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  1. Article ; Online: Mitochondrial RNA granules are fluid condensates positioned by membrane dynamics.

    Rey, Timo / Zaganelli, Sofia / Cuillery, Emilie / Vartholomaiou, Evangelia / Croisier, Marie / Martinou, Jean-Claude / Manley, Suliana

    Nature cell biology

    2020  Volume 22, Issue 10, Page(s) 1180–1186

    Abstract: Mitochondria contain the genetic information and expression machinery to produce essential respiratory chain proteins. Within the mitochondrial matrix, newly synthesized RNA, RNA processing proteins and mitoribosome assembly factors form punctate sub- ... ...

    Abstract Mitochondria contain the genetic information and expression machinery to produce essential respiratory chain proteins. Within the mitochondrial matrix, newly synthesized RNA, RNA processing proteins and mitoribosome assembly factors form punctate sub-compartments referred to as mitochondrial RNA granules (MRGs)
    MeSH term(s) HeLa Cells ; Humans ; Microscopy, Fluorescence ; Mitochondria/physiology ; Mitochondrial Dynamics ; Mitochondrial Membranes/physiology ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondrial Ribosomes/physiology ; RNA, Mitochondrial/genetics ; RNA, Mitochondrial/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances Mitochondrial Proteins ; RNA, Mitochondrial ; RNA-Binding Proteins
    Language English
    Publishing date 2020-09-28
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1474722-4
    ISSN 1476-4679 ; 1465-7392
    ISSN (online) 1476-4679
    ISSN 1465-7392
    DOI 10.1038/s41556-020-00584-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5169: Show issues Location:
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    Zs.MG 12: Show issues

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  2. Article ; Online: Distinct fission signatures predict mitochondrial degradation or biogenesis.

    Kleele, Tatjana / Rey, Timo / Winter, Julius / Zaganelli, Sofia / Mahecic, Dora / Perreten Lambert, Hélène / Ruberto, Francesco Paolo / Nemir, Mohamed / Wai, Timothy / Pedrazzini, Thierry / Manley, Suliana

    Nature

    2021  Volume 593, Issue 7859, Page(s) 435–439

    Abstract: Mitochondrial fission is a highly regulated process that, when disrupted, can alter metabolism, proliferation and ... ...

    Abstract Mitochondrial fission is a highly regulated process that, when disrupted, can alter metabolism, proliferation and apoptosis
    MeSH term(s) Actins ; Animals ; COS Cells ; Cell Survival ; Cells, Cultured ; Chlorocebus aethiops ; DNA, Mitochondrial/analysis ; DNA, Mitochondrial/metabolism ; Dynamins ; Endoplasmic Reticulum ; Humans ; Lysosomes ; Membrane Proteins ; Mice ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Dynamics ; Mitochondrial Proteins ; Mitophagy
    Chemical Substances Actins ; DNA, Mitochondrial ; FIS1 protein, human ; Membrane Proteins ; Mitochondrial Proteins ; DNM1L protein, human (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5)
    Language English
    Publishing date 2021-05-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-021-03510-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 26: Show issues Location:
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    Zs.MG 9: Show issues
    Zs.MO 244: Show issues

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  3. Article ; Online: FASTKD1 and FASTKD4 have opposite effects on expression of specific mitochondrial RNAs, depending upon their endonuclease-like RAP domain.

    Boehm, Erik / Zaganelli, Sofia / Maundrell, Kinsey / Jourdain, Alexis A / Thore, Stéphane / Martinou, Jean-Claude

    Nucleic acids research

    2017  Volume 45, Issue 10, Page(s) 6135–6146

    Abstract: FASTK family proteins have been identified as regulators of mitochondrial RNA homeostasis linked to mitochondrial diseases, but much remains unknown about these proteins. We show that CRISPR-mediated disruption of FASTKD1 increases ND3 mRNA level, while ... ...

