Purification and Characterization of a Second Type Thioredoxin Peroxidase (Type II TPx) from <i>Saccharomyces cerevisiae</i>

Jeong, Jin Sook; Kwon, Soo Jin; Kang, Sang Won; Rhee, Sue Goo; Kim, Kanghwa

doi:10.1021/bi9817818

Cited by 109 publications

(111 citation statements)

References 21 publications

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“…Tsa1p and Tsa2p are thiol peroxidases, which are known to eliminate H 2 O 2 and alkyl hydroperoxides by using thiol-reducing equivalents (33,34). ⌬tsa1,2 has been shown earlier to be more sensitive toward H 2 O 2 when compared with wt (24).…”

Section: Discussionmentioning

confidence: 99%

Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes

Bienert

Møller

Kristiansen

et al. 2007

Journal of Biological Chemistry

1,164

775

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The metabolism of aerobic organisms continuously produces reactive oxygen species. Although potentially toxic, these compounds also function in signaling. One important feature of signaling compounds is their ability to move between different compartments, e.g. to cross membranes. Here we present evidence that aquaporins can channel hydrogen peroxide (H 2 O 2 ). Twenty-four aquaporins from plants and mammals were screened in five yeast strains differing in sensitivity toward oxidative stress. Expression of human AQP8 and plant Arabidopsis TIP1;1 and TIP1;2 in yeast decreased growth and survival in the presence of H 2 O 2 . Further evidence for aquaporin-mediated H 2 O 2 diffusion was obtained by a fluorescence assay with intact yeast cells using an intracellular reactive oxygen species-sensitive fluorescent dye. Application of silver ions (Ag ؉ ), which block aquaporin-mediated water diffusion in a fast kinetics swelling assay, also reversed both the aquaporindependent growth repression and the H 2 O 2 -induced fluorescence. Our results present the first molecular genetic evidence for the diffusion of H 2 O 2 through specific members of the aquaporin family.Hydrogen peroxide (H 2 O 2 ) 2 belongs to the group of reactive oxygen species (ROS). ROS are generated in a number of key metabolic processes in cells like the electron transport chain in the inner mitochondrial membrane (1) and, specific for plants, the chloroplast thylakoid membrane (2).Because ROS can potentially damage proteins, lipids, and nucleic acids, cells have a number of ROS-scavenging systems that are able to remove these molecules and to maintain a relatively low and constant ROS concentration (3). However, ROS are also intermediates in various signal transduction pathways and have been shown to initiate responses to various stresses and disorders (for recent reviews, see Refs. 4 and 5). Arabidopsis mutants lacking an NADPH oxidase were not able to respond adequately to potassium deficiency (6) and were impaired in stomatal closure (7), providing genetic evidence for a role of NADPH oxidase in signaling.ROS are interconvertible molecules including singlet oxygen, superoxide, hydroxyl radical, and H 2 O 2 . H 2 O 2 has a distinctive set of features compared with other ROS. (i) It is not charged, (ii) it is not a radical, (iii) it possesses an intermediate oxidation number, (iv) it is relatively stable under physiological conditions, and (v) catalase can disproportionate it into water and molecular oxygen without the expense of reduction equivalents.Although substantial progress has been made regarding the formation and scavenging of ROS, little is known about their transport from the site of origin to the place of action or detoxification. Recently three studies from mammalian systems have provided evidence that H 2 O 2 , in addition to the well studied role in intracellular signaling, is also used as an intercellular signal molecule (8 -10). This implies that a necessary step within these signal transduction pathways is the transport of H 2 O 2 ...

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Section: Discussionmentioning

confidence: 99%

Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes

Bienert

Møller

Kristiansen

et al. 2007

Journal of Biological Chemistry

1,164

775

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“…The amino acid residues showing consensus value above 90% and 50% are in upper case and lower case, respectively. nomenclature is still used for yeast enzymes because all yeast Prx enzymes known to date are receiving the reducing equivalents from Trx (15,27 ).…”

Section: General Properties Of Prx Enzymesmentioning

confidence: 99%

“…Yeast contains a Prx V homolog, initially named type II TPx (15) and now renamed cTPx III because of its cytosolic localization (27 ). cTPx III was puri ed based on its capacity to reduce alkylhydroperoxide s preferentially over H 2 O 2 (15).…”

Section: Atypical 2-cys Prx Subgroup Membersmentioning

confidence: 99%

“…cTPx III was puri ed based on its capacity to reduce alkylhydroperoxide s preferentially over H 2 O 2 (15). The amino acid sequence of 176 amino acids of cTPx III revealed no substantial homology to that of the 195 residues of cTPx I with the exception of a short segment preceding the catalytic site Cys62 of cTPx III, but showed 30% sequence identity to mammalian Prx V. Although, like mammalian Prx V, cTPx III contains two additional cysteine residues at positions 31 and 120, these two Cys residues do not correspond to Cys73 and Cys152 of Prx V. The reaction intermediate of cTPx III appears to be different from that of mammalian Prx V: The oxidized Cys62 of cTPx III reacts with the Cys120-SH group of another cTPx III molecule to form an intermolecular disul de linkage (15). The resulting disul de can then be reduced by Trx, but not by GSH.…”

Section: Atypical 2-cys Prx Subgroup Membersmentioning

confidence: 99%

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Peroxiredoxin, a Novel Family of Peroxidases

Kang²,

et al. 2001

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“…Finally, Prx Q was identified initially in Sedum lineare as a homolog of the Escherichia coli bacterioferritin co-migratory protein [3]. Among the four groups, the type II Prxs are the least studied with respect to peroxidase activity, although it has recently been observed in yeast [9,10], Arabidopsis [6,9,11], poplar [4], and Chinese cabbage [12]. At least in Arabidopsis, the type II Prx is complex and composed of several different members.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of a Type II Peroxiredoxin Gene from Panax ginseng C. A. Meyer

Kim¹,

Lee²,

Lee³

et al. 2010

Journal of Ginseng Research

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A peroxiredoxin cDNA (PgPrx) was isolated and characterized from the leaves of Panax ginseng. The cDNA is 716 nucleotides long and has an open reading frame of 489 base pairs with a deduced amino acid sequence of 162 residues. The calculated molecular mass of the mature protein is approximately 17.4 kDa with a predicted isoelectric point of 5.37. A GenBank BlastX search revealed that the deduced amino acid sequence of PgPrx shares a high degree homology with type II peroxiredoxin (Prx) proteins in other plants. The PgPrx gene was highly expressed in leaves, and expressed at a low level in the stem. To analyze the gene expression of PgPrx in response to various abiotic stresses, we utilized real-time quantitative RT-PCR. Our results reveal that PgPrx expression is induced by ultraviolet irradiation, low temperature, and salt. The induction of PgPrx in response to abiotic stimuli suggests that ginseng Prx may function to protect the host against environmental stresses.

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Purification and Characterization of a Second Type Thioredoxin Peroxidase (Type II TPx) from Saccharomyces cerevisiae

Cited by 109 publications

References 21 publications

Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes

Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes

Peroxiredoxin, a Novel Family of Peroxidases

Isolation and Characterization of a Type II Peroxiredoxin Gene from Panax ginseng C. A. Meyer

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