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Article ; Online: Plunge Freezing: A Tool for the Ultrastructural and Immunolocalization Studies of Suspension Cells in Transmission Electron Microscopy.

Blancard, Corinne / Salin, Bénédicte

Journal of visualized experiments : JoVE

2017 , Issue 123

Abstract: Transmission Electron Microscopy (TEM) is an extraordinary tool for studying cell ultrastructure, in order to localize proteins and visualize macromolecular complexes at very high resolution. However, to get as close as possible to the native state, ... ...

Abstract	Transmission Electron Microscopy (TEM) is an extraordinary tool for studying cell ultrastructure, in order to localize proteins and visualize macromolecular complexes at very high resolution. However, to get as close as possible to the native state, perfect sample preservation is required. Conventional electron microscopy (EM) fixation with aldehydes, for instance, does not provide good ultrastructural preservation. The slow penetration of fixatives induces cell reorganization and loss of various cell components. Therefore, conventional EM fixation does not allow for an instantaneous stabilization and preservation of structures and antigenicity. The best choice for examining intracellular events is to use cryofixation followed by the freeze-substitution fixation method that keeps cells in their native state. High-pressure freezing/freeze-substitution, which preserves the integrity of cellular ultrastructure, is the most commonly used method, but requires expensive equipment. Here, an easy-to-use and low-cost freeze fixation method followed by freeze-substitution for suspension cell cultures is presented.
MeSH term(s)	Bacteria/ultrastructure ; Cryopreservation/methods ; Freezing ; Microscopy, Electron, Transmission/methods ; Pressure ; Yeasts/ultrastructure
Language	English
Publishing date	2017-05-05
Publishing country	United States
Document type	Journal Article ; Video-Audio Media
ISSN	1940-087X
ISSN (online)	1940-087X
DOI	10.3791/54874
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Article: Plunge freezing: a tool for the ultrastructural and immunolocalization studies of suspension cells in transmission electron microscopy

Blancard, Corinne / Salin, Bénédicte

Journal of visualized experiments. 2017 May 05, , no. 123

2017

Abstract	Transmission Electron Microscopy (TEM) is an extraordinary tool for studying cell ultrastructure, in order to localize proteins and visualize macromolecular complexes at very high resolution. However, to get as close as possible to the native state, perfect sample preservation is required. Conventional electron microscopy (EM) fixation with aldehydes, for instance, does not provide good ultrastructural preservation. The slow penetration of fixatives induces cell reorganization and loss of various cell components. Therefore, conventional EM fixation does not allow for an instantaneous stabilization and preservation of structures and antigenicity. The best choice for examining intracellular events is to use cryofixation followed by the freeze-substitution fixation method that keeps cells in their native state. High-pressure freezing/freeze-substitution, which preserves the integrity of cellular ultrastructure, is the most commonly used method, but requires expensive equipment. Here, an easy-to-use and low-cost freeze fixation method followed by freeze-substitution for suspension cell cultures is presented.
Keywords	aldehydes ; cryopreservation ; equipment ; freezing ; proteins ; transmission electron microscopy ; ultrastructure
Language	English
Dates of publication	2017-0505
Size	p. e54874.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/54874
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Article ; Online: TFK1, a basal body transition fibre protein that is essential for cytokinesis in Trypanosoma brucei.

Ramanantsalama, Miharisoa Rijatiana / Landrein, Nicolas / Casas, Elina / Salin, Bénédicte / Blancard, Corinne / Bonhivers, Mélanie / Robinson, Derrick R / Dacheux, Denis

Journal of cell science

2022 Volume 135, Issue 11

Abstract: In Trypanosoma brucei, transition fibres (TFs) form a nine-bladed pattern-like structure connecting the base of the flagellum to the flagellar pocket membrane. Despite the characterization of two TF proteins, CEP164C and T. brucei (Tb)RP2, little is ... ...

