{
  "abstract": "Endonucleolytic removal of 5’-leader sequences from tRNA precursor transcripts (pre-tRNAs) by RNase P is essential for protein synthesis. Beyond RNA-based RNase P enzymes, protein-only versions of the enzyme exert this function in various Eukarya (there termed PRORPs) and in some bacteria ( Aquifex aeolicus and close relatives); both enzyme types belong to distinct subgroups of the PIN domain metallonuclease superfamily. Homologs of Aquifex RNase P (HARPs) are also expressed in some other bacteria and many archaea, where they coexist with RNA-based RNase P and do not represent the main RNase P activity. Here we solved the structure of the bacterial HARP from Halorhodospira halophila by cryo-EM revealing a novel screw-like dodecameric assembly. Biochemical experiments demonstrate that oligomerization is required for RNase P activity of HARPs. We propose that the tRNA substrate binds to an extended spike-helix (SH) domain that protrudes from the screw-like assembly to position the 5’-end in close proximity to the active site of the neighboring dimer subunit. The structure suggests that eukaryotic PRORPs and prokaryotic HARPs recognize the same structural elements of pre-tRNAs (tRNA elbow region and cleavage site). Our analysis thus delivers the structural and mechanistic basis for pre-tRNA processing by the prokaryotic HARP system.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "name": "Rebecca Feyh"
    },
    {
      "name": "Nadine B Waeber"
    },
    {
      "name": "Simone Prinz"
    },
    {
      "name": "Pietro Ivan Giammarinaro"
    },
    {
      "name": "Gert Bange"
    },
    {
      "name": "Georg Hochberg"
    },
    {
      "name": "Roland K Hartmann"
    },
    {
      "name": "Florian Altegoer"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/5zk2b24j8znpp.bib",
  "cited_by": 20,
  "doi": "10.7554/elife.70160",
  "fulltext_url": null,
  "id": "5zk2b24j8znpp",
  "issns": [
    "2050-084X"
  ],
  "landing_url": "https://hal.science/hal-05780522v1",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.sdv.bbm"
    ],
    [
      "hal",
      "2.sdv.bbm.bs"
    ],
    [
      "openalex",
      "1312|RNA and protein synthesis mechanisms"
    ]
  ],
  "openalex": "W3173908141",
  "pdf_url": null,
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-06",
  "publisher": "eLife Sciences Publication",
  "ris": "https://research.draconitic.com/paper/5zk2b24j8znpp.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:48Z",
      "native_id": "hal-05780522",
      "source": "hal",
      "url": "https://hal.science/hal-05780522v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "hal:2.sdv.bbm.bs",
      "subfield": "structural-biology"
    },
    {
      "field": "biology",
      "origin": "hal:0.sdv",
      "subfield": "general"
    }
  ],
  "title": "Structure and mechanistic features of the prokaryotic minimal RNase P",
  "title_text": "Structure and mechanistic features of the prokaryotic minimal RNase P",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:48Z",
  "url": "https://research.draconitic.com/paper/5zk2b24j8znpp",
  "venue": "eLife",
  "versions": []
}