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  1. Article ; Online: The

    Bohl, Valentin / Hollmann, Nele Merret / Melzer, Tobias / Katikaridis, Panagiotis / Meins, Lena / Simon, Bernd / Flemming, Dirk / Sinning, Irmgard / Hennig, Janosch / Mogk, Axel

    eLife

    2024  Volume 12

    Abstract: Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during, e.g., food ...

    Abstract Heat stress can cause cell death by triggering the aggregation of essential proteins. In bacteria, aggregated proteins are rescued by the canonical Hsp70/AAA+ (ClpB) bi-chaperone disaggregase. Man-made, severe stress conditions applied during, e.g., food processing represent a novel threat for bacteria by exceeding the capacity of the Hsp70/ClpB system. Here, we report on the potent autonomous AAA+ disaggregase ClpL from
    MeSH term(s) Humans ; Animals ; Listeria monocytogenes ; Cell Death ; Estrus ; Food ; HSP70 Heat-Shock Proteins ; Neural Tube Defects
    Chemical Substances HSP70 Heat-Shock Proteins
    Language English
    Publishing date 2024-04-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 2687154-3
    ISSN 2050-084X ; 2050-084X
    ISSN (online) 2050-084X
    ISSN 2050-084X
    DOI 10.7554/eLife.92746
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  2. Book ; Online ; Thesis: Structure and dynamics of Upstream of N Ras and their influence on RNA binding and translation regulation

    Hollmann, Nele Merret [Verfasser] / Hennig, Janosch [Akademischer Betreuer]

    2021  

    Author's details Nele Merret Hollmann ; Betreuer: Janosch Hennig
    Keywords Naturwissenschaften ; Science
    Subject code sg500
    Language English
    Publisher Universitätsbibliothek Heidelberg
    Publishing place Heidelberg
    Document type Book ; Online ; Thesis
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  3. Article ; Online: Upstream of N-Ras C-terminal cold shock domains mediate poly(A) specificity in a novel RNA recognition mode and bind poly(A) binding protein.

    Hollmann, Nele Merret / Jagtap, Pravin Kumar Ankush / Linse, Johanna-Barbara / Ullmann, Philip / Payr, Marco / Murciano, Brice / Simon, Bernd / Hub, Jochen S / Hennig, Janosch

    Nucleic acids research

    2023  Volume 51, Issue 4, Page(s) 1895–1913

    Abstract: RNA binding proteins (RBPs) often engage multiple RNA binding domains (RBDs) to increase target specificity and affinity. However, the complexity of target recognition of multiple RBDs remains largely unexplored. Here we use Upstream of N-Ras (Unr), a ... ...

    Abstract RNA binding proteins (RBPs) often engage multiple RNA binding domains (RBDs) to increase target specificity and affinity. However, the complexity of target recognition of multiple RBDs remains largely unexplored. Here we use Upstream of N-Ras (Unr), a multidomain RBP, to demonstrate how multiple RBDs orchestrate target specificity. A crystal structure of the three C-terminal RNA binding cold-shock domains (CSD) of Unr bound to a poly(A) sequence exemplifies how recognition goes beyond the classical ππ-stacking in CSDs. Further structural studies reveal several interaction surfaces between the N-terminal and C-terminal part of Unr with the poly(A)-binding protein (pAbp). All interactions are validated by mutational analyses and the high-resolution structures presented here will guide further studies to understand how both proteins act together in cellular processes.
    MeSH term(s) Cold-Shock Response ; DNA-Binding Proteins/genetics ; Poly A/metabolism ; Poly(A)-Binding Proteins/metabolism ; Protein Binding ; RNA/chemistry
    Chemical Substances DNA-Binding Proteins ; Poly A (24937-83-5) ; Poly(A)-Binding Proteins ; RNA (63231-63-0) ; UNR protein, Drosophila
    Language English
    Publishing date 2023-01-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    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/gkac1277
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  4. Article ; Online: Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras.

    Hollmann, Nele Merret / Jagtap, Pravin Kumar Ankush / Masiewicz, Pawel / Guitart, Tanit / Simon, Bernd / Provaznik, Jan / Stein, Frank / Haberkant, Per / Sweetapple, Lara Jayne / Villacorta, Laura / Mooijman, Dylan / Benes, Vladimir / Savitski, Mikhail M / Gebauer, Fátima / Hennig, Janosch

    Cell reports

    2020  Volume 32, Issue 3, Page(s) 107930

    Abstract: RNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their ... ...

