{"entity": "publication", "iuid": "e2e9056a5bb24db69ccda270bfc87261", "timestamp": "2026-03-16T18:24:55.216Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/e2e9056a5bb24db69ccda270bfc87261.json"}, "display": {"href": "https://publications.scilifelab.se/publication/e2e9056a5bb24db69ccda270bfc87261"}}, "title": "Assembly mechanisms of the bacterial cytoskeletal protein FilP.", "authors": [{"family": "Javadi", "given": "Ala", "initials": "A", "orcid": "0000-0003-2522-4759", "researcher": {"href": "https://publications.scilifelab.se/researcher/59463007a2894b68b0dde8acccbd7cfb.json"}}, {"family": "S\u00f6derholm", "given": "Niklas", "initials": "N", "orcid": "0000-0003-3964-3751", "researcher": {"href": "https://publications.scilifelab.se/researcher/ff74d1308e044d7f81ddbe1eb73cfd9c.json"}}, {"family": "Olofsson", "given": "Annelie", "initials": "A"}, {"family": "Fl\u00e4rdh", "given": "Klas", "initials": "K"}, {"family": "Sandblad", "given": "Linda", "initials": "L", "orcid": "0000-0003-3492-3287", "researcher": {"href": "https://publications.scilifelab.se/researcher/070825e0190a4e9a932e79663d2bc89f.json"}}], "type": "journal article", "published": "2019-06-00", "journal": {"volume": "2", "issn": "2575-1077", "issue": "3", "pages": "e201800290", "title": "Life Sci. Alliance", "issn-l": "2575-1077"}, "abstract": "Despite low-sequence homology, the intermediate filament (IF)-like protein FilP from Streptomyces coelicolor displays structural and biochemical similarities to the metazoan nuclear IF lamin. FilP, like IF proteins, is composed of central coiled-coil domains interrupted by short linkers and flanked by head and tail domains. FilP polymerizes into repetitive filament bundles with paracrystalline properties. However, the cations Na+ and K+ are found to induce the formation of a FilP hexagonal meshwork with the same 60-nm repetitive unit as the filaments. Studies of polymerization kinetics, in combination with EM techniques, enabled visualization of the basic building block-a transiently soluble rod-shaped FilP molecule-and its assembly into protofilaments and filament bundles. Cryoelectron tomography provided a 3D view of the FilP bundle structure and an original assembly model of an IF-like protein of prokaryotic origin, thereby enabling a comparison with the assembly of metazoan IF.", "doi": "10.26508/lsa.201800290", "pmid": "31243049", "labels": {"Cryo-EM": "Collaborative"}, "xrefs": [{"db": "pii", "key": "2/3/e201800290"}, {"db": "pmc", "key": "PMC6599971"}], "notes": [], "created": "2020-01-08T08:09:07.158Z", "modified": "2021-06-21T10:01:55.898Z"}