Transduction of Cu,Zn-superoxide dismutase mediated by an HIV-1 Tat protein basic domain into mammalian cells

Hyeok Yil Kwon, Won Sik Eum, Hyun Woo Jang, Jung Hoon Kang, Jiyoon Ryu, Byung Ryong Lee, Li Hua Jin, Jinseu Park, Soo Young Choi

Research output: Contribution to journalArticlepeer-review

126 Scopus citations


A human Cu,Zn-superoxide dismutase (Cu,Zn-SOD) gene was fused with a gene fragment encoding the nine amino acid transactivator of transcription (Tat) protein transduction domain (RKKRRQRRR) of HIV-1 in a bacterial expression vector to produce a genetic in-frame Tat-SOD fusion protein. The expressed and purified Tat-SOD fusion protein in Escherichia coli can enter HeLa cells in a time- and dose-dependent manner when added exogenously in a culture media. Denatured Tat-SOD protein was transduced much more efficiently into cells than were native proteins. Once inside the cells, transduced Tat-SOD protein was enzymatically active and stable for 24 h. The cell viability of HeLa cells treated with paraquat, an intracellular superoxide anion generator, was increased by transduced Tat-SOD. These lines of results suggest that the transduction of Tat-SOD fusion protein may be one of the ways to replenish the Cu,Zn-SOD in the various disorders related to this antioxidant enzyme. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)163-167
Number of pages5
JournalFEBS Letters
Issue number2-3
StatePublished - Nov 24 2000
Externally publishedYes


  • Copper,zinc-superoxide dismutase
  • Human immunodeficiency virus type 1 transactivator of transcription
  • Transduction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Transduction of Cu,Zn-superoxide dismutase mediated by an HIV-1 Tat protein basic domain into mammalian cells'. Together they form a unique fingerprint.

Cite this