Y. M. Konstantinov, E. L. Tauson, D. S. Verbitski, o. Ya. Dichenko, A. Sh. Arziev. Identification of highly conserved hydrophobic aminoacid motif in deduced amino acid sequenceof elymus sibiricus l. mitochondrial s13 ribosomal protein. // Journal of General Biology. 2000. V. 61. Number 2.

Siberian Branch of Russian Academy of Science, Siberian Institute of Plant Physiology and Biochemistry, P.O. Box 1243, 664033 Irkutsk

Abstract

The nucleotide sequence of mitochondrial ribosomal protein rpsl3 gene from wildperennial grass Elymus sibiricus is presented. It was determined by the method of PCRamplification with specific oligonucleotide primers and the direct sequencing of theamplification product. The sequence of E. sibiricus mitochondrial gene for S13 predicts ahydrophobic ribosomal protein of 116 amino acids that shows strong similarity to those ofwheat (99, 7% identity) and maize (98%). The deduced amino acid sequence of S13 proteinfrom E. sibiricus and homologous plant's (Zea mays, Daucus carota, Nicotiana tabacum, Marchantia polymorpha) and nonplant's (Escherichia coli) proteins shows the presence ofhydrophobic amino acids' motif -L-X1O-L-X1O-M-X1O-L-X1O-L-. Slightly modified it canbe found in many other ribosomal proteins. This conserved motif is presumed to beparticularly important for association of the ribosomal S13 protein with other proteins in thesmall subunit of the mitochondrial ribosome.