Use the keywords feature with a free QxMD account.
Use Read by QxMD to access full text via your institution or open access sources.
Read also provides personalized recommendations to keep you up to date in your field.
Existing User
Sign InNew to Read
Sign Up#1
EDITORIAL
Marie Sissler, Fabien Darfeuille
No abstract text is available yet for this article.
February 2024: Biochimie
#2
JOURNAL ARTICLE
Andrea Accogli, Sheng-Jia Lin, Mariasavina Severino, Sung-Hoon Kim, Kevin Huang, Clarissa Rocca, Megan Landsverk, Maha Zaki, Almundher Al-Maawali, Varunvenkat M Srinivasan, Khalid Al-Thihli, G Bradly Schaefer, Monica Davis, Davide Tonduti, Chiara Doneda, Lara M Marten, Chris Mühlhausen, Maria Gomez, Eleonora Lamantea, Rafael Mena, Mathilde Nizon, Vincent Procaccio, Amber Begtrup, Aida Telegrafi, Hong Cui, Heidi L Schulz, Julia Mohr, Saskia Biskup, Mariana Amina Loos, Hilda Verónica Aráoz, Vincenzo Salpietro, Laura Davis Keppen, Manali Chitre, Cassidy Petree, Lucy Raymond, Julie Vogt, Lindsey B Swayer, Alice A Basinger, Signe Vandal Pedersen, Toni S Pearson, Dorothy K Grange, Lokesh Lingapp, Paige McDunnah, Rita Horvath, Benjamin Cogne, Bertrand Isidor, Andreas Hahn, Karen Gripp, Seyed Mehdi Jafarnejad, Elsebet Ostergaard, Carlos E Prada, Daniele Ghezzi, Vykuntaraju K Gowda, Robert W Taylor, Nahum Sonenberg, Henry Houlden, Marie Sissler, Gaurav K Varshney, Reza Maroofian
PURPOSE: Biallelic variants in TARS2, encoding the mitochondrial threonyl-tRNA-synthetase, have been reported in a small group of individuals displaying a neurodevelopmental phenotype, but with limited neuroradiological data and insufficient evidence for causality of the variants. METHODS: Exome or genome sequencing was carried out in 15 families. Clinical and neuroradiological evaluation was performed for all affected individuals, including review of 10 previously reported individuals...
July 13, 2023: Genetics in Medicine: Official Journal of the American College of Medical Genetics
#3
JOURNAL ARTICLE
Stéphanie Durrieu-Gaillard, Marie Sissler, Yaser Hashem
Kinetoplastids are unicellular eukaryotic parasites responsible for human pathologies such as Chagas disease, sleeping sickness or Leishmaniasis, caused by Trypanosoma cruzi, Trypanosoma brucei , and various Leishmania spp ., respectively. They harbor a single large mitochondrion that is essential for the survival of the parasite. Interestingly, most of the mitochondrial gene expression machineries and processes present significant differences from their nuclear and cytosolic counterparts. A striking example concerns their mitochondrial ribosomes, in charge of translating the few essential mRNAs encoded by mitochondrial genomes...
May 20, 2022: Bio-protocol
#4
JOURNAL ARTICLE
Marie Sissler
Aminoacyl-tRNA synthetases (aaRSs) are housekeeping enzymes that catalyze the specific attachment of amino acids onto cognate tRNAs, providing building blocks for ribosomal protein synthesis. Due to the absolutely essential nature of these enzymes, the possibility that mutations in their sequence could be the underlying cause of diseases had not been foreseen. However, we are learning of patients bearing familial mutations in aaRSs at an exponential rate. In a recent issue of JBC, Jin and coworkers analyzed the impact of two such mutations in the very special bi-functional human glutamyl-prolyl-tRNA synthetase (EPRS) and convincingly decode how these mutations elicit the integrated stress response...
November 6, 2021: Journal of Biological Chemistry
#5
JOURNAL ARTICLE
Marie Sissler, Yaser Hashem
No abstract text is available yet for this article.
