RNA-Binding Properties of the Plant Protein Nt-4/1

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S. S. Makarova^1*, A. G. Solovyev², and S. Y. Morozov²

¹Lomonosov Moscow State University, Biological Faculty, 119234 Moscow, Russia; fax: (495) 939-4309; E-mail: info@mail.bio.msu.ru

²Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, 119992 Moscow, Russia; fax: (495) 939-0338; E-mail: fxb@genebee.msu.su

^* To whom correspondence should be addressed.

Received January 29, 2014; Revision received April 7, 2014

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The tobacco α-helical protein Nt-4/1 with unknown function forms ribonucleoprotein (RNP) complexes in vitro. Results obtained by retardation of RNP complexes in agarose gel were confirmed by Western–Northern hybridization. Several deletion and point mutants of Nt-4/1 were constructed, and the RNA-binding site was mapped in a positively charged region of the C-terminal domain of the protein. The results of this study and those described earlier support our hypothesis of the participation of Nt-4/1 protein in spreading RNA-containing pathogens in the plant.

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KEY WORDS: protein Nt-4/1, potato spindle tuber viroid, RNA binding

DOI: 10.1134/S000629791407013X

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