Abstract
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.
Highlights
Y-Box Binding Protein 1 (YB-1) is a multifunctional nucleocytoplasmic protein that interacts with both RNA and DNA
We found that fibril formation by YB-1 is mediated by its cold shock domain (CSD), while different regions of its disordered terminal domains differentially contribute to the process
We have shown that YB-1 fibrils are amyloid-like, but this structure is reversible and disassembles under physiological conditions
Summary
YB-1 is a multifunctional nucleocytoplasmic protein that interacts with both RNA and DNA. YB-1 mediates mRNA localization on tubulin [1,2] and actin [3] cytoskeletons. It can be found in stress granules [4], P-bodies [5] and centrosomes [6,7]. YB-1 is involved in regulation of transcription [8,9] and translation [10,11], alternative splicing [12,13], DNA reparation, gene-toxic stress response, and development of multidrug resistance [14]. For a comprehensive review of YB-1 functions, see [23]
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