Biology 26, no. 8 (2006): 3215–30. http://dx.doi.org/10.1128/mcb.26.8.3215-3230.2006.

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ABSTRACT p21-activated kinase 5 (Pak5) is an effector for the small GTPase Cdc42, known to activate cell survival signaling pathways. Previously, we have shown that Pak5 localizes primarily to mitochondria. To study the relationship between Pak5 localization and its effects on apoptosis, we identified three N-terminal regions that regulate the localization of this kinase: a mitochondrial targeting sequence, a nuclear export sequence, and a nuclear localization sequence. When the first two sequences are deleted, Pak5 is retained in the nucleus and no longer protects cells from apoptosis. Moreov

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Pelloquin, L., P. Belenguer, Y. Menon, N. Gas, and B. Ducommun. "Fission yeast Msp1 is a mitochondrial dynamin-related protein." Journal of Cell Science 112, no. 22 (1999): 4151–61. http://dx.doi.org/10.1242/jcs.112.22.4151.

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We recently identified Msp1p, a fission yeast Schizosaccharomyces pombe dynamin-related protein, which is essential for the maintenance of mitochondrial DNA. The Msp1p sequence displays typical features of a mitochondrial protein. Here we report in vitro and in vivo data that validate that prediction. We demonstrate that the targeting sequence of Msp1p is processed by recombinant mitochondrial processing peptidase and that Msp1p is imported into S. pombe mitochondria in vitro in the presence of cellular extracts. We show that the first 109 residues of Msp1p encompass a functional peptide signa

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Yamaguchi, Kazunori, Keiko Hata, Koichi Koseki, et al. "Evidence for mitochondrial localization of a novel human sialidase (NEU4)." Biochemical Journal 390, no. 1 (2005): 85–93. http://dx.doi.org/10.1042/bj20050017.

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Based on the human cDNA sequence predicted to represent the NEU4 sialidase gene in public databases, a cDNA covering the entire coding sequence was isolated from human brain and expressed in mammalian cells. The cDNA encodes two isoforms: one possessing an N-terminal 12-amino-acid sequence that is predicted to be a mitochondrial targeting sequence, and the other lacking these amino acids. Expression of the isoforms is tissuespecific, as assessed by reverse transcription–PCR. Brain, muscle and kidney contained both isoforms; liver showed the highest expression, and the short form was predominan

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Haucke, V., C. S. Ocana, A. Hönlinger, K. Tokatlidis, N. Pfanner, and G. Schatz. "Analysis of the sorting signals directing NADH-cytochrome b5 reductase to two locations within yeast mitochondria." Molecular and Cellular Biology 17, no. 7 (1997): 4024–32. http://dx.doi.org/10.1128/mcb.17.7.4024.

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Mitochondrial NADH-cytochrome b5 reductase (Mcr1p) is encoded by a single nuclear gene and imported into two different submitochondrial compartments: the outer membrane and the intermembrane space. We now show that the amino-terminal 47 amino acids suffice to target the Mcr1 protein to both destinations. The first 12 residues of this sequence function as a weak matrix-targeting signal; the remaining residues are mostly hydrophobic and serve as an intramitochondrial sorting signal for the outer membrane and the intermembrane space. A double point mutation within the hydrophobic region of the ta

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Villa-Abrille, María C., Eugenio Cingolani, Horacio E. Cingolani, and Bernardo V. Alvarez. "Silencing of cardiac mitochondrial NHE1 prevents mitochondrial permeability transition pore opening." American Journal of Physiology-Heart and Circulatory Physiology 300, no. 4 (2011): H1237—H1251. http://dx.doi.org/10.1152/ajpheart.00840.2010.

