Molecular and structural-biological analysis of Nicotiana plumbaginifolia mutants for identification of the site on their β-tubulins of interaction with dinitroanilines and phosphorothioamides
Tóm tắt
The identification of the location of a point mutation on β-tubulin molecules of amiprophosmethyland trifluralin-resistant Nicotiana plumbaginifolia lines are described in this work. It was shown that in the first case, this mutation is related with the substitution of serine residue for proline in position 248; in the second case, with the substitution of phenylalanine for serine in position 317 of the β-tubulin’s amino acid sequence. Three-dimensional models of the β-tubulin molecule from Chlamydomonas with the well-known location of mutations determining dinitroaniline- and phosphorothioamides resistance (the substitution of lysine residue for methionine in position 350), and β-tubulin from Nicotiana plumbagnifolia have been reconstructed. On the basis of the analysis of the interaction site for dinitroanilines and phosphorothioamides located on the Chlamydomonas β-tubulin’s molecule it was concluded that the revealed mutations on Nicotiana plumbaginifolia β-tubulin are affected by the residues of the amino acids, participating in the formation of this site.
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