Abstract	In Trypanosoma brucei, transition fibres (TFs) form a nine-bladed pattern-like structure connecting the base of the flagellum to the flagellar pocket membrane. Despite the characterization of two TF proteins, CEP164C and T. brucei (Tb)RP2, little is known about the organization of these fibres. Here, we report the identification and characterization of the first kinetoplastid-specific TF protein, named TFK1 (Tb927.6.1180). Bioinformatics and functional domain analysis identified three distinct domains in TFK1 - an N-terminal domain of an unpredicted function, a coiled-coil domain involved in TFK1-TFK1 interaction and a C-terminal intrinsically disordered region potentially involved in protein interaction. Cellular immunolocalization showed that TFK1 is a newly identified basal body maturation marker. Furthermore, using ultrastructure expansion and immuno-electron microscopies we localized CEP164C and TbRP2 at the TF, and TFK1 on the distal appendage matrix of the TF. Importantly, RNAi-mediated knockdown of TFK1 in bloodstream form cells induced misplacement of basal bodies, a defect in the furrow or fold generation, and eventually cell death. We hypothesize that TFK1 is a basal body positioning-specific actor and a key regulator of cytokinesis in the bloodstream form Trypanosoma brucei.
MeSH term(s)	Basal Bodies/metabolism ; Cytokinesis ; Flagella/metabolism ; Protozoan Proteins/metabolism ; Trypanosoma brucei brucei/metabolism
Chemical Substances	Protozoan Proteins
Language	English
Publishing date	2022-06-09
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.259893
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Article ; Online: Partial Prion Cross-Seeding between Fungal and Mammalian Amyloid Signaling Motifs.

Bardin, Thierry / Daskalov, Asen / Barrouilhet, Sophie / Granger-Farbos, Alexandra / Salin, Bénédicte / Blancard, Corinne / Kauffmann, Brice / Saupe, Sven J / Coustou, Virginie

mBio

2021 Volume 12, Issue 1

Abstract: In filamentous fungi, NLR-based signalosomes activate downstream membrane-targeting cell death-inducing proteins by a mechanism of amyloid templating. In the ... ...

Abstract	In filamentous fungi, NLR-based signalosomes activate downstream membrane-targeting cell death-inducing proteins by a mechanism of amyloid templating. In the species
MeSH term(s)	Amyloid/genetics ; Amyloid/metabolism ; Animals ; Chaetomium/genetics ; Chaetomium/physiology ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Fungal Proteins/pharmacokinetics ; Humans ; Mammals/genetics ; Mammals/metabolism ; Multigene Family ; Nucleotide Motifs ; Podospora/genetics ; Podospora/physiology ; Prions/classification ; Prions/genetics ; Prions/physiology ; Signal Transduction/genetics ; Signal Transduction/physiology
Chemical Substances	Amyloid ; Fungal Proteins ; Prions
Language	English
Publishing date	2021-02-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.02782-20
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Article ; Online: The mitochondrial phosphatidylserine decarboxylase Psd1 is involved in nitrogen starvation-induced mitophagy in yeast.

Vigié, Pierre / Cougouilles, Elodie / Bhatia-Kiššová, Ingrid / Salin, Bénédicte / Blancard, Corinne / Camougrand, Nadine

Journal of cell science

2019 Volume 132, Issue 1

Abstract: Mitophagy, the selective degradation of mitochondria by autophagy, is a central process that is essential for the maintenance of cell homeostasis. It is implicated in the clearance of superfluous or damaged mitochondria and requires specific proteins and ...