August 2021: Nature Structural & Molecular Biology
#6
JOURNAL ARTICLE
Camila Parrot, Luc Moulinier, Florian Bernard, Yaser Hashem, Denis Dupuy, Marie Sissler
Trypanosomatid parasites are responsible for various human diseases, such as sleeping sickness, animal trypanosomiasis, or cutaneous and visceral leishmaniases. The few available drugs to fight related parasitic infections are often toxic and present poor efficiency and specificity, and thus finding new molecular targets is imperative. Aminoacyl-tRNA synthetases (aaRSs) are essential components of the translational machinery as they catalyze the specific attachment of an amino acid onto cognate tRNA(s). In trypanosomatids, one gene encodes both cytosolic- and mitochondrial-targeted aaRSs, with only three exceptions...
June 24, 2021: Journal of Biological Chemistry
#7
JOURNAL ARTICLE
Charles-Joris Roux, Giulia Barcia, Manuel Schiff, Marie Sissler, Raphaël Levy, Volodia Dangouloff-Ros, Isabelle Desguerre, Shimon Edvardson, Orli Elpeleg, Agnès Rötig, Arnold Munnich, Nathalie Boddaert
BACKGROUND AND PURPOSE: Mitochondrial aminoacyl-tRNA synthetases-encoded by ARS2 genes-are evolutionarily conserved enzymes that catalyse the attachment of amino acids to their cognate tRNAs, ensuring the accuracy of the mitochondrial translation process. ARS2 gene mutations are associated with a wide range of clinical presentations affecting the CNS. METHODS: Two senior neuroradiologists analysed brain MRI of 25 patients (age range: 3 d-25 yrs.; 11 males; 14 females) with biallelic pathogenic variants of 11 ARS2 genes in a retrospective study conducted between 2002 and 2019...
June 2021: Molecular Genetics and Metabolism
#8
JOURNAL ARTICLE
Heddy Soufari, Florent Waltz, Camila Parrot, Stéphanie Durrieu-Gaillard, Anthony Bochler, Lauriane Kuhn, Marie Sissler, Yaser Hashem
Kinetoplastids are unicellular eukaryotic parasites responsible for such human pathologies as Chagas disease, sleeping sickness, and leishmaniasis. They have a single large mitochondrion, essential for the parasite survival. In kinetoplastid mitochondria, most of the molecular machineries and gene expression processes have significantly diverged and specialized, with an extreme example being their mitochondrial ribosomes. These large complexes are in charge of translating the few essential mRNAs encoded by mitochondrial genomes...
November 9, 2020: Proceedings of the National Academy of Sciences of the United States of America
#9
REVIEW
Ligia Elena González-Serrano, Joseph W Chihade, Marie Sissler
Mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) are essential components of the mitochondrial translation machinery. The correlation of mitochondrial disorders with mutations in these enzymes has raised the interest of the scientific community over the past several years. Most surprising has been the wide-ranging presentation of clinical manifestations in patients with mt-aaRS mutations, despite the enzymes' common biochemical role. Even among cases where a common physiological system is affected, phenotypes, severity, and age of onset varies depending on which mt-aaRS is mutated...
January 15, 2019: Journal of Biological Chemistry
#10
JOURNAL ARTICLE
Maryam Hosseini, Poorna Roy, Marie Sissler, Craig L Zirbel, Eric Westhof, Neocles Leontis
Mammalian mitochondrial ribosomes evolved from bacterial ribosomes by reduction of ribosomal RNAs, increase of ribosomal protein content, and loss of guanine nucleotides. Guanine is the base most sensitive to oxidative damage. By systematically comparing high-quality, small ribosomal subunit RNA sequence alignments and solved 3D ribosome structures from mammalian mitochondria and bacteria, we deduce rules for folding a complex RNA with the remaining guanines shielded from solvent. Almost all conserved guanines in both bacterial and mammalian mitochondrial ribosomal RNA form guanine-specific, local or long-range, RNA-RNA or RNA-protein interactions...