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Inhibition of Na+/H+ exchanger 1 (NHE1) reduces cardiac ischemia-reperfusion (I/R) injury and also cardiac hypertrophy and failure. Although the mechanisms underlying these NHE1-mediated effects suggest delay of mitochondrial permeability transition pore (MPTP) opening, and reduction of mitochondrial-derived superoxide production, the possibility of NHE1 blockade targeting mitochondria has been incompletely explored. A short-hairpin RNA sequence mediating specific knock down of NHE1 expression was incorporated into a lentiviral vector (shRNA-NHE1) and transduced in the rat myocardium. NHE1 exp

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Adrian, G. S., M. T. McCammon, D. L. Montgomery, and M. G. Douglas. "Sequences required for delivery and localization of the ADP/ATP translocator to the mitochondrial inner membrane." Molecular and Cellular Biology 6, no. 2 (1986): 626–34. http://dx.doi.org/10.1128/mcb.6.2.626-634.1986.

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The ADP/ATP translocator, a transmembrane protein of the mitochondrial inner membrane, is coded in Saccharomyces cerevisiae by the nuclear gene PET9. DNA sequence analysis of the PET9 gene showed that it encoded a protein of 309 amino acids which exhibited a high degree of homology with mitochondrial translocator proteins from other sources. This mitochondrial precursor, in contrast to many others, does not contain a transient presequence which has been shown to direct the posttranslational localization of proteins in the organelle. Gene fusions between the PET9 gene and the gene encoding beta

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Adrian, G. S., M. T. McCammon, D. L. Montgomery, and M. G. Douglas. "Sequences required for delivery and localization of the ADP/ATP translocator to the mitochondrial inner membrane." Molecular and Cellular Biology 6, no. 2 (1986): 626–34. http://dx.doi.org/10.1128/mcb.6.2.626.

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The ADP/ATP translocator, a transmembrane protein of the mitochondrial inner membrane, is coded in Saccharomyces cerevisiae by the nuclear gene PET9. DNA sequence analysis of the PET9 gene showed that it encoded a protein of 309 amino acids which exhibited a high degree of homology with mitochondrial translocator proteins from other sources. This mitochondrial precursor, in contrast to many others, does not contain a transient presequence which has been shown to direct the posttranslational localization of proteins in the organelle. Gene fusions between the PET9 gene and the gene encoding beta

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Geissler, Andreas, Thomas Krimmer, Ulf Bömer, Bernard Guiard, Joachim Rassow, and Nikolaus Pfanner. "Membrane Potential-Driven Protein Import into Mitochondria." Molecular Biology of the Cell 11, no. 11 (2000): 3977–91. http://dx.doi.org/10.1091/mbc.11.11.3977.

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The transport of preproteins into or across the mitochondrial inner membrane requires the membrane potential Δψ across this membrane. Two roles of Δψ in the import of cleavable preproteins have been described: an electrophoretic effect on the positively charged matrix-targeting sequences and the activation of the translocase subunit Tim23. We report the unexpected finding that deletion of a segment within the sorting sequence of cytochromeb 2 , which is located behind the matrix-targeting sequence, strongly influenced the Δψ-dependence of import. The differential Δψ-dependence was independent

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MORGAN, Rhian R., Rachel ERRINGTON, and George H. ELDER. "Identification of sequences required for the import of human protoporphyrinogen oxidase to mitochondria." Biochemical Journal 377, no. 2 (2004): 281–87. http://dx.doi.org/10.1042/bj20030978.

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Protoporphyrinogen oxidase (PPOX; EC 1.3.3.4), the penultimate enzyme of haem biosynthesis, is a nucleus-encoded flavoprotein strongly associated with the outer surface of the inner mitochondrial membrane. It is attached to this membrane by an unknown mechanism that appears not to involve a membrane-spanning domain. The pathway for its import to mitochondria and insertion into the inner membrane has not been established. We have fused human PPOXs containing N-terminal deletions, C-terminal deletions or missense mutations to yellow fluorescent protein (YFP) and have used these constructs to inv

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BIRDSEY, Graeme M., and Christopher J. DANPURE. "Evolution of alanine:glyoxylate aminotransferase intracellular targeting: structural and functional analysis of the guinea pig gene." Biochemical Journal 331, no. 1 (1998): 49–60. http://dx.doi.org/10.1042/bj3310049.