Abstract	Mitophagy, the selective degradation of mitochondria by autophagy, is a central process that is essential for the maintenance of cell homeostasis. It is implicated in the clearance of superfluous or damaged mitochondria and requires specific proteins and regulators to perform. In yeast, Atg32, an outer mitochondrial membrane protein, interacts with the ubiquitin-like Atg8 protein, promoting the recruitment of mitochondria to the phagophore and their sequestration within autophagosomes. Atg8 is anchored to the phagophore and autophagosome membranes thanks to a phosphatidylethanolamine tail. In
MeSH term(s)	Autophagy ; Autophagy-Related Protein 8 Family/genetics ; Autophagy-Related Protein 8 Family/metabolism ; Autophagy-Related Proteins/genetics ; Autophagy-Related Proteins/metabolism ; Carboxy-Lyases/genetics ; Carboxy-Lyases/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitophagy ; Nitrogen/deficiency ; Phosphatidylethanolamines/metabolism ; Receptors, Cytoplasmic and Nuclear/genetics ; Receptors, Cytoplasmic and Nuclear/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Starvation ; Vacuoles/metabolism
Chemical Substances	ATG8 protein, S cerevisiae ; Atg32 protein, S cerevisiae ; Autophagy-Related Protein 8 Family ; Autophagy-Related Proteins ; Mitochondrial Proteins ; Phosphatidylethanolamines ; Receptors, Cytoplasmic and Nuclear ; Saccharomyces cerevisiae Proteins ; phosphatidylethanolamine (39382-08-6) ; Carboxy-Lyases (EC 4.1.1.-) ; Psd1 protein, S cerevisiae (EC 4.1.1.-) ; Nitrogen (N762921K75)
Language	English
Publishing date	2019-01-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.221655
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Article ; Online: Identification of new components of the basal pole of <i>Toxoplasma gondii</i> provides novel insights into its molecular organization and functions.

Roumégous, Chloé / Abou Hammoud, Aya / Fuster, Damien / Dupuy, Jean-William / Blancard, Corinne / Salin, Bénédicte / Robinson, Derrick R / Renesto, Patricia / Tardieux, Isabelle / Frénal, Karine

Frontiers in cellular and infection microbiology

2022 Volume 12, Page(s) 1010038

Abstract: ... The ... Toxoplasma gondii ... tachyzoite is a singled-cell obligate intracellular parasite responsible for the acute phase of toxoplasmosis. This polarized cell exhibits an apical complex, a hallmark of the phylum Apicomplexa, essential for motility, ... ...

Abstract	The Toxoplasma gondii tachyzoite is a singled-cell obligate intracellular parasite responsible for the acute phase of toxoplasmosis. This polarized cell exhibits an apical complex, a hallmark of the phylum Apicomplexa, essential for motility, invasion, and egress from the host cell. Located on the opposite end of the cell is the basal complex, an elaborated cytoskeletal structure that also plays critical roles in the lytic cycle of the parasite, being involved in motility, cell division, constriction and cytokinesis, as well as intravacuolar cell-cell communication. Nevertheless, only a few proteins of this structure have been described and functionally assessed. In this study, we used spatial proteomics to identify new basal complex components (BCC), and in situ imaging, including ultrastructure expansion microscopy, to position them. We thus confirmed the localization of nine BCCs out of the 12 selected candidates and assigned them to different sub-compartments of the basal complex, including two new domains located above the basal ring and below the posterior cup. Their functional investigation revealed that none of these BCCs are essential for parasite growth in vitro. However, one BCC is critical for constricting of the basal complex, likely through direct interaction with the class VI myosin heavy chain J (MyoJ), and for gliding motility. Four other BCCs, including a phosphatase and a guanylate-binding protein, are involved in the formation and/or maintenance of the intravacuolar parasite connection, which is required for the rosette organization and synchronicity of cell division.
MeSH term(s)	Humans ; Toxoplasma/metabolism ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Toxoplasmosis/parasitology ; Cytoskeleton/metabolism ; Cell Division
Chemical Substances	Protozoan Proteins
Language	English
Publishing date	2022-10-13
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.1010038
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Article: Identification of NLR-associated Amyloid Signaling Motifs in Bacterial Genomes

Dyrka, Witold / Coustou, Virginie / Daskalov, Asen / Lends, Alons / Bardin, Thierry / Berbon, Mélanie / Kauffmann, Brice / Blancard, Corinne / Salin, Bénédicte / Loquet, Antoine / Saupe, Sven J

Journal of molecular biology. 2020 Nov. 20, v. 432, no. 23

2020

Abstract: In filamentous fungi, amyloid signaling sequences allow Nod-like receptors (NLRs) to activate downstream cell-death inducing proteins with HeLo and HeLo-like (HELL) domains and amyloid RHIM and RHIM-related motifs control immune defense pathways in ... ...

