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Updated: Apr 26, 2026

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
RNA-binding properties of the plant protein Nt-4/1
S S Makarova1, A G Solovyev, S Y Morozov
1Lomonosov Moscow State University, Biological Faculty, Moscow, 119234, Russia. info@mail.bio.msu.ru.
Abstract:
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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