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Eukaryotic Cell, July 2005, p. 1211-1220, Vol. 4, No. 7
1535-9778/05/$08.00+0     doi:10.1128/EC.4.7.1211-1220.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Functional Characterization of an Evolutionarily Distinct Phosphopantetheinyl Transferase in the Apicomplexan Cryptosporidium parvum{dagger}

Xiaomin Cai,1 Dustin Herschap,1 and Guan Zhu1,2*

Department of Veterinary Pathobiology, College of Veterinary Medicine,1 Faculty of Genetics Program, Texas A&M University, 4467 TAMU, College Station, Texas 77840-44672

Received 20 March 2005/ Accepted 9 May 2005

Recently, two types of fatty acid synthases (FASs) have been discovered from apicomplexan parasites. Although significant progress has been made in characterizing these apicomplexan FASs, virtually nothing was previously known about the activation and regulation of these enzymes. In this study, we report the discovery and characterization of two distinct types of phosphopantetheinyl transferase (PPTase) that are responsible for synthesizing holo-acyl carrier protein (ACP) from three apicomplexan parasites: surfactin production element (SFP) type in Cryptosporidium parvum (CpSFP-PPT), holo-ACP synthase (ACPS)-type in Plasmodium falciparum (PfACPS-PPT), and both SFP and ACPS types in Toxoplasma gondii (TgSFP-PPT and TgACPS-PPT). CpSFP-PPT and TgSFP-PPT are monofunctional, cytosolic, and phylogenetically related to animal PPTases. However, PfACPS-PPT and TgACPS-PPT are bifunctional (fused with a metal-dependent hydrolase), likely targeted to the apicoplast, and more closely related to proteobacterial PPTases. The function of apicomplexan PPTases has been confirmed by detailed functional analysis using recombinant CpSFP-PPT expressed from an artificially synthesized gene with codon usage optimized for Escherichia coli. The recombinant CpSFP-PPT was able to activate the ACP domains from the C. parvum type I FAS in vitro using either CoA or acetyl-CoA as a substrate, or in vivo when coexpressed in bacteria, with kinetic characteristics typical of PPTases. These observations suggest that the two types of fatty acid synthases in the Apicomplexa are activated and regulated by two evolutionarily distinct PPTases.

* Corresponding author. Mailing address: Department of Veterinary Pathobiology, College of Veterinary Medicine, Texas A&M University, 4467 TAMU, College Station, TX 77843-4467. Phone: (979) 845-6981. Fax: (979) 845-9972. E-mail: gzhu{at}cvm.tamu.edu.

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

Eukaryotic Cell, July 2005, p. 1211-1220, Vol. 4, No. 7
1535-9778/05/$08.00+0     doi:10.1128/EC.4.7.1211-1220.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Fritzler, J. M., Millership, J. J., Zhu, G. (2007). Cryptosporidium parvum Long-Chain Fatty Acid Elongase. Eukaryot Cell 6: 2018-2028 [Abstract] [Full Text]  
  • Mazumdar, J., Striepen, B. (2007). Make It or Take It: Fatty Acid Metabolism of Apicomplexan Parasites. Eukaryot Cell 6: 1727-1735 [Full Text]  
  • Zeng, B., Cai, X., Zhu, G. (2006). Functional characterization of a fatty acyl-CoA-binding protein (ACBP) from the apicomplexan Cryptosporidium parvum.. Microbiology 152: 2355-2363 [Abstract] [Full Text]  
  • Rider, S. D. Jr., Cai, X., Sullivan, W. J. Jr., Smith, A. T., Radke, J., White, M., Zhu, G. (2005). The Protozoan Parasite Cryptosporidium parvum Possesses Two Functionally and Evolutionarily Divergent Replication Protein A Large Subunits. J. Biol. Chem. 280: 31460-31469 [Abstract] [Full Text]  


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