RNA-binding properties of the plant protein Nt-4/1

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-b...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2014-07, Vol.79 (7), p.717-726
Main Authors: Makarova, S. S., Solovyev, A. G., Morozov, S. Y.
Format: Article
Language:English
Subjects:
Binding proteins
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Botanical research
DNA - chemistry
Host-Pathogen Interactions
Life Sciences
Microbiology
Mutation
Nicotiana - virology
Physiological aspects
Plant biology
Plant Diseases - virology
Plant pathology
Plant proteins
Plant Proteins - chemistry
Plant Viruses - genetics
Protein Binding
Protein research
Proteins
Ribonucleic acid
RNA
RNA sequencing
RNA, Double-Stranded - chemistry
RNA, Viral - chemistry
RNA-Binding Proteins - chemistry
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Summary: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.
ISSN:0006-2979
1608-3040
DOI:10.1134/S000629791407013X