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Báo cáo khoa học: Mitochondrial targeting of human peroxiredoxin V protein and regulation of PRDX5 gene expression by nuclear transcription factors controlling biogenesis of mitochondria

Peroxiredoxin V (PRDX5) is a member of the family of mammalian pro-teins that neutralize reactive oxygen species. The PRDX5gene is constitu-tively expressed at a high level in many human tissues, but functional elements of its promoter responsible for a high basal activity in the absence of oxidative stress have still not been identified. | ễFEBS Journal Mitochondrial targeting of human peroxiredoxin V protein and regulation of PRDX5 gene expression by nuclear transcription factors controlling biogenesis of mitochondria Andrey Kropotov1 Nadezhda Usmanova1 Vladimir Serikov2 Boris Zhivotovsky3 and Nikolai Tomilin1 1 Institute of Cytology Russian Academy of Sciences St Petersburg Russia 2 Children s HospitalOakland Research Institute Oakland CA USA 3 Institute of EnvironmentalMedicine Division of Toxicology Karolinska Institutet Stockholm Sweden Keywords antioxidant protein localization mitochondria peroxirerdoxin V transcription Correspondence N. Tomilin Institute of Cytology Russian Academy of Sciences Tikchorestkii Avenue 4 194064 St Petersburg Russia Fax 7 812 2970341 Tel 7 812 2975512 E-mail nvtom@mail.ru Received 25 July 2007 revised 30 August 2007 accepted 11 September 2007 doi 10.1111 j.1742-4658.2007.06103.x Peroxiredoxin V PRDX5 is a member of the family of mammalian proteins that neutralize reactive oxygen species. The PRDX5 gene is constitutively expressed at a high level in many human tissues but functional elements of its promoter responsible for a high basal activity in the absence of oxidative stress have still not been identified. Among predicted binding sites for transcription factors in the human PRDX5 promoter are binding sites for nuclear respiratory factor 1 NFR-1 and nuclear respiratory factor 2 also called GABPA which regulate the biogenesis of mitochondria. We constructed luciferase reporter gene plasmids containing stepwise deletions of the PRDX5 promoter and examined their activities in transient transfections. Our results suggest that basal PRDX5 promoter activity mostly depends on NFR-1 and GABPA sites. The latter in the PRDX5 promoter were conserved in the six mammalian genomes analyzed human chimpanzee cow mouse rat and dog and a fraction of human PRDX5 associates with the mitochondrial matrix. We also found that the N-termi-nal 50 amino acids of the full-length human PRDX5