{"entity": "publication", "iuid": "814bc0f2347147d09206e9eaeb1977f8", "timestamp": "2026-09-12T20:10:56.076Z", "links": {"self": {"href": "https://publications.scilifelab.se/publication/814bc0f2347147d09206e9eaeb1977f8.json"}, "display": {"href": "https://publications.scilifelab.se/publication/814bc0f2347147d09206e9eaeb1977f8"}}, "title": "Affinity to cellulose is a shared property among coiled-coil domains of intermediate filaments and prokaryotic intermediate filament-like proteins.", "authors": [{"family": "S\u00f6derholm", "given": "Niklas", "initials": "N"}, {"family": "Javadi", "given": "Ala", "initials": "A"}, {"family": "Flores", "given": "Isabel Sierra", "initials": "IS"}, {"family": "Fl\u00e4rdh", "given": "Klas", "initials": "K", "orcid": "0000-0002-7131-9743", "researcher": {"href": "https://publications.scilifelab.se/researcher/bfd785cebfc64364b2c4206a568c8681.json"}}, {"family": "Sandblad", "given": "Linda", "initials": "L", "orcid": "0000-0003-3492-3287", "researcher": {"href": "https://publications.scilifelab.se/researcher/070825e0190a4e9a932e79663d2bc89f.json"}}], "type": "journal article", "published": "2018-11-08", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "8", "issue": "1", "pages": "16524", "issn-l": "2045-2322"}, "abstract": "Coiled-coil domains of intermediate filaments (IF) and prokaryotic IF-like proteins enable oligomerisation and filamentation, and no additional function is ascribed to these coiled-coil domains. However, an IF-like protein from Streptomyces reticuli was reported to display cellulose affinity. We demonstrate that cellulose affinity is an intrinsic property of the IF-like proteins FilP and Scy and the coiled-coil protein DivIVA from the genus Streptomyces. Furthermore, IF-like proteins and DivIVA from other prokaryotic species and metazoan IF display cellulose affinity despite having little sequence homology. Cellulose affinity-based purification is utilised to isolate native FilP protein from the whole cell lysate of S. coelicolor. Moreover, cellulose affinity allowed for the isolation of IF and IF-like protein from the whole cell lysate of C. crescentus and a mouse macrophage cell line. The binding to cellulose is mediated by certain combinations of coiled-coil domains, as demornstrated for FilP and lamin. Fusions of target proteins to cellulose-binding coiled-coil domains allowed for cellulose-based protein purification. The data presented show that cellulose affinity is a novel function of certain coiled-coil domains of IF and IF-like proteins from evolutionary diverse species.", "doi": "10.1038/s41598-018-34886-7", "pmid": "30410115", "labels": {"Cryo-EM": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41598-018-34886-7"}, {"db": "pmc", "key": "PMC6224456"}], "notes": [], "created": "2019-01-10T21:17:58.974Z", "modified": "2021-07-05T17:20:56.117Z"}