Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Isolation and Sequence Analysis of Two Ornithine Decarboxylase Antizyme Genes from Flounder (Paralichthys olivaceus)

  • LEE JAE HYUNG (Department of Microbiology, Pukyong National University) ;
  • SEO YONG BAE (Department of Microbiology, Pukyong National University) ;
  • YOON MOON YOUNG (Department of Chemistry, Hanyang University) ;
  • CHOI JUNG DO (Department of Life Sciences, Chungbuk National University) ;
  • KIM YOUNG TAE (Department of Microbiology, Pukyong National University)
  • Published : 2005.04.01
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Abstract

Ornithine decarboxylase (ODC) antizyme is a key regulatory protein in the control of cellular polyamines. We have isolated two distinct ODC antizyme cDNA clones (AZS and AZL) from a flounder (Paralichthys olivaceus) brain cDNA library. Their sequences revealed that both clones required translational frameshifting for expression. Taking + 1 frameshifting into account, AZS and AZL products were 221 and 218 amino acid residues long, respectively, and shared $83.3\%$ amino acid sequence identity. Comparison of the structure and nucleotide sequence of the antizyme genes showed that the genes were highly conserved in flounder, zebrafish, mouse, and human. A phylogenetic tree was constructed, based on the antizyme amino acid sequences from various species. The presence of the two types of antizyme mRNA species in brain, kidney, liver, and embryo was confirmed by using the reverse transcription­polymerase chain reaction (RT-PCR) and Northern blot analysis. Recombinant proteins of flounder ODC antizymes, containing His-Nus-S tag at the amino-terminus, were overexpressed as His-AZL and His-AZS fusion proteins in Escherichia coli BL21 (DE3) pLys by using the pET­44a(+) expression vector.

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