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The distribution of alanine:glyoxylate aminotransferase 1 (AGT) within liver cells has changed many times during mammalian evolution. Depending on the particular species, AGT can be found in mitochondria or peroxisomes, or mitochondria and peroxisomes. In some cases significant cytosolic AGT is also present. In the livers of most rodents, AGT has what is thought to be the more ‘ancestral ’ distribution (i.e. mitochondrial and peroxisomal). However, AGT is distributed very differently in the guinea pig, being peroxisomal and cytosolic. In this study, we have attempted to determine the molecular

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Grant, Rhys, Ahmed Abdelbaki, Alessia Bertoldi, et al. "Constitutive regulation of mitochondrial morphology by Aurora A kinase depends on a predicted cryptic targeting sequence at the N-terminus." Open Biology 8, no. 6 (2018): 170272. http://dx.doi.org/10.1098/rsob.170272.

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Aurora A kinase (AURKA) is a major regulator of mitosis and an important driver of cancer progression. The roles of AURKA outside of mitosis, and how these might contribute to cancer progression, are not well understood. Here, we show that a fraction of cytoplasmic AURKA is associated with mitochondria, co-fractionating in cell extracts and interacting with mitochondrial proteins by reciprocal co-immunoprecipitation. We have also found that the dynamics of the mitochondrial network are sensitive to AURKA inhibition, depletion or overexpression. This can account for the different mitochondrial

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Dyall, Sabrina D., Carla M. Koehler, Maria G. Delgadillo-Correa, et al. "Presence of a Member of the Mitochondrial Carrier Family in Hydrogenosomes: Conservation of Membrane-Targeting Pathways between Hydrogenosomes and Mitochondria." Molecular and Cellular Biology 20, no. 7 (2000): 2488–97. http://dx.doi.org/10.1128/mcb.20.7.2488-2497.2000.

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ABSTRACT A number of microaerophilic eukaryotes lack mitochondria but possess another organelle involved in energy metabolism, the hydrogenosome. Limited phylogenetic analyses of nuclear genes support a common origin for these two organelles. We have identified a protein of the mitochondrial carrier family in the hydrogenosome ofTrichomonas vaginalis and have shown that this protein, Hmp31, is phylogenetically related to the mitochondrial ADP-ATP carrier (AAC). We demonstrate that the hydrogenosomal AAC can be targeted to the inner membrane of mitochondria isolated from Saccharomyces cerevisia

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Shteinfer-Kuzmine, Anna, Shirel Argueti-Ostrovsky, Marcel F. Leyton-Jaimes, et al. "Targeting the Mitochondrial Protein VDAC1 as a Potential Therapeutic Strategy in ALS." International Journal of Molecular Sciences 23, no. 17 (2022): 9946. http://dx.doi.org/10.3390/ijms23179946.

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Impaired mitochondrial function has been proposed as a causative factor in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), caused by motor neuron degeneration. Mutations in superoxide dismutase (SOD1) cause ALS and SOD1 mutants were shown to interact with the voltage-dependent anion channel 1 (VDAC1), affecting its normal function. VDAC1 is a multi-functional channel located at the outer mitochondrial membrane that serves as a mitochondrial gatekeeper controlling metabolic and energetic crosstalk between mitochondria and the rest of the cell and it is a key player in

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Eliyahu, Erez, Lilach Pnueli, Daniel Melamed, et al. "Tom20 Mediates Localization of mRNAs to Mitochondria in a Translation-Dependent Manner." Molecular and Cellular Biology 30, no. 1 (2009): 284–94. http://dx.doi.org/10.1128/mcb.00651-09.

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ABSTRACT mRNAs encoding mitochondrial proteins are enriched in the vicinity of mitochondria, presumably to facilitate protein transport. A possible mechanism for enrichment may involve interaction of the translocase of the mitochondrial outer membrane (TOM) complex with the precursor protein while it is translated, thereby leading to association of polysomal mRNAs with mitochondria. To test this hypothesis, we isolated mitochondrial fractions from yeast cells lacking the major import receptor, Tom20, and compared their mRNA repertoire to that of wild-type cells by DNA microarrays. Most mRNAs e

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Medd, S. M., J. E. Walker, and R. D. Jolly. "Characterization of the expressed genes for subunit c of mitochondrial ATP synthase in sheep with ceroid lipofuscinosis." Biochemical Journal 293, no. 1 (1993): 65–73. http://dx.doi.org/10.1042/bj2930065.

