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YB-1 is capable of forming extended nanofibrils

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Abstract

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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Abbreviations

AFM:

atomic force microscopy

CSD:

cold shock domain

EM:

electron microscopy

HOPG:

highly ordered pyrolytic graphite

YB-1:

Y-box binding protein 1

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Authors and Affiliations

  1. Institute of Protein Research, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia

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

Authors
  1. O. M. Selivanova
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  2. S. G. Guryanov
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  3. G. A. Enin
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  4. M. A. Skabkin
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  5. L. P. Ovchinnikov
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  6. I. N. Serdyuk
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Corresponding author

Correspondence to I. N. Serdyuk.

Additional information

Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM09-351, December 20, 2009.

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Selivanova, O.M., Guryanov, S.G., Enin, G.A. et al. YB-1 is capable of forming extended nanofibrils. Biochemistry Moscow 75, 115–120 (2010). https://doi.org/10.1134/S0006297910010153

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  • DOI: https://doi.org/10.1134/S0006297910010153

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