{
  "abstract": "The ATPase SecA drives the post-translational translocation of proteins through the SecY channel in the bacterial inner membrane. SecA is a dimer that can dissociate into monomers under certain conditions. To address the functional importance of the monomeric state, we generated an Escherichia coli SecA mutant that is almost completely monomeric (>99%), consistent with predictions from the crystal structure of Bacillus subtilis SecA. In vitro, the monomeric derivative retained significant activity in various assays, and in vivo, it sustained 85% of the growth rate of wild type cells and reduced the accumulation of precursor proteins in the cytoplasm. Disulfide cross-linking in intact cells showed that mutant SecA is monomeric and that even its parental dimeric form is dissociated. Our results suggest that SecA functions as a monomer during protein translocation in vivo.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "name": "Eran Or"
    },
    {
      "name": "Dana Boyd"
    },
    {
      "name": "Stéphanie Gon"
    },
    {
      "name": "Jonathan Beckwith"
    },
    {
      "name": "Tom Rapoport"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4p4pk9czbzrrs.bib",
  "cited_by": 104,
  "doi": "10.1074/jbc.m413947200",
  "fulltext_url": null,
  "id": "4p4pk9czbzrrs",
  "issns": [
    "0021-9258",
    "1083-351X"
  ],
  "landing_url": "https://hal.science/hal-05843712v1",
  "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.mp"
    ],
    [
      "openalex",
      "1311|Bacterial Genetics and Biotechnology"
    ]
  ],
  "openalex": "W2029394681",
  "pdf_url": "http://www.jbc.org/article/S0021925819629248/pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-29",
  "publisher": "American Society for Biochemistry and Molecular Biology",
  "ris": "https://research.draconitic.com/paper/4p4pk9czbzrrs.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:18:03Z",
      "native_id": "hal-05843712",
      "source": "hal",
      "url": "https://hal.science/hal-05843712v1"
    }
  ],
  "subjects": [
    {
      "field": "biology",
      "origin": "hal:1.sdv.mp",
      "subfield": "microbiology"
    }
  ],
  "title": "The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation",
  "title_text": "The Bacterial ATPase SecA Functions as a Monomer in Protein Translocation",
  "type": "peer-reviewed",
  "updated_at": "2026-10-31T12:20:56Z",
  "url": "https://research.draconitic.com/paper/4p4pk9czbzrrs",
  "venue": "Journal of Biological Chemistry",
  "versions": []
}