Waltz Florent, Salinas-Giegé Thalia, Englmeier Robert, Meichel Herrade, Soufari Heddy, Kuhn Lauriane, Pfeffer Stefan, Förster Friedrich, Engel Benjamin D., Giegé Philippe, Drouard Laurence, Hashem Yaser
How to build a ribosome from RNA fragments in Chlamydomonas mitochondria Article de journal
Dans: Nature Communications, vol. 12, no. 1, p. 7176, 2021, ISSN: 2041-1723.
Résumé | Liens | BibTeX | Étiquettes: Chlamydomonas reinhardtii, Cryoelectron Microscopy, mitochondria, Mitochondrial Proteins, Mitochondrial Ribosomes, PPSE, Ribosomal Proteins, ribosomes, RNA
@article{waltz_how_2021,
title = {How to build a ribosome from RNA fragments in Chlamydomonas mitochondria},
author = {Florent Waltz and Thalia Salinas-Giegé and Robert Englmeier and Herrade Meichel and Heddy Soufari and Lauriane Kuhn and Stefan Pfeffer and Friedrich Förster and Benjamin D. Engel and Philippe Giegé and Laurence Drouard and Yaser Hashem},
doi = {10.1038/s41467-021-27200-z},
issn = {2041-1723},
year = {2021},
date = {2021-12-01},
journal = {Nature Communications},
volume = {12},
number = {1},
pages = {7176},
abstract = {Mitochondria are the powerhouse of eukaryotic cells. They possess their own gene expression machineries where highly divergent and specialized ribosomes, named hereafter mitoribosomes, translate the few essential messenger RNAs still encoded by mitochondrial genomes. Here, we present a biochemical and structural characterization of the mitoribosome in the model green alga Chlamydomonas reinhardtii, as well as a functional study of some of its specific components. Single particle cryo-electron microscopy resolves how the Chlamydomonas mitoribosome is assembled from 13 rRNA fragments encoded by separate non-contiguous gene pieces. Additional proteins, mainly OPR, PPR and mTERF helical repeat proteins, are found in Chlamydomonas mitoribosome, revealing the structure of an OPR protein in complex with its RNA binding partner. Targeted amiRNA silencing indicates that these ribosomal proteins are required for mitoribosome integrity. Finally, we use cryo-electron tomography to show that Chlamydomonas mitoribosomes are attached to the inner mitochondrial membrane via two contact points mediated by Chlamydomonas-specific proteins. Our study expands our understanding of mitoribosome diversity and the various strategies these specialized molecular machines adopt for membrane tethering.},
keywords = {Chlamydomonas reinhardtii, Cryoelectron Microscopy, mitochondria, Mitochondrial Proteins, Mitochondrial Ribosomes, PPSE, Ribosomal Proteins, ribosomes, RNA},
pubstate = {published},
tppubtype = {article}
}
Weber-Lotfi Frédérique, Koulintchenko Milana V, Ibrahim Noha, Hammann Philippe, Mileshina Daria V, Konstantinov Yuri M, Dietrich André
Nucleic acid import into mitochondria: New insights into the translocation pathways. Article de journal
Dans: Biochimica et biophysica acta, vol. 1853, no. 12, p. 3165–3181, 2015, ISSN: 0006-3002 0006-3002, (Place: Netherlands).