November 16, 2018: Nucleic Acids Research
#11
JOURNAL ARTICLE
Ligia Elena González-Serrano, Loukmane Karim, Florian Pierre, Hagen Schwenzer, Agnès Rötig, Arnold Munnich, Marie Sissler
Human mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) are key enzymes in the mitochondrial protein translation system and catalyze the charging of amino acids on their cognate tRNAs. Mutations in their nuclear genes are associated with pathologies having a broad spectrum of clinical phenotypes, but with no clear molecular mechanism(s). For example, mutations in the nuclear genes encoding mt-AspRS and mt-ArgRS are correlated with the moderate neurodegenerative disorder leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL) and with the severe neurodevelopmental disorder pontocerebellar hypoplasia type 6 (PCH6), respectively...
August 31, 2018: Journal of Biological Chemistry
#12
REVIEW
Marie Sissler, Ligia Elena González-Serrano, Eric Westhof
Dysfunctions in mitochondria - the powerhouses of the cell - lead to several human pathologies. Because mitochondria integrate nuclear and mitochondrial genetic systems, they are richly intertwined with cellular activities. The nucleus-encoded mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) are key components of the mitochondrial translation apparatus. Mutations in these enzymes predominantly affect the central nervous system (CNS) but also target other organs. Comparable mutations in mt-aaRSs can lead to vastly diverse diseases, occurring at different stages in life, and within different tissues; this represents a confounding issue...
August 2017: Trends in Molecular Medicine
#13
JOURNAL ARTICLE
Luc Moulinier, Raymond Ripp, Gaston Castillo, Olivier Poch, Marie Sissler
Numerous mutations in each of the mitochondrial aminoacyl-tRNA synthetases (aaRSs) have been implicated in human diseases. The mutations are autosomal and recessive and lead mainly to neurological disorders, although with pleiotropic effects. The processes and interactions that drive the etiology of the disorders associated with mitochondrial aaRSs (mt-aaRSs) are far from understood. The complexity of the clinical, genetic, and structural data requires concerted, interdisciplinary efforts to understand the molecular biology of these disorders...
October 2017: Human Mutation
#14
JOURNAL ARTICLE
Christine Carapito, Lauriane Kuhn, Loukmane Karim, Magali Rompais, Thierry Rabilloud, Hagen Schwenzer, Marie Sissler
Human mitochondrial aminoacyl-tRNA synthetases (mt-aaRSs) are encoded in the nucleus, synthesized in the cytosol and targeted for importation into mitochondria by a N-terminal mitochondrial targeting sequence. This targeting sequence is presumably cleaved upon entry into the mitochondria, following a process still not fully deciphered in human, despite essential roles for the mitochondrial biogenesis. Maturation processes are indeed essential both for the release of a functional enzyme and to route correctly the protein within mitochondria...
January 15, 2017: Methods: a Companion to Methods in Enzymology
#15
COMMENT
Marie Sissler
No abstract text is available yet for this article.
September 2016: BioEssays: News and Reviews in Molecular, Cellular and Developmental Biology
#16
JOURNAL ARTICLE
Claude Sauter, Bernard Lorber, Agnès Gaudry, Loukmane Karim, Hagen Schwenzer, Frank Wien, Pierre Roblin, Catherine Florentz, Marie Sissler
Mutations in human mitochondrial aminoacyl-tRNA synthetases are associated with a variety of neurodegenerative disorders. The effects of these mutations on the structure and function of the enzymes remain to be established. Here, we investigate six mutants of the aspartyl-tRNA synthetase correlated with leukoencephalopathies. Our integrated strategy, combining an ensemble of biochemical and biophysical approaches, reveals that mutants are diversely affected with respect to their solubility in cellular extracts and stability in solution, but not in architecture...
