YB-1 is capable of forming extended nanofibrils

• Published in: Biochemistry (Moscow) Vol. 75; no. 1; pp. 115 - 120
• Main Authors: Selivanova, O. M., Guryanov, S. G., Enin, G. A., Skabkin, M. A., Ovchinnikov, L. P., Serdyuk, I. N.
• Format: Journal Article
• Language: English
• Published: Dordrecht SP MAIK Nauka/Interperiodica 2010; Springer; Springer Nature B.V
• Subjects: Accelerated Publication; Amyloid - chemistry; Amyloid - ultrastructure; Atomic force microscopy; Binding sites; Biochemistry; Biomedical and Life Sciences; Biomedicine; Bioorganic Chemistry; Humans; Ions; Life Sciences; Lithium Chloride - chemistry; Microbiology; Microscopy, Atomic Force; Osmolar Concentration; Protein Binding; Proteins; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification; Time Factors; Transmission electron microscopy; Y-Box-Binding Protein 1 - chemistry; Y-Box-Binding Protein 1 - genetics; Y-Box-Binding Protein 1 - isolation & purification; electron microscopy; protein fibrils; YB-1; high ionic strength; atomic force microscopy
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297910010153

Here we are the first to report that multifunctional Y-box binding protein 1 (YB-1) forms extended fibrils with a diameter of 15–20 nm. The YB-1 fibrils were visualized by atomic force and electron microscopy after 1-h incubation in solution with 2 M LiCl. Their length grew with incubation time and could exceed 10 μm; their shape is helical or zigzag-like. They possess polarity and tend to associate with one another to give structures of a higher order, like ribbons or bundles. The YB-1 fibrillar architecture has a distinct periodicity with a repeat unit of about 52 nm.