title: RNA-binding properties of the plant protein Nt-4/1.
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.
authors.affiliation: Lomonosov Moscow State University, Biological Faculty, Moscow, 119234, Russia. info@mail.bio.msu.ru.
authors.forename: S S
authors.initials: SS
authors.lastname: Makarova
authors.forename: A G
authors.initials: AG
authors.lastname: Solovyev
authors.forename: S Y
authors.initials: SY
authors.lastname: Morozov
mesh_terms: D004247:DNA / Q000737:chemistry; D054884:Host-Pathogen Interactions; D010935:Plant Diseases / Q000821:virology; D010940:Plant Proteins / Q000737:chemistry*; D010942:Plant Viruses / Q000235:genetics; D011485:Protein Binding; D012330:RNA, Double-Stranded / Q000737:chemistry*; D012367:RNA, Viral / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry*; D014026:Nicotiana / Q000821:virology
chemical_list: D010940:Plant Proteins; D012330:RNA, Double-Stranded; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D004247:DNA