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The human and bovine genomes each contain two expressed nuclear genes, called P1 and P2, for subunit c, a hydrophobic subunit of the membrane sector, Fo, of mitochondrial ATP synthase. Both P1 and P2 encode the same mature protein, but the associated mitochondrial import sequences are different. In sheep with the neurodegenerative disease ceroid lipofuscinosis, and also in humans with Batten's disease, unmodified subunit c accumulates in lysosome-derived organelles in a variety of tissues. However, the sequences of cDNAs for P1 and P2 from sheep with ceroid lipofuscinosis were identical to tho

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Choy, Francis, Lisa Sharp, and Derek A. Applegarth. "Glycine cleavage enzyme complex: Rabbit H-protein cDNA sequence analysis and comparison to human, cow, and chicken." Biochemistry and Cell Biology 78, no. 6 (2000): 725–30. http://dx.doi.org/10.1139/o00-081.

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The H-protein is one of the four essential components (H-, L-, P-, and T-proteins) of the mammalian glycine cleavage enzyme complex, the major degradative pathway of glycine. We have isolated the full-length cDNA of the H-protein gene from the rabbit (Oryctolagus caniculus) by reverse transcription of liver poly-A mRNA and determined its nucleotide sequence (GenBank Acc. No. BankIt 318281 AF 231451). Similar to that in human, the rabbit H-protein gene possesses a 519-bp open reading frame that translates a 173-amino-acid (aa) protein. This reading frame is comprised of a 48-aa mitochondrial ta

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Sedman, Tiina, Silja Kuusk, Sirje Kivi, and Juhan Sedman. "A DNA Helicase Required for Maintenance of the Functional Mitochondrial Genome in Saccharomyces cerevisiae." Molecular and Cellular Biology 20, no. 5 (2000): 1816–24. http://dx.doi.org/10.1128/mcb.20.5.1816-1824.2000.

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ABSTRACT A novel DNA helicase, a homolog of several prokaryotic helicases, including Escherichia coli Rep and UvrD proteins, is encoded by the Saccharomyces cerevisiae nuclear genome open reading frame YOL095c on the chromosome XV. Our data demonstrate that the helicase is localized in the yeast mitochondria and is loosely associated with the mitochondrial inner membrane during biochemical fractionation. The sequence of the C-terminal end of the 80-kDa helicase protein is similar to a typical N-terminal mitochondrial targeting signal; deletions and point mutations in this region abolish transp

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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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Tamura, Toshiya, Harilyn W. McMicken, Charles V. Smith, and Thomas N. Hansen. "Mitochondrial Targeting of Glutathione Reductase Requires a Leader Sequence." Biochemical and Biophysical Research Communications 222, no. 3 (1996): 659–63. http://dx.doi.org/10.1006/bbrc.1996.0800.

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Singh, K. K., G. M. Small, and A. S. Lewin. "Alternative topogenic signals in peroxisomal citrate synthase of Saccharomyces cerevisiae." Molecular and Cellular Biology 12, no. 12 (1992): 5593–99. http://dx.doi.org/10.1128/mcb.12.12.5593-5599.1992.

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The tripeptide serine-lysine-leucine (SKL) occurs at the carboxyl terminus of many peroxisomal proteins and serves as a peroxisomal targeting signal. Saccharomyces cerevisiae has two isozymes of citrate synthase. The peroxisomal form, encoded by CIT2, terminates in SKL, while the mitochondrial form, encoded by CIT1, begins with an amino-terminal mitochondrial signal sequence and ends in SKN. We analyzed the importance of SKL as a topogenic signal for citrate synthase, using oleate to induce peroxisomes and density gradients to fractionate organelles. Our experiments revealed that SKL was neces

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Singh, K. K., G. M. Small, and A. S. Lewin. "Alternative topogenic signals in peroxisomal citrate synthase of Saccharomyces cerevisiae." Molecular and Cellular Biology 12, no. 12 (1992): 5593–99. http://dx.doi.org/10.1128/mcb.12.12.5593.

