Affinity to cellulose is a shared property among coiled-coil domains of intermediate filaments and prokaryotic intermediate filament-like proteins

Sci Rep. 2018 Nov 8;8(1):16524. doi: 10.1038/s41598-018-34886-7.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacteria / chemistry
  • Bacteria / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Cell Cycle Proteins / chemistry
  • Cell Cycle Proteins / metabolism
  • Cell Line
  • Cellulose / metabolism*
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism
  • Intermediate Filaments / chemistry*
  • Intermediate Filaments / metabolism*
  • Macrophages / cytology
  • Macrophages / metabolism*
  • Mass Spectrometry
  • Mice
  • Protein Binding
  • Protein Domains
  • Sequence Homology
  • Streptomyces coelicolor / chemistry
  • Streptomyces coelicolor / metabolism


  • Bacterial Proteins
  • Cell Cycle Proteins
  • DivIVA protein, bacteria
  • Cellulose