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J. Biol. Chem., Vol. 275, Issue 27, 20346-20354, July 7, 2000
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From the Peroxidases of the peroxiredoxin (Prx) family
contain a Cys residue that is preceded by a conserved sequence in the
NH2-terminal region. A new type of mammalian Prx,
designated PrxV, has now been identified as the result of a data base
search with this conserved Cys-containing sequence. The 162-amino acid
PrxV shares only ~10% sequence identity with previously identified
mammalian Prx enzymes and contains Cys residues at positions 73 and 152 in addition to that (Cys48) corresponding to the conserved
Cys. Analysis of mutant human PrxV proteins in which each of these
three Cys residues was individually replaced with serine suggested that
the sulfhydryl group of Cys48 is the site of oxidation by
peroxides and that oxidized Cys48 reacts with the
sulfhydryl group of Cys152 to form an intramolecular
disulfide linkage. The oxidized intermediate of PrxV is thus distinct
from those of other Prx enzymes, which form either an intermolecular
disulfide or a sulfenic acid intermediate. The disulfide formed by PrxV
is reduced by thioredoxin but not by glutaredoxin or glutathione. Thus,
PrxV mutants lacking Cys48 or Cys152 showed no
detectable thioredoxin-dependent peroxidase activity, whereas mutation of Cys73 had no effect on activity.
Immunoblot analysis revealed that PrxV is widely expressed in rat
tissues and cultured mammalian cells and is localized intracellularly
to cytosol, mitochondria, and peroxisomes. The peroxidase function of
PrxV in vivo was demonstrated by the observations that
transient expression of the wild-type protein, but not that of the
Cys48 mutant, in NIH 3T3 cells inhibited
H2O2 accumulation and activation of c-Jun
NH2-terminal kinase induced by tumor necrosis
factor-
Identification of a New Type of Mammalian Peroxiredoxin That
Forms an Intramolecular Disulfide as a Reaction Intermediate*
§¶,§,
,, and§§
Laboratory of Cell Signaling and
** Department of Extramural Affairs, NHLBI, National Institutes of
Health, Bethesda, Maryland 20892 and the Department of Food
and Nutrition, Chonnam National University,
Kwangju 500-757, Korea
.
*
This work was supported in part by a grant (to K. K.) from
the Korea Science and Engineering Foundation through the Center for
Cell Signaling Research of Ewha Women's University.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Korea Research Institute of Bioscience and
Biotechnology, Yusong, Taejon 305-600, Korea.
§§
To whom correspondence should be addressed: Bldg. 3, Rm. 120, National Institutes of Health, Bethesda, MD 20892. Tel.: 301-496-9646; Fax: 301-480-0357; E-mail: rheesg@nhlbi.nih.gov.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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