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Identification of cDNAS encoding plastid-targeted glutathione peroxidase

  1. Philip M. Mullineaux,
  2. Stanislaw Karpinski,
  3. Ana Jiménez,
  4. Suzanne P. Cleary,
  5. Colin Robinson,
  6. Gary P. Creissen

Article first published online: 21 APR 2002

DOI: 10.1046/j.1365-313X.1998.00052.x

Issue

The Plant Journal

The Plant Journal

Volume 13, Issue 3, pages 375–379, February 1998

Additional Information

How to Cite

Mullineaux, P. M., Karpinski, S., Jiménez, A., Cleary, S. P., Robinson, C. and Creissen, G. P. (1998), Identification of cDNAS encoding plastid-targeted glutathione peroxidase. The Plant Journal, 13: 375–379. doi: 10.1046/j.1365-313X.1998.00052.x

Author Information

  1. 11John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK,, 22Department of Forest Genetics and Plant Physiology, Faculty of Forestry, Swedish University of Agricultural Sciences, S-90183 Umeå, Sweden,, 33Department de Nutrición y Fisiología Vegetal, Centro de Edafología y Biología Aplicada del Segura, Consejo Superior de Investigaciones Cientificas (CSIC), Apdo. 195, E-30080 Murcia, Spain, and, 44Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK

*Glutathione peroxidase in chloroplasts

Publication History

  1. Issue published online: 21 APR 2002
  2. Article first published online: 21 APR 2002

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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.

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