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  1. Artikel: Structural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes.

    Bhatta, Arjun / Hillen, Hauke S

    Trends in biochemical sciences

    2022  Band 47, Heft 11, Seite(n) 965–977

    Abstract: Ribonuclease P (RNase P) enzymes are responsible for the 5' processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase ... ...

    Abstract Ribonuclease P (RNase P) enzymes are responsible for the 5' processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase Ps (PRORPs) can be found in all three domains of life and can be divided into two structurally different types: eukaryotic and prokaryotic. Recent structural studies on members of both families reveal a surprising diversity of molecular architectures, but also highlight conceptual and mechanistic similarities. Here, we provide a comparison between the different types of PRORP enzymes and review how the combination of structural, biochemical, and biophysical studies has led to a molecular picture of protein-mediated tRNA processing.
    Mesh-Begriff(e) Arabidopsis/genetics ; Humans ; RNA Processing, Post-Transcriptional ; RNA, Catalytic/metabolism ; RNA, Transfer/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/genetics ; Ribonuclease P/metabolism
    Chemische Substanzen RNA, Catalytic ; RNA, Transfer (9014-25-9) ; Ribonuclease P (EC 3.1.26.5)
    Sprache Englisch
    Erscheinungsdatum 2022-06-18
    Erscheinungsland England
    Dokumenttyp Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 194216-5
    ISSN 1362-4326 ; 0968-0004 ; 0376-5067
    ISSN (online) 1362-4326
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2022.05.006
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel: Structural and mechanistic basis of RNA processing by protein-only ribonuclease P enzymes

    Bhatta, Arjun / Hillen, Hauke S.

    Trends in biochemical sciences. 2022,

    2022  

    Abstract: Ribonuclease P (RNase P) enzymes are responsible for the 5′ processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase ... ...

    Abstract Ribonuclease P (RNase P) enzymes are responsible for the 5′ processing of tRNA precursors. In addition to the well-characterised ribozyme-based RNase P enzymes, an evolutionarily distinct group of protein-only RNase Ps exists. These proteinaceous RNase Ps (PRORPs) can be found in all three domains of life and can be divided into two structurally different types: eukaryotic and prokaryotic. Recent structural studies on members of both families reveal a surprising diversity of molecular architectures, but also highlight conceptual and mechanistic similarities. Here, we provide a comparison between the different types of PRORP enzymes and review how the combination of structural, biochemical, and biophysical studies has led to a molecular picture of protein-mediated tRNA processing.
    Schlagwörter RNA precursors ; architecture ; ribonucleases
    Sprache Englisch
    Erscheinungsort Elsevier Ltd
    Dokumenttyp Artikel
    Anmerkung Pre-press version
    ZDB-ID 194220-7
    ISSN 0968-0004 ; 0376-5067
    ISSN 0968-0004 ; 0376-5067
    DOI 10.1016/j.tibs.2022.05.006
    Datenquelle NAL Katalog (AGRICOLA)

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    Verfügbar in ZB MED Bonn

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  3. Artikel ; Online: Structural basis of RNA processing by human mitochondrial RNase P.

    Bhatta, Arjun / Dienemann, Christian / Cramer, Patrick / Hillen, Hauke S

    Nature structural & molecular biology

    2021  Band 28, Heft 9, Seite(n) 713–723

    Abstract: Human mitochondrial transcripts contain messenger and ribosomal RNAs flanked by transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to liberate all RNA species. In contrast to nuclear or bacterial RNase P, mtRNase P is not a ...

    Abstract Human mitochondrial transcripts contain messenger and ribosomal RNAs flanked by transfer RNAs (tRNAs), which are excised by mitochondrial RNase (mtRNase) P and Z to liberate all RNA species. In contrast to nuclear or bacterial RNase P, mtRNase P is not a ribozyme but comprises three protein subunits that carry out RNA cleavage and methylation by unknown mechanisms. Here, we present the cryo-EM structure of human mtRNase P bound to precursor tRNA, which reveals a unique mechanism of substrate recognition and processing. Subunits TRMT10C and SDR5C1 form a subcomplex that binds conserved mitochondrial tRNA elements, including the anticodon loop, and positions the tRNA for methylation. The endonuclease PRORP is recruited and activated through interactions with its PPR and nuclease domains to ensure precise pre-tRNA cleavage. The structure provides the molecular basis for the first step of RNA processing in human mitochondria.
    Mesh-Begriff(e) 3-Hydroxyacyl CoA Dehydrogenases/chemistry ; 3-Hydroxyacyl CoA Dehydrogenases/metabolism ; Anticodon/chemistry ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/metabolism ; Archaeal Proteins/chemistry ; Archaeal Proteins/metabolism ; Cryoelectron Microscopy ; Humans ; Methylation ; Methyltransferases/chemistry ; Methyltransferases/genetics ; Methyltransferases/metabolism ; Mitochondria/enzymology ; Models, Molecular ; Mutation, Missense ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Protein Interaction Mapping ; RNA Precursors/metabolism ; RNA Processing, Post-Transcriptional ; RNA, Fungal/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/metabolism ; Species Specificity ; Structure-Activity Relationship ; Substrate Specificity
    Chemische Substanzen Anticodon ; Arabidopsis Proteins ; Archaeal Proteins ; RNA Precursors ; RNA, Fungal ; Recombinant Proteins ; 3-Hydroxyacyl CoA Dehydrogenases (EC 1.1.1.-) ; HSD17B10 protein, human (EC 1.1.1.35) ; Methyltransferases (EC 2.1.1.-) ; TRMT10c protein, human (EC 2.1.1.-) ; PRORP protein, human (EC 3.1.26.5) ; PRORP1 protein, Arabidopsis (EC 3.1.26.5) ; Ribonuclease P (EC 3.1.26.5)
    Sprache Englisch
    Erscheinungsdatum 2021-09-06
    Erscheinungsland United States
    Dokumenttyp Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-021-00637-y
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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