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

    Bhatta, Arjun / Hillen, Hauke S

    Trends in biochemical sciences

    2022  Volume 47, Issue 11, Page(s) 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 term(s) Arabidopsis/genetics ; Humans ; RNA Processing, Post-Transcriptional ; RNA, Catalytic/metabolism ; RNA, Transfer/metabolism ; Ribonuclease P/chemistry ; Ribonuclease P/genetics ; Ribonuclease P/metabolism
    Chemical Substances RNA, Catalytic ; RNA, Transfer (9014-25-9) ; Ribonuclease P (EC 3.1.26.5)
    Language English
    Publishing date 2022-06-18
    Publishing country England
    Document type 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1207: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
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  2. Article: 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.
    Keywords RNA precursors ; architecture ; ribonucleases
    Language English
    Publishing place Elsevier Ltd
    Document type Article
    Note 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
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 78/716: Show issues

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  3. Article ; 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  Volume 28, Issue 9, Page(s) 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 term(s) 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
    Chemical Substances 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)
    Language English
    Publishing date 2021-09-06
    Publishing country United States
    Document type 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
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4101: Show issues Location:
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    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)
    Zs.MG 56: Show issues

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