Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Kwon HY,Eum WS,Jang HW,Kang JH,Ryu J,Ryong Lee B,Jin LH,Park J,Choi SYdoi
10.1016/s0014-5793(00)02215-8keywords:
subject
Has Abstractpub_date
2000-11-24 00:00:00pages
163-7issue
2-3eissn
0014-5793issn
1873-3468pii
S0014-5793(00)02215-8journal_volume
485pub_type
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