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Eukaryotic Cell, September 2008, p. 1518-1529, Vol. 7, No. 9
1535-9778/08/$08.00+0     doi:10.1128/EC.00081-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

A Thioredoxin Family Protein of the Apicoplast Periphery Identifies Abundant Candidate Transport Vesicles in Toxoplasma gondii{triangledown} ,{dagger}

Amy E. DeRocher,1 Isabelle Coppens,2 Anuradha Karnataki,1,3 Luke A. Gilbert,4,{ddagger} Michael E. Rome,4 Jean E. Feagin,1,3 Peter J. Bradley,4 and Marilyn Parsons1,3*

Seattle Biomedical Research Institute, 307 Westlake Ave. N., Seattle, Washington 98109,1 Department of Molecular Microbiology and Immunology, Johns Hopkins University Bloomberg School of Public Health, 615 N. Wolfe Street, Baltimore, Maryland 21205,2 Interdisciplinary Program in Pathobiology, Department of Global Health, University of Washington, Seattle, Washington 98195,3 Department of Microbiology, Immunology, and Molecular Genetics, 609 Charles E. Young Dr. East, University of California, Los Angeles, Los Angeles, California 900954

Received 5 March 2008/ Accepted 13 June 2008

Toxoplasma gondii, which causes toxoplasmic encephalitis and birth defects, contains an essential chloroplast-related organelle to which proteins are trafficked via the secretory system. This organelle, the apicoplast, is bounded by multiple membranes. In this report we identify a novel apicoplast-associated thioredoxin family protein, ATrx1, which is predominantly soluble or peripherally associated with membranes, and which localizes primarily to the outer compartments of the organelle. As such, it represents the first protein to be identified as residing in the apicoplast intermembrane spaces. ATrx1 lacks the apicoplast targeting sequences typical of luminal proteins. However, sequences near the N terminus are required for proper targeting of ATrx1, which is proteolytically processed from a larger precursor to multiple smaller forms. This protein reveals a population of vesicles, hitherto unrecognized as being highly abundant in the cell, which may serve to transport proteins to the apicoplast.

* Corresponding author. Mailing address: Seattle Biomedical Research Institute, 307 Westlake Ave. N., Seattle, WA 98109. Phone: (206) 256-7315. Fax: (206) 256-7229. E-mail: marilyn.parsons{at}sbri.org

{triangledown} Published ahead of print on 27 June 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

{ddagger} Present address: MIT Center for Cancer Research, 40 Ames St. E17-123, Cambridge, MA 02142.

Eukaryotic Cell, September 2008, p. 1518-1529, Vol. 7, No. 9
1535-9778/08/$08.00+0     doi:10.1128/EC.00081-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Rome, M. E., Beck, J. R., Turetzky, J. M., Webster, P., Bradley, P. J. (2008). Intervacuolar Transport and Unique Topology of GRA14, a Novel Dense Granule Protein in Toxoplasma gondii. Infect. Immun. 76: 4865-4875 [Abstract] [Full Text]  


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