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  1. Article ; Online: Structure and tethering mechanism of dynein-2 intermediate chains in intraflagellar transport.

    Mukhopadhyay, Aakash G / Toropova, Katerina / Daly, Lydia / Wells, Jennifer N / Vuolo, Laura / Mladenov, Miroslav / Seda, Marian / Jenkins, Dagan / Stephens, David J / Roberts, Anthony J

    The EMBO journal

    2024  Volume 43, Issue 7, Page(s) 1257–1272

    Abstract: Dynein-2 is a large multiprotein complex that powers retrograde intraflagellar transport (IFT) of cargoes within cilia/flagella, but the molecular mechanism underlying this function is still emerging. Distinctively, dynein-2 contains two identical force- ... ...

    Abstract Dynein-2 is a large multiprotein complex that powers retrograde intraflagellar transport (IFT) of cargoes within cilia/flagella, but the molecular mechanism underlying this function is still emerging. Distinctively, dynein-2 contains two identical force-generating heavy chains that interact with two different intermediate chains (WDR34 and WDR60). Here, we dissect regulation of dynein-2 function by WDR34 and WDR60 using an integrative approach including cryo-electron microscopy and CRISPR/Cas9-enabled cell biology. A 3.9 Å resolution structure shows how WDR34 and WDR60 use surprisingly different interactions to engage equivalent sites of the two heavy chains. We show that cilia can assemble in the absence of either WDR34 or WDR60 individually, but not both subunits. Dynein-2-dependent distribution of cargoes depends more strongly on WDR60, because the unique N-terminal extension of WDR60 facilitates dynein-2 targeting to cilia. Strikingly, this N-terminal extension can be transplanted onto WDR34 and retain function, suggesting it acts as a flexible tether to the IFT "trains" that assemble at the ciliary base. We discuss how use of unstructured tethers represents an emerging theme in IFT train interactions.
    MeSH term(s) Dyneins/metabolism ; Cryoelectron Microscopy ; Biological Transport ; Cilia/metabolism ; Flagella/metabolism
    Chemical Substances Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2024-03-07
    Publishing country England
    Document type Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.1038/s44318-024-00060-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1808: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 100: Show issues

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  2. Article ; Online: Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.

    Wells, Jennifer N / Buschauer, Robert / Mackens-Kiani, Timur / Best, Katharina / Kratzat, Hanna / Berninghausen, Otto / Becker, Thomas / Gilbert, Wendy / Cheng, Jingdong / Beckmann, Roland

    PLoS biology

    2020  Volume 18, Issue 7, Page(s) e3000780

    Abstract: Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a ... ...

    Abstract Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target of Myb protein 1 (Stm1; SERPINE1 mRNA-binding protein 1 [SERBP1] in mammals), and recently, late-annotated short open reading frame 2 (Lso2; coiled-coil domain containing short open reading frame 124 [CCDC124] in mammals) was found to be involved in translational recovery after starvation from stationary phase. Here, we present cryo-electron microscopy (cryo-EM) structures of translationally inactive yeast and human ribosomes. We found Lso2/CCDC124 accumulating on idle ribosomes in the nonrotated state, in contrast to Stm1/SERBP1-bound ribosomes, which display a rotated state. Lso2/CCDC124 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system, which splits Lso2-containing, but not Stm1-containing, ribosomes. We propose a model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes.
    MeSH term(s) Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Sequence ; Binding Sites ; Cell Cycle Proteins/chemistry ; Cell Cycle Proteins/metabolism ; Conserved Sequence ; Evolution, Molecular ; HEK293 Cells ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/metabolism ; Models, Molecular ; Peptides/chemistry ; Protein Binding ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Transfer/metabolism ; RNA-Binding Proteins/metabolism ; Ribosomal Proteins/chemistry ; Ribosomal Proteins/metabolism ; Ribosomes/metabolism ; Ribosomes/ultrastructure ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae/ultrastructure ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Structure-Activity Relationship
    Chemical Substances Adaptor Proteins, Signal Transducing ; Ccdc124 protein, human ; Cell Cycle Proteins ; Intracellular Signaling Peptides and Proteins ; LSO2 protein, S cerevisiae ; PA2G4 protein, human ; Peptides ; RNA, Messenger ; RNA-Binding Proteins ; Ribosomal Proteins ; Saccharomyces cerevisiae Proteins ; RNA, Transfer (9014-25-9)
    Language English
    Publishing date 2020-07-20
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126776-5
    ISSN 1545-7885 ; 1544-9173
    ISSN (online) 1545-7885
    ISSN 1544-9173
    DOI 10.1371/journal.pbio.3000780
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6193: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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  3. Article ; Online: Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation.

    Mus, Florence / Eilers, Brian J / Alleman, Alexander B / Kabasakal, Burak V / Wells, Jennifer N / Murray, James W / Nocek, Boguslaw P / DuBois, Jennifer L / Peters, John W

    Scientific reports

    2017  Volume 7, Issue 1, Page(s) 7234

    Abstract: Microorganisms use carboxylase enzymes to form new carbon-carbon bonds by introducing carbon dioxide gas ( ... ...

    Abstract Microorganisms use carboxylase enzymes to form new carbon-carbon bonds by introducing carbon dioxide gas (CO
    MeSH term(s) Acetone/chemistry ; Adenosine Triphosphate/chemistry ; Binding Sites ; Carbon Dioxide/chemistry ; Carboxy-Lyases/chemistry ; Carboxy-Lyases/genetics ; Catalytic Domain ; Ligands ; Models, Molecular ; Molecular Conformation ; Protein Binding ; Protein Interaction Domains and Motifs ; Structure-Activity Relationship
    Chemical Substances Ligands ; Acetone (1364PS73AF) ; Carbon Dioxide (142M471B3J) ; Adenosine Triphosphate (8L70Q75FXE) ; Carboxy-Lyases (EC 4.1.1.-) ; acetone carboxylase (EC 4.1.1.-)
    Language English
    Publishing date 2017-08-03
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-017-06973-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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