Abstract	In filamentous fungi, amyloid signaling sequences allow Nod-like receptors (NLRs) to activate downstream cell-death inducing proteins with HeLo and HeLo-like (HELL) domains and amyloid RHIM and RHIM-related motifs control immune defense pathways in mammals and flies. Herein, we show bioinformatically that analogous amyloid signaling motifs exist in bacteria. These short motifs are found at the N terminus of NLRs and at the C terminus of proteins with a domain we term BELL. The corresponding NLR and BELL proteins are encoded by adjacent genes. We identify 10 families of such bacterial amyloid signaling sequences (BASS), one of which (BASS3) is homologous to RHIM and a fungal amyloid motif termed PP. BASS motifs occur nearly exclusively in bacteria forming multicellular structures (mainly in Actinobacteria and Cyanobacteria). We analyze experimentally a subset of seven of these motifs (from the most common BASS1 family and the RHIM-related BASS3 family) and find that these sequences form fibrils in vitro. Using a fungal in vivo model, we show that all tested BASS-motifs form prions and that the NLR-side motifs seed prion-formation of the corresponding BELL-side motif. We find that BASS3 motifs show partial prion cross-seeding with mammalian RHIM and fungal PP-motifs and that proline mutations on key positions of the BASS3 core motif, conserved in RHIM and PP-motifs, abolish prion formation. This work expands the paradigm of prion amyloid signaling to multicellular prokaryotes and suggests a long-term evolutionary conservation of these motifs from bacteria, to fungi and animals.
Keywords	Actinobacteria ; Cyanobacteria ; Diptera ; amyloid ; bacteria ; cell death ; evolution ; fungi ; genes ; immune response ; mammals ; models ; mutation ; prions ; prokaryotic cells ; proline ; receptors
Language	English
Dates of publication	2020-1120
Size	p. 6005-6027.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2020.10.004
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Article ; Online: Correction to Mitochondrial ADP/ATP Carrier: Preventing Conformational Changes by Point Mutations Inactivates Nucleotide Transport Activity.

Babot, Marion / Blancard, Corinne / Zeman, Igor / Lauquin, Guy J-M / Trézéguet, Véronique

Biochemistry

2016 Volume 55, Issue 16, Page(s) 2422

Language	English
Publishing date	2016-04-26
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.6b00310
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Article ; Online: Identification of NLR-associated Amyloid Signaling Motifs in Bacterial Genomes.

Dyrka, Witold / Coustou, Virginie / Daskalov, Asen / Lends, Alons / Bardin, Thierry / Berbon, Mélanie / Kauffmann, Brice / Blancard, Corinne / Salin, Bénédicte / Loquet, Antoine / Saupe, Sven J

Journal of molecular biology

2020 Volume 432, Issue 23, Page(s) 6005–6027

Abstract	In filamentous fungi, amyloid signaling sequences allow Nod-like receptors (NLRs) to activate downstream cell-death inducing proteins with HeLo and HeLo-like (HELL) domains and amyloid RHIM and RHIM-related motifs control immune defense pathways in mammals and flies. Herein, we show bioinformatically that analogous amyloid signaling motifs exist in bacteria. These short motifs are found at the N terminus of NLRs and at the C terminus of proteins with a domain we term BELL. The corresponding NLR and BELL proteins are encoded by adjacent genes. We identify 10 families of such bacterial amyloid signaling sequences (BASS), one of which (BASS3) is homologous to RHIM and a fungal amyloid motif termed PP. BASS motifs occur nearly exclusively in bacteria forming multicellular structures (mainly in Actinobacteria and Cyanobacteria). We analyze experimentally a subset of seven of these motifs (from the most common BASS1 family and the RHIM-related BASS3 family) and find that these sequences form fibrils in vitro. Using a fungal in vivo model, we show that all tested BASS-motifs form prions and that the NLR-side motifs seed prion-formation of the corresponding BELL-side motif. We find that BASS3 motifs show partial prion cross-seeding with mammalian RHIM and fungal PP-motifs and that proline mutations on key positions of the BASS3 core motif, conserved in RHIM and PP-motifs, abolish prion formation. This work expands the paradigm of prion amyloid signaling to multicellular prokaryotes and suggests a long-term evolutionary conservation of these motifs from bacteria, to fungi and animals.
MeSH term(s)	Amino Acid Motifs/genetics ; Amino Acid Sequence/genetics ; Amyloid/genetics ; Amyloidogenic Proteins/genetics ; Animals ; Cyanobacteria/genetics ; Drosophila/genetics ; Evolution, Molecular ; Fungi/genetics ; Genome, Bacterial/genetics ; Immunity, Innate/genetics ; NLR Proteins/genetics ; Prions/genetics ; Signal Transduction/genetics
Chemical Substances	Amyloid ; Amyloidogenic Proteins ; NLR Proteins ; Prions
Language	English
Publishing date	2020-10-13
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2020.10.004
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Article ; Online: TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting in situ assembly of mammalian ATP synthase proton channel.

