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    • Keywords


      Adaptive evolution; hemopexin; Ka/Ks; MMP-'9; positive selection

    • Abstract


      Matrix metalloproteinases-9 (MMP-9) is an important cancer-associated, zinc-dependent endopeptidase. To investigate the natural selection hypothesis of MMP-9, the orthologous sequences from 12 vertebrates were compared and a molecular evolution analysis was performed. Results suggest that amino acid residues present in the middle region of the protein are more selectively constrained, whereas amino acid residues in the C-terminal region of the MM~P-9 protein including exon 13 showed lowest conservation level in non-primate species, suggesting that it is an exon with fast evolving rate compared to the others analyzed. InterProScan analysis shows that exon 13 was located in hemopexin (PEX) domain of MM~P-9. Positive selection was detected in PEX domain of MMP-9 protein between human and other species, which indicates that selective pressure may play a role in shaping the function of MM~P-9 in the course of evolution.

    • Author Affiliations


      Yang Liu1 Yang Zhao2 Chunlei Lu3 Maobin Fu2 Tonghai Dou2 Xiaoming Tan4

      1. Shanghai Institute of Quah.t.v Inspection and Techm.cal Research/National Quah.t.v Supervision and Inspection Center for Food Products (Shanghai), Shanghai 200233, People's Republic of China
      2. Department of Microbiology and Microbial Engineering, School of Life Science, Fudan Urn.versit.v, Shanghai 200433, People s Republic of China
      3. Department of Laparoscopic Surgery, Shandong Urn.versity, Linyi People Hospital, Linyi, Shandong Province, People's Republic of China
      4. Department of Respiratory Disease, The Southern Division of Renji Hospital, School of Medicine, Shanghai Jiao Tong Urn.versit.v, Shanghai 201112, People's Republic of China
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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