YB-1 Is Capable of Forming Extended Nanofibrils

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O. M. Selivanova, S. G. Guryanov, G. A. Enin, M. A. Skabkin, L. P. Ovchinnikov, and I. N. Serdyuk^*

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; E-mail: serdyuk@vega.protres.ru

^* To whom correspondence should be addressed.

Received December 4, 2009

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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.

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KEY WORDS: YB-1, protein fibrils, atomic force microscopy, electron microscopy, high ionic strength

DOI: 10.1134/S0006297910010153

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