Bahri, Hela / Buratto, Jeremie / Rojo, Manuel / Dompierre, Jim Paul / Salin, Bénédicte / Blancard, Corinne / Cuvellier, Sylvain / Rose, Marie / Ben Ammar Elgaaied, Amel / Tetaud, Emmanuel / di Rago, Jean-Paul / Devin, Anne / Duvezin-Caubet, Stéphane

Biochimica et biophysica acta. Molecular cell research

2020 Volume 1868, Issue 4, Page(s) 118942

Abstract: Mitochondrial ATP-synthesis is catalyzed by a F1Fo-ATP synthase, an enzyme of dual genetic origin enriched at the edge of cristae where it plays a key role in their structure/stability. The enzyme's biogenesis remains poorly understood, both from a ... ...

Abstract	Mitochondrial ATP-synthesis is catalyzed by a F1Fo-ATP synthase, an enzyme of dual genetic origin enriched at the edge of cristae where it plays a key role in their structure/stability. The enzyme's biogenesis remains poorly understood, both from a mechanistic and a compartmentalization point of view. The present study provides novel molecular insights into this process through investigations on a human protein called TMEM70 with an unclear role in the assembly of ATP synthase. A recent study has revealed the existence of physical interactions between TMEM70 and the subunit c (Su.c), a protein present in 8 identical copies forming a transmembrane oligomeric ring (c-ring) within the ATP synthase proton translocating domain (Fo). Herein we analyzed the ATP-synthase assembly in cells lacking TMEM70, mitochondrial DNA or F1 subunits and observe a direct correlation between TMEM70 and Su.c levels, regardless of the status of other ATP synthase subunits or of mitochondrial bioenergetics. Immunoprecipitation, two-dimensional blue-native/SDS-PAGE, and pulse-chase experiments reveal that TMEM70 forms large oligomers that interact with Su.c not yet incorporated into ATP synthase complexes. Moreover, discrete TMEM70-Su.c complexes with increasing Su.c contents can be detected, suggesting a role for TMEM70 oligomers in the gradual assembly of the c-ring. Furthermore, we demonstrate using expansion super-resolution microscopy the specific localization of TMEM70 at the inner cristae membrane, distinct from the MICOS component MIC60. Taken together, our results show that TMEM70 oligomers provide a scaffold for c-ring assembly and that mammalian ATP synthase is assembled within inner cristae membranes.
MeSH term(s)	Cell Line ; Energy Metabolism ; Gene Knockout Techniques ; HEK293 Cells ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Microscopy, Electron ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondrial Proton-Translocating ATPases/chemistry ; Mitochondrial Proton-Translocating ATPases/metabolism ; Protein Domains ; Protein Multimerization
Chemical Substances	Membrane Proteins ; Mitochondrial Proteins ; TMEM70 protein, human ; Mitochondrial Proton-Translocating ATPases (EC 3.6.3.-)
Language	English
Publishing date	2020-12-23
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamcr.2020.118942
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