PLoS ONE (Jan 2012)

Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.

  • Sergey G Guryanov,
  • Olga M Selivanova,
  • Alexey D Nikulin,
  • Gennady A Enin,
  • Bogdan S Melnik,
  • Dmitry A Kretov,
  • Igor N Serdyuk,
  • Lev P Ovchinnikov

DOI
https://doi.org/10.1371/journal.pone.0036969
Journal volume & issue
Vol. 7, no. 5
p. e36969

Abstract

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YB-1, a multifunctional DNA- and RNA-binding nucleocytoplasmic protein, is involved in the majority of DNA- and mRNA-dependent events in the cell. It consists of three structurally different domains: its central cold shock domain has the structure of a β-barrel, while the flanking domains are predicted to be intrinsically disordered. Recently, we showed that YB-1 is capable of forming elongated fibrils under high ionic strength conditions. Here we report that it is the cold shock domain that is responsible for formation of YB-1 fibrils, while the terminal domains differentially modulate this process depending on salt conditions. We demonstrate that YB-1 fibrils have amyloid-like features, including affinity for specific dyes and a typical X-ray diffraction pattern, and that in contrast to most of amyloids, they disassemble under nearly physiological conditions.