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The tripeptide serine-lysine-leucine (SKL) occurs at the carboxyl terminus of many peroxisomal proteins and serves as a peroxisomal targeting signal. Saccharomyces cerevisiae has two isozymes of citrate synthase. The peroxisomal form, encoded by CIT2, terminates in SKL, while the mitochondrial form, encoded by CIT1, begins with an amino-terminal mitochondrial signal sequence and ends in SKN. We analyzed the importance of SKL as a topogenic signal for citrate synthase, using oleate to induce peroxisomes and density gradients to fractionate organelles. Our experiments revealed that SKL was neces

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Sim, Juhyun, Jiyoung Park, Hyun Ae Woo, and Sue Goo Rhee. "Maturation of Mitochondrially Targeted Prx V Involves a Second Cleavage by Mitochondrial Intermediate Peptidase That Is Sensitive to Inhibition by H2O2." Antioxidants 10, no. 3 (2021): 346. http://dx.doi.org/10.3390/antiox10030346.

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Prx V mRNA contains two in-frame AUG codons, producing a long (L-Prx V) and short form of Prx V (S-Prx V), and mouse L-Prx V is expressed as a precursor protein containing a 49-amino acid N-terminal mitochondria targeting sequence. Here, we show that the N-terminal 41-residue sequence of L-Prx V is cleaved by mitochondrial processing peptidase (MPP) in the mitochondrial matrix to produce an intermediate Prx V (I-Prx V) with a destabilizing phenylalanine at its N-terminus, and further, that the next 8-residue sequence is cleaved by mitochondrial intermediate peptidase (MIP) to convert I-Prx V t

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Arrington, David D., Terry R. Van Vleet, and Rick G. Schnellmann. "Calpain 10: a mitochondrial calpain and its role in calcium-induced mitochondrial dysfunction." American Journal of Physiology-Cell Physiology 291, no. 6 (2006): C1159—C1171. http://dx.doi.org/10.1152/ajpcell.00207.2006.

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Calpains, Ca2+-activated cysteine proteases, are cytosolic enzymes implicated in numerous cellular functions and pathologies. We identified a mitochondrial Ca2+-inducible protease that hydrolyzed a calpain substrate (SLLVY-AMC) and was inhibited by active site-directed calpain inhibitors as calpain 10, an atypical calpain lacking domain IV. Immunoblot analysis and activity assays revealed calpain 10 in the mitochondrial outer membrane, intermembrane space, inner membrane, and matrix fractions. Mitochondrial staining was observed when COOH-terminal green fluorescent protein-tagged calpain 10 wa

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Wang, Bing-Jun, Jing-Ming Xia, Qian Wang, Jiang-Long Yu, Zhiyin Song, and Huabin Zhao. "Diet and Adaptive Evolution of Alanine-Glyoxylate Aminotransferase Mitochondrial Targeting in Birds." Molecular Biology and Evolution 37, no. 3 (2019): 786–98. http://dx.doi.org/10.1093/molbev/msz266.

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Abstract Adaptations to different diets represent a hallmark of animal diversity. The diets of birds are highly variable, making them an excellent model system for studying adaptive evolution driven by dietary changes. To test whether molecular adaptations to diet have occurred during the evolution of birds, we examined a dietary enzyme alanine-glyoxylate aminotransferase (AGT), which tends to target mitochondria in carnivorous mammals, peroxisomes in herbivorous mammals, and both mitochondria and peroxisomes in omnivorous mammals. A total of 31 bird species were examined in this study, which

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PETROVA, Ventsislava Y., Diane DRESCHER, Anna V. KUJUMDZIEVA, and Manfred J. SCHMITT. "Dual targeting of yeast catalase A to peroxisomes and mitochondria." Biochemical Journal 380, no. 2 (2004): 393–400. http://dx.doi.org/10.1042/bj20040042.