Résumé | Liens | BibTeX | Étiquettes: Arabidopsis/metabolism, Biological Transport, Import factor, mitochondria, Mitochondria/*metabolism, Nucleic acid transport, Nucleic Acids/*metabolism, Permeability transition pore, Plant, PPSE, Saccharomyces cerevisiae/metabolism, Yeast
@article{weber-lotfi_nucleic_2015,
title = {Nucleic acid import into mitochondria: New insights into the translocation pathways.},
author = {Frédérique Weber-Lotfi and Milana V Koulintchenko and Noha Ibrahim and Philippe Hammann and Daria V Mileshina and Yuri M Konstantinov and André Dietrich},
doi = {10.1016/j.bbamcr.2015.09.011},
issn = {0006-3002 0006-3002},
year = {2015},
date = {2015-01-01},
journal = {Biochimica et biophysica acta},
volume = {1853},
number = {12},
pages = {3165--3181},
abstract = {Mitochondria have retained indispensable but limited genetic information and they import both proteins and nucleic acids from the cytosol. RNA import is essential for gene expression and regulation, whereas competence for DNA uptake is likely to contribute to organellar genome dynamics and evolution. Contrary to protein import mechanisms, the way nucleic acids cross the mitochondrial membranes remains poorly understood. Using proteomic, genetic and biochemical approaches with both plant and yeast organelles, we develop here a model for DNA uptake into mitochondria. The first step includes the voltage-dependent anion channel and an outer membrane-located precursor fraction of a protein normally located in the inner membrane. To proceed, the DNA is then potentially recruited in the intermembrane space by an accessible subunit of one of the respiratory chain complexes. Final translocation through the inner membrane remains the most versatile but points to the components considered to make the mitochondrial permeability transition pore. Depending on the size, DNA and RNA cooperate or compete for mitochondrial uptake, which shows that they share import mechanisms. On the other hand, our results imply the existence of more than one route for nucleic acid translocation into mitochondria.},
note = {Place: Netherlands},
keywords = {Arabidopsis/metabolism, Biological Transport, Import factor, mitochondria, Mitochondria/*metabolism, Nucleic acid transport, Nucleic Acids/*metabolism, Permeability transition pore, Plant, PPSE, Saccharomyces cerevisiae/metabolism, Yeast},
pubstate = {published},
tppubtype = {article}
}
Ali-Boucetta Hanene, Al-Jamal Khuloud T, Müller Karin H, Li Shouping, Porter Alexandra E, Eddaoudi Ayad, Prato Maurizio, Bianco Alberto, Kostarelos Kostas
Cellular uptake and cytotoxic impact of chemically functionalized and polymer-coated carbon nanotubes Article de journal
Dans: Small (Weinheim an Der Bergstrasse, Germany), vol. 7, no. 22, p. 3230–3238, 2011, ISSN: 1613-6829.
Résumé | Liens | BibTeX | Étiquettes: Annexin A5, carbon, Cell Death, Cell Line, Endocytosis, Flow Cytometry, Fluorescein-5-isothiocyanate, Humans, I2CT, L-Lactate Dehydrogenase, mitochondria, Nanotubes, Polymers, Propidium, Surface Properties, Team-Bianco, tumor, water
@article{ali-boucetta_cellular_2011,
title = {Cellular uptake and cytotoxic impact of chemically functionalized and polymer-coated carbon nanotubes},
author = {Hanene Ali-Boucetta and Khuloud T Al-Jamal and Karin H Müller and Shouping Li and Alexandra E Porter and Ayad Eddaoudi and Maurizio Prato and Alberto Bianco and Kostas Kostarelos},
doi = {10.1002/smll.201101004},
issn = {1613-6829},
year = {2011},
date = {2011-11-01},
journal = {Small (Weinheim an Der Bergstrasse, Germany)},
volume = {7},
number = {22},
pages = {3230--3238},
abstract = {The impact of nanomaterials such as carbon nanotubes on biological matter is a topic of increasing interest and concern and requires a multifaceted approach to be resolved. A modified cytotoxic (lactate dehydrogenase (LDH)) assay is developed in an attempt to offer a valid and reliable methodology for screening carbon nanotube toxicity in vitro. Two of the most widely used types of surface-modified multiwalled carbon nanotubes (MWNTs) are tested: ammonium-functionalized MWNTs (MWNT-NH3+ ) and Pluronic F127 coated MWNTs (MWNT:F127). Chemically functionalized MWNTs show significantly greater cellular uptake into lung epithelial A549 cells compared to the non-covalently Pluronic F127-coated MWNTs. In spite of this, MWNT:F127 exhibit enhanced cytotoxicity according to the modified LDH assay. The validity of the modified LDH assay is further validated by direct comparison with other less reliable or accurate cytotoxicity assays. These findings indicate the reliability of the modified LDH assay as a screening tool to assess carbon nanotube cytotoxicity and illustrate that high levels of carbon nanotube cellular internalization do not necessarily lead to adverse responses.},
keywords = {Annexin A5, carbon, Cell Death, Cell Line, Endocytosis, Flow Cytometry, Fluorescein-5-isothiocyanate, Humans, I2CT, L-Lactate Dehydrogenase, mitochondria, Nanotubes, Polymers, Propidium, Surface Properties, Team-Bianco, tumor, water},
pubstate = {published},
tppubtype = {article}
}
Bergdoll M., Remy M. H., Cagnon C., Masson J. M., Dumas P.
