Molecular Characterization and Expression of CuZn-superoxide Dismutase (PSOD1) from Populus alba${\times}$Populus glandulosa

  • Lee Jun-Won (Biopia Co., Ltd.) ;
  • In Jun-Gyo (Department of Oriental Medicinal Materials and Processing, Kyung Hee University) ;
  • Lee Bum-Soo (Department of Oriental Medicinal Materials and Processing, Kyung Hee University) ;
  • Choi Yong-Eui (Division of Forest Resources, Kangwon National University) ;
  • Kim Jin-Ju (Division of Forest Resources, Kangwon National University) ;
  • Yang Deok-Chun (Department of Oriental Medicinal Materials and Processing, Kyung Hee University)
  • Published : 2005.04.01

Abstract

A cDNA, PSOD1, encoding cytosolic copper/zinc superoxide dismutase (CuZn-SOD) was cloned and characterized from a full length cDNA library prepared from Populus alba${\times}$Populus glandulosa cultured in vitro. A PSOD1, is 725 nucleotides long and has an open reading frame of 459 bp with 152 amino acid residues (pI 5.43). The deduced amino acid sequence of PSOD1 perfect matched to the previously reported CuZn-SOD (CAC33845.1). Consensus amino acid residues (His-45, -47, -62, -70, -79, -119) were involved in Cu-, Cu/Zn-, and Zn- binding ligands. The deduced amino acid sequence of PSOD1 exhibited the high level of similarity from 100 to $85\%$ among previously registered SOD genes. The expression of PSOD1 in poplar increased at the 1 mM $H_{2}O_2$ and drought stress during 30 min and 60 min, but the ozone treated poplar increased at 30 min in the early time and then decreased at 60 min.

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