    Abstract FASTK family proteins have been identified as regulators of mitochondrial RNA homeostasis linked to mitochondrial diseases, but much remains unknown about these proteins. We show that CRISPR-mediated disruption of FASTKD1 increases ND3 mRNA level, while disruption of FASTKD4 reduces the level of ND3 and of other mature mRNAs including ND5 and CYB, and causes accumulation of ND5-CYB precursor RNA. Disrupting both FASTKD1 and FASTKD4 in the same cell results in decreased ND3 mRNA similar to the effect of depleting FASTKD4 alone, indicating that FASTKD4 loss is epistatic. Interestingly, very low levels of FASTKD4 are sufficient to prevent ND3 loss and ND5-CYB precursor accumulation, suggesting that FASTKD4 may act catalytically. Furthermore, structural modeling predicts that each RAP domain of FASTK proteins contains a nuclease fold with a conserved aspartate residue at the putative active site. Accordingly, mutation of this residue in FASTKD4 abolishes its function. Experiments with FASTK chimeras indicate that the RAP domain is essential for the function of the FASTK proteins, while the region upstream determines RNA targeting and protein localization. In conclusion, this paper identifies new aspects of FASTK protein biology and suggests that the RAP domain function depends on an intrinsic nucleolytic activity.
    MeSH term(s) Amino Acid Sequence ; CRISPR-Cas Systems ; Cytochromes b/genetics ; Electron Transport Complex I/genetics ; Gene Expression Regulation ; Gene Knockdown Techniques ; HEK293 Cells ; Humans ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/physiology ; Models, Molecular ; Protein Conformation ; Protein Domains ; RNA/genetics ; RNA/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Mitochondrial ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/physiology ; Sequence Alignment ; Sequence Homology ; Transcription, Genetic
    Chemical Substances FASTKD1 protein, human ; Mitochondrial Proteins ; RNA, Messenger ; RNA, Mitochondrial ; RNA-Binding Proteins ; TBRG4 protein, human ; RNA (63231-63-0) ; Cytochromes b (9035-37-4) ; MT-ND5 protein, human (EC 1.6.99.3) ; Electron Transport Complex I (EC 7.1.1.2) ; MT-ND3 protein, human (EC 7.1.1.2)
    Language English
    Publishing date 2017-03-20
    Publishing country England
    Document type Comparative Study ; Journal Article
    ZDB-ID 186809-3
    ISSN 1362-4962 ; 1362-4954 ; 0301-5610 ; 0305-1048
    ISSN (online) 1362-4962 ; 1362-4954
    ISSN 0301-5610 ; 0305-1048
    DOI 10.1093/nar/gkx164
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1067: Show issues Location:
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  4. Article ; Online: The Pseudouridine Synthase RPUSD4 Is an Essential Component of Mitochondrial RNA Granules.

    Zaganelli, Sofia / Rebelo-Guiomar, Pedro / Maundrell, Kinsey / Rozanska, Agata / Pierredon, Sandra / Powell, Christopher A / Jourdain, Alexis A / Hulo, Nicolas / Lightowlers, Robert N / Chrzanowska-Lightowlers, Zofia M / Minczuk, Michal / Martinou, Jean-Claude

    The Journal of biological chemistry

    2017  Volume 292, Issue 11, Page(s) 4519–4532

    Abstract: Mitochondrial gene expression is a fundamental process that is largely dependent on nuclear-encoded proteins. Several steps of mitochondrial RNA processing and maturation, including RNA post-transcriptional modification, appear to be spatially organized ... ...

    Abstract Mitochondrial gene expression is a fundamental process that is largely dependent on nuclear-encoded proteins. Several steps of mitochondrial RNA processing and maturation, including RNA post-transcriptional modification, appear to be spatially organized into distinct foci, which we have previously termed mitochondrial RNA granules (MRGs). Although an increasing number of proteins have been localized to MRGs, a comprehensive analysis of the proteome of these structures is still lacking. Here, we have applied a microscopy-based approach that has allowed us to identify novel components of the MRG proteome. Among these, we have focused our attention on RPUSD4, an uncharacterized mitochondrial putative pseudouridine synthase. We show that RPUSD4 depletion leads to a severe reduction of the steady-state level of the 16S mitochondrial (mt) rRNA with defects in the biogenesis of the mitoribosome large subunit and consequently in mitochondrial translation. We report that RPUSD4 binds 16S mt-rRNA, mt-tRNA
    MeSH term(s) Cell Line ; Humans ; Intramolecular Transferases/analysis ; Intramolecular Transferases/genetics ; Intramolecular Transferases/metabolism ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Proteins/metabolism ; Protein Transport ; RNA/metabolism ; RNA Interference ; RNA, Mitochondrial ; RNA, Ribosomal, 16S/metabolism ; RNA, Small Interfering/genetics ; RNA, Transfer, Met/metabolism ; RNA, Transfer, Phe/metabolism
    Chemical Substances Mitochondrial Proteins ; RNA, Mitochondrial ; RNA, Ribosomal, 16S ; RNA, Small Interfering ; RNA, Transfer, Met ; RNA, Transfer, Phe ; RNA (63231-63-0) ; Intramolecular Transferases (EC 5.4.-) ; pseudouridine synthases (EC 5.4.99.-)
    Language English
    Publishing date 2017-01-12
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M116.771105
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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