2015: Scientific Reports
#17
JOURNAL ARTICLE
Mariella Simon, Elodie M Richard, Xinjian Wang, Mohsin Shahzad, Vincent H Huang, Tanveer A Qaiser, Prasanth Potluri, Sarah E Mahl, Antonio Davila, Sabiha Nazli, Saege Hancock, Margret Yu, Jay Gargus, Richard Chang, Nada Al-Sheqaih, William G Newman, Jose Abdenur, Arnold Starr, Rashmi Hegde, Thomas Dorn, Anke Busch, Eddie Park, Jie Wu, Hagen Schwenzer, Adrian Flierl, Catherine Florentz, Marie Sissler, Shaheen N Khan, Ronghua Li, Min-Xin Guan, Thomas B Friedman, Doris K Wu, Vincent Procaccio, Sheikh Riazuddin, Douglas C Wallace, Zubair M Ahmed, Taosheng Huang, Saima Riazuddin
Here we demonstrate association of variants in the mitochondrial asparaginyl-tRNA synthetase NARS2 with human hearing loss and Leigh syndrome. A homozygous missense mutation ([c.637G>T; p.Val213Phe]) is the underlying cause of nonsyndromic hearing loss (DFNB94) and compound heterozygous mutations ([c.969T>A; p.Tyr323*] + [c.1142A>G; p.Asn381Ser]) result in mitochondrial respiratory chain deficiency and Leigh syndrome, which is a neurodegenerative disease characterized by symmetric, bilateral lesions in the basal ganglia, thalamus, and brain stem...
March 2015: PLoS Genetics
#18
REVIEW
Jonathan L Huot, Ludovic Enkler, Cyrille Megel, Loukmane Karim, Daphné Laporte, Hubert D Becker, Anne-Marie Duchêne, Marie Sissler, Laurence Maréchal-Drouard
Mitochondria originate from the α-proteobacterial domain of life. Since this unique event occurred, mitochondrial genomes of protozoans, fungi, plants and metazoans have highly derived and diverged away from the common ancestral DNA. These resulting genomes highly differ from one another, but all present-day mitochondrial DNAs have a very reduced coding capacity. Strikingly however, ATP production coupled to electron transport and translation of mitochondrial proteins are the two common functions retained in all mitochondrial DNAs...
May 2014: Biochimie
#19
JOURNAL ARTICLE
Hagen Schwenzer, Gert C Scheper, Nathalie Zorn, Luc Moulinier, Agnès Gaudry, Emmanuelle Leize, Franck Martin, Catherine Florentz, Olivier Poch, Marie Sissler
Mammalian mitochondrial aminoacyl-tRNA synthetases are nuclear-encoded enzymes that are essential for mitochondrial protein synthesis. Due to an endosymbiotic origin of the mitochondria, many of them share structural domains with homologous bacterial enzymes of same specificity. This is also the case for human mitochondrial aspartyl-tRNA synthetase (AspRS) that shares the so-called bacterial insertion domain with bacterial homologs. The function of this domain in the mitochondrial proteins is unclear. Here, we show by bioinformatic analyses that the sequences coding for the bacterial insertion domain are less conserved in opisthokont and protist than in bacteria and viridiplantae...
May 2014: Biochimie
#20
REVIEW
Hagen Schwenzer, Joffrey Zoll, Catherine Florentz, Marie Sissler
Mitochondria are considered as the powerhouse of eukaryotic cells. They host several central metabolic processes fueling the oxidative phosphorylation pathway (OXPHOS) that produces ATP from its precursors ADP and inorganic phosphate Pi (PPi). The respiratory chain complexes responsible for the OXPHOS pathway are formed from complementary sets of protein subunits encoded by the nuclear genome and the mitochondrial genome, respectively. The expression of the mitochondrial genome requires a specific and fully active translation machinery from which aminoacyl-tRNA synthetases (aaRSs) are key actors...
2014: Topics in Current Chemistry
Make the most of Read.
Download the mobile app.
Download the mobile app.
Fetching more papers... 
