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Identification of cDNAS encoding plastid‐targeted glutathione peroxidase
Author(s) -
Mullineaux Philip M.,
Karpinski Stanislaw,
Jiménez Ana,
Cleary Suzanne P.,
Robinson Colin,
Creissen Gary P.
Publication year - 1998
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1998.00052.x
Subject(s) - chloroplast , phospholipid hydroperoxide glutathione peroxidase , plastid , complementary dna , chloroplast stroma , transit peptide , biology , biochemistry , arabidopsis , microbiology and biotechnology , enzyme , gene , glutathione , glutathione peroxidase , thylakoid , mutant
Summary A cDNA was isolated from pea leaf RNA which encodes a phospholipid hydroperoxide glutathione peroxidase (PHGPX; E.C. 1.1.1.1.9). The N‐terminal section of this PHGPX encodes a recognisable chloroplast transit peptide. Efficient import in vitro of the pre‐PHGPX protein into the stroma of isolated pea chloroplasts confirmed that the PHGPX is a chloroplast‐located enzyme. The pea PHGPX has highly conserved homologues in Arabidopsis , citrus and Nicotiana sylvestris and the authors suggest that these proteins are also localised in the chloroplast and not in the cytosol as previously supposed.