Proline-dependent oligomerization with arm exchange Article de journal
Dans: Structure, vol. 5, no. 3, p. 391-401, 1997, (0969-2126 Journal Article).
Résumé | BibTeX | Étiquettes: *Acetyltransferases, *Dimerization, *Protein, Acid, Alignment, Amino, Aminotransferases/chemistry, Animals, Aspartate, ATPase/chemistry, Bacterial, Binding, Cattle, Chickens, Comparative, Conformation, Data, Folding, Heart/enzymology, Human, mitochondria, Models, Molecular, Mutagenesis, Na(+)-K(+)-Exchanging, Pancreatic/chemistry, Plant, Proline/*physiology, Protein, Proteins/chemistry, Pyrophosphatases/chemistry, Ribonuclease, Sequence, Site-Directed, Structural, Study, Viral, Viruses/chemistry
@article{,
title = {Proline-dependent oligomerization with arm exchange},
author = { M. Bergdoll and M. H. Remy and C. Cagnon and J. M. Masson and P. Dumas},
year = {1997},
date = {1997-01-01},
journal = {Structure},
volume = {5},
number = {3},
pages = {391-401},
abstract = {BACKGROUND: Oligomerization is often necessary for protein activity or regulation and its efficiency is fundamental for the cell. The quaternary structure of a large number of oligomers consists of protomers tightly anchored to each other by exchanged arms or swapped domains. However, nothing is known about how the arms can be kept in a favourable conformation before such an oligomerization. RESULTS: Upon examination of such quaternary structures, we observe an extremely frequent occurrence of proline residues at the point where the arm leaves the protomer. Sequence alignment and site-directed mutagenesis confirm the importance of these prolines. The conservation of these residues at the hinge regions can be explained by the constraints that they impose on polypeptide conformation and dynamics: by rigidifying the mainchain, prolines favour extended conformations of arms thus favouring oligomerization, and may prevent interaction of the arms with the core of the protomer. CONCLUSIONS: Hinge prolines can be considered as 'quaternary structure helpers'. The presence of a proline should be considered when searching for a determinant of oligomerization with arm exchange and could be used to engineer synthetic oligomers or to displace a monomers to oligomers equilibrium by mutation of this proline residue.},
note = {0969-2126
Journal Article},
keywords = {*Acetyltransferases, *Dimerization, *Protein, Acid, Alignment, Amino, Aminotransferases/chemistry, Animals, Aspartate, ATPase/chemistry, Bacterial, Binding, Cattle, Chickens, Comparative, Conformation, Data, Folding, Heart/enzymology, Human, mitochondria, Models, Molecular, Mutagenesis, Na(+)-K(+)-Exchanging, Pancreatic/chemistry, Plant, Proline/*physiology, Protein, Proteins/chemistry, Pyrophosphatases/chemistry, Ribonuclease, Sequence, Site-Directed, Structural, Study, Viral, Viruses/chemistry},
pubstate = {published},
tppubtype = {article}
}
Zachary Daniel, Hoffmann Jules A
The haemocytes of Calliphora erythrocephala (Meig.) (Diptera) Article de journal
Dans: Z Zellforsch Mikrosk Anat, vol. 141, no. 1, p. 55–73, 1973, ISSN: 0340-0336.
BibTeX | Étiquettes: Animals, Cell Count, Cell Nucleus, Diptera, Electron, Endoplasmic Reticulum, Hemolymph, Hemostasis, hoffmann, Inclusion Bodies, Larva, Lipids, Lysosomes, M3i, Microscopy, mitochondria, Phase-Contrast, Pupa, Radiation Effects
@article{zachary_haemocytes_1973,
title = {The haemocytes of Calliphora erythrocephala (Meig.) (Diptera)},
author = {Daniel Zachary and Jules A Hoffmann},
issn = {0340-0336},
year = {1973},
date = {1973-07-01},
journal = {Z Zellforsch Mikrosk Anat},
volume = {141},
number = {1},
pages = {55--73},
keywords = {Animals, Cell Count, Cell Nucleus, Diptera, Electron, Endoplasmic Reticulum, Hemolymph, Hemostasis, hoffmann, Inclusion Bodies, Larva, Lipids, Lysosomes, M3i, Microscopy, mitochondria, Phase-Contrast, Pupa, Radiation Effects},
pubstate = {published},
tppubtype = {article}
}