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Yeast catalase A (Cta1p) contains two peroxisomal targeting signals (SSNSKF) localized at its C-terminus and within the N-terminal third of the protein, which both can target foreign proteins to peroxisomes. In the present study we demonstrated that Cta1p can also enter mitochondria, although the enzyme lacks a classical mitochondrial import sequence. Cta1p co-targeting was studied in a catalase A null mutant after growth on different carbon sources, and expression of a Cta1p–GFP (green fluorescent protein)-fusion protein or a Cta1p derivative containing either a c-Myc epitope (Cta1pmyc) or a

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WANG, Liya, and Staffan ERIKSSON. "Cloning and characterization of full-length mouse thymidine kinase 2: the N-terminal sequence directs import of the precursor protein into mitochondria." Biochemical Journal 351, no. 2 (2000): 469–76. http://dx.doi.org/10.1042/bj3510469.

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The subcellular localization of mitochondrial thymidine kinase (TK2) has been questioned, since no mitochondrial targeting sequences have been found in cloned human TK2 cDNAs. Here we report the cloning of mouse TK2 cDNA from a mouse full-length enriched cDNA library. The mouse TK2 cDNA codes for a protein of 270 amino acids, with a 40-amino-acid presumed N-terminal mitochondrial targeting signal. In vitro translation and translocation experiments with purified rat mitochondria confirmed that the N-terminal sequence directed import of the precursor TK2 into the mitochondrial matrix. A single 2

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Winter, Lilli, Christina Abrahamsberg, and Gerhard Wiche. "Plectin isoform 1b mediates mitochondrion–intermediate filament network linkage and controls organelle shape." Journal of Cell Biology 181, no. 6 (2008): 903–11. http://dx.doi.org/10.1083/jcb.200710151.

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Plectin is a versatile intermediate filament (IF)–bound cytolinker protein with a variety of differentially spliced isoforms accounting for its multiple functions. One particular isoform, plectin 1b (P1b), remains associated with mitochondria after biochemical fractionation of fibroblasts and cells expressing exogenous P1b. Here, we determined that P1b is inserted into the outer mitochondrial membrane with the exon 1b–encoded N-terminal sequence serving as a mitochondrial targeting and anchoring signal. To study P1b-related mitochondrial functions, we generated mice that selectively lack this

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Regev-Rudzki, N., O. Yogev, and O. Pines. "The mitochondrial targeting sequence tilts the balance between mitochondrial and cytosolic dual localization." Journal of Cell Science 121, no. 14 (2008): 2423–31. http://dx.doi.org/10.1242/jcs.029207.

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Xie, Bin, Hao Li, Qi Wang та ін. "Further Characterization of Human DNA Polymerase δ Interacting Protein 38". Journal of Biological Chemistry 280, № 23 (2005): 22375–84. http://dx.doi.org/10.1074/jbc.m414597200.

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Polymerase δ interacting protein 38 (PDIP38) was identified as a human DNA polymerase (pol) δ interacting protein through a direct interaction with p50, the small subunit of human pol δ. PDIP38 was also found to interact with proliferating cell nuclear antigen, which suggested that it might play a role in vivo in the processes of DNA replication and DNA repair in the nucleus. In order to characterize further this novel protein, we have examined its subcellular localization by the use of immunochemical and cellular fractionation techniques. These studies show that PDIP38 is a novel mitochondria

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Rose, A. M., P. B. Joyce, A. K. Hopper, and N. C. Martin. "Separate information required for nuclear and subnuclear localization: additional complexity in localizing an enzyme shared by mitochondria and nuclei." Molecular and Cellular Biology 12, no. 12 (1992): 5652–58. http://dx.doi.org/10.1128/mcb.12.12.5652-5658.1992.

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The TRM1 gene of Saccharomyces cerevisiae codes for a tRNA modification enzyme, N2,N2-dimethylguanosine-specific tRNA methyltransferase (m2(2)Gtase), shared by mitochondria and nuclei. Immunofluorescent staining at the nuclear periphery demonstrates that m2(2)Gtase localizes at or near the nuclear membrane. In determining sequences necessary for targeting the enzyme to nuclei and mitochondria, we found that information required to deliver the enzyme to the nucleus is not sufficient for its correct subnuclear localization. We also determined that mislocalizing the enzyme from the nucleus to the

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