Abstract: Ribosomal protein S13 (RPS13) is a key member of the ribosomal protein family, and plays an important role in the ribosome. In this study, total RNA was isolated from roots, stems and leaves of Cnidium monnieri (L.) Cuss. RT-PCR was used to obtain an open reading frame（ORF）of the rps13 which encoded 151 amino acid polypeptide; the target gene was cloned to pET22b(+) vector, then the recombinant plasmid was transformed into E. coli BL21 competent cells, and the fusion protein was expressed with induction of isopropyl β-D-1-thiogalactopyranoside (IPTG) and identified by Western Blotting. The three dimensional structure models showed that RPS13 contained six helices and the whole molecule appeared as a spiral structure with two clusters of helices connected by a long random coil, which may help to maintain the dynamic bridging interactions between the large and small subunits of ribosome. The phylogenetic analysis showed that the RPS13 of Cnidium monnieri (L.) Cuss. was highly conserved in evolution and most closely related to RPS13 of carrot. Expression and bioinformatics analysis of the RPS13 lay a foundation for the further study of its biological function.

Key words: Cnidium monnieri (L.) Cuss., ribosomal protein S13, protein expression, bioinformatics analysis