Glutaredoxin 1 from Evolutionary Ancient Hydra: Characteristics of the Enzyme and Its Possible Functions in Cell

AbstractGlutaredoxin (Grx) is an antioxidant redox protein that uses glutathione  (GSH) as an electron donor. Grx plays a crucial role in various cellular processes, such as antioxidant defense, control of cellular redox state, redox control of transcription, reversible S-glutathionylation of specific proteins, apoptosis, cell differentiation, etc. In the current study, we have isolated and characterized dithiol glutaredoxin fromHydra vulgaris Ind-Pune (HvGrx1). Sequence analysis showed thatHvGrx1 belongs to the Grx family with the classical Grx motif (CPYC). Phylogenetic analysis and homology modeling revealed thatHvGrx1 is closely related to Grx2 from zebrafish.HvGrx1 gene was cloned and expressed inEscherichia coli cells; the purified protein had a molecular weight of 11.82  kDa.HvGrx1 efficiently reducedβ-hydroxyethyl disulfide (HED) with the temperature optimum of 25 °C and pH optimum 8.0.HvGrx1 was ubiquitously expressed in all body parts ofHydra. Expression ofHvGrx1 mRNA and enzymatic activity ofHvGrx1 were significantly upregulated post H2O2 treatment. When expressed in human cells,HvGrx1 protected the cells from oxidative stress and enhanced cell proliferation and migration. AlthoughHydra is a simple invertebrate,HvGrx1 is evolutionary closer to its homologs from higher vertebrates (similar to many otherHydra proteins).
Source: Biochemistry (Moscow) - Category: Biochemistry Source Type: research