    Abstract RNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their interactions with RNA. However, how multiple RBDs recognize their cognate single-stranded RNA (ssRNA) sequences in concert remains poorly understood. Here, we use Upstream of N-Ras (Unr) as a model system to address this question. Although reported to contain five ssRNA-binding cold-shock domains (CSDs), we demonstrate that Unr includes an additional four CSDs that do not bind RNA (pseudo-RBDs) but are involved in mediating RNA tertiary structure specificity by reducing the conformational heterogeneity of Unr. Disrupting the interactions between canonical and non-canonical CSDs impacts RNA binding, Unr-mediated translation regulation, and the Unr-dependent RNA interactome. Taken together, our studies reveal a new paradigm in protein-RNA recognition, where interactions between RBDs and pseudo-RBDs select RNA tertiary structures, influence RNP assembly, and define target specificity.
    MeSH term(s) Amino Acid Sequence ; Animals ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/chemistry ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Nucleic Acid Conformation ; Protein Biosynthesis ; Protein Domains ; RNA/chemistry ; RNA/metabolism
    Chemical Substances DNA-Binding Proteins ; Drosophila Proteins ; UNR protein, Drosophila ; RNA (63231-63-0)
    Language English
    Publishing date 2020-07-03
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2020.107930
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.

    Ankush Jagtap, Pravin Kumar / Müller, Marisa / Masiewicz, Pawel / von Bülow, Sören / Hollmann, Nele Merret / Chen, Po-Chia / Simon, Bernd / Thomae, Andreas W / Becker, Peter B / Hennig, Janosch

    Nucleic acids research

    2018  Volume 47, Issue 8, Page(s) 4319–4333

    Abstract: Maleless (MLE) is an evolutionary conserved member of the DExH family of helicases in Drosophila. Besides its function in RNA editing and presumably siRNA processing, MLE is best known for its role in remodelling non-coding roX RNA in the context of X ... ...

    Abstract Maleless (MLE) is an evolutionary conserved member of the DExH family of helicases in Drosophila. Besides its function in RNA editing and presumably siRNA processing, MLE is best known for its role in remodelling non-coding roX RNA in the context of X chromosome dosage compensation in male flies. MLE and its human orthologue, DHX9 contain two tandem double-stranded RNA binding domains (dsRBDs) located at the N-terminal region. The two dsRBDs are essential for localization of MLE at the X-territory and it is presumed that this involves binding roX secondary structures. However, for dsRBD1 roX RNA binding has so far not been described. Here, we determined the solution NMR structure of dsRBD1 and dsRBD2 of MLE in tandem and investigated its role in double-stranded RNA (dsRNA) binding. Our NMR and SAXS data show that both dsRBDs act as independent structural modules in solution and are canonical, non-sequence-specific dsRBDs featuring non-canonical KKxAXK RNA binding motifs. NMR titrations combined with filter binding experiments and isothermal titration calorimetry (ITC) document the contribution of dsRBD1 to dsRNA binding in vitro. Curiously, dsRBD1 mutants in which dsRNA binding in vitro is strongly compromised do not affect roX2 RNA binding and MLE localization in cells. These data suggest alternative functions for dsRBD1 in vivo.
    MeSH term(s) Amino Acid Sequence ; Animals ; Binding Sites ; Chromosomal Proteins, Non-Histone/chemistry ; Chromosomal Proteins, Non-Histone/genetics ; Chromosomal Proteins, Non-Histone/metabolism ; Cloning, Molecular ; DNA Helicases/chemistry ; DNA Helicases/genetics ; DNA Helicases/metabolism ; Dosage Compensation, Genetic ; Double-Stranded RNA Binding Motif ; Drosophila Proteins/chemistry ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/chemistry ; Drosophila melanogaster/genetics ; Drosophila melanogaster/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Gene Expression Regulation ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Kinetics ; Male ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; RNA, Long Noncoding/chemistry ; RNA, Long Noncoding/genetics ; RNA, Long Noncoding/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Transcription Factors/chemistry ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances Chromosomal Proteins, Non-Histone ; Drosophila Proteins ; RNA, Long Noncoding ; Recombinant Proteins ; Transcription Factors ; mle protein, Drosophila ; roX1 protein, Drosophila ; DNA Helicases (EC 3.6.4.-)
    Language English
    Publishing date 2018-12-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    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/gkz